Ceramides in Alzheimer’s Disease: Key Mediators of Neuronal Apoptosis Induced by Oxidative Stress and A β Accumulation

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289 · see citing works

Apolipoprotein E and Alzheimer disease: risk, mechanisms and therapy

Liu, C.-C., Kanekiyo, T., Xu, H., & Bu, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.263 · Cited by 3,459 · see citing works

Oxidative Stress and Neurodegenerative Diseases: A Review of Upstream and Downstream Antioxidant Therapeutic Options

Uttara, B., Singh, A., Zamboni, P., & Mahajan, R. (2009) · Current Neuropharmacology · doi:10.2174/157015909787602823 · Cited by 3,378 · see citing works

Reactive oxygen species, cellular redox systems, and apoptosis

Circu, M. L., & Aw, T. Y. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.12.022 · Cited by 3,340 · see citing works

Principles of bioactive lipid signalling: lessons from sphingolipids

Hannun, Y. A., & Obeid, L. M. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2329 · Cited by 3,331 · see citing works

Alzheimer’s disease

Blennow, K., de Leon, M. J., & Zetterberg, H. (2006) · The Lancet · doi:10.1016/s0140-6736(06)69113-7 · Cited by 3,134 · see citing works

Copper toxicity, oxidative stress, and antioxidant nutrients

Gaetke, L. M. (2003) · Toxicology · doi:10.1016/s0300-483x(03)00159-8 · Cited by 2,166 · see citing works

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120 · see citing works

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

Janssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,890 · see citing works

Suppression of ceramide-mediated programmed cell death by sphingosine-1-phosphate

Cuvillier, O., Pirianov, G., Kleuser, B., Vanek, P. G., Coso, O. A., Gutkind, J. S., & Spiegel, S. (1996) · Nature · doi:10.1038/381800a0 · Cited by 1,532 · see citing works

Life and Death of Neurons in the Aging Brain

Morrison, J. H., & Hof, P. R. (1997) · Science · doi:10.1126/science.278.5337.412 · Cited by 1,344 · see citing works

Amyloid Precursor Protein Trafficking, Processing, and Function

Thinakaran, G., & Koo, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800019200 · Cited by 1,141 · see citing works

Involvement of oxidative stress-induced abnormalities in ceramide and cholesterol metabolism in brain aging and Alzheimer's disease

Cutler, R. G., Kelly, J., Storie, K., Pedersen, W. A., Tammara, A., Hatanpaa, K. J., Troncoso, J. C., & Mattson, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305799101 · Cited by 1,135 · see citing works

Consumption of Fish and n-3 Fatty Acids and Risk of Incident Alzheimer Disease

Morris, M. C., Evans, D. A., Bienias, J. L., Tangney, C. C., Bennett, D. A., Wilson, R. S., Aggarwal, N., & Schneider, J. (2003) · Archives of Neurology · doi:10.1001/archneur.60.7.940 · Cited by 1,135 · see citing works

Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo

Fassbender, K. C., Simons, M., Bergmann, C., Stroick, M., Lütjohann, D., Keller, P., Runz, H., Kühl, S., Bertsch, T., von Bergmann, K., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081620098 · Cited by 1,078 · see citing works

Neurodegenerative diseases and oxidative stress

Emerit, J., Edeas, M. A., & Bricaire, F. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2003.11.004 · Cited by 1,031 · see citing works

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · see citing works

Oxidative Stress and the Pathogenesis of Alzheimer's Disease

Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855 · see citing works

The Genetics of Alzheimer Disease: Back to the Future

Bertram, L., Lill, C. M., & Tanzi, R. E. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.013 · Cited by 834 · see citing works

Oxidative Alterations in Alzheimer's Disease

Markesbery, W. R., & Carney, J. M. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00215.x · Cited by 789 · see citing works

Does neuroinflammation fan the flame in neurodegenerative diseases?

Frank-Cannon, T. C., Alto, L. T., McAlpine, F. E., & Tansey, M. G. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-47 · Cited by 751 · see citing works

Evidence that amyloid beta-peptide-induced lipid peroxidation and its sequelae in Alzheimer’s disease brain contribute to neuronal death1

Allanbutterfield, D., Castegna, A., Lauderback, C. M., & Drake, J. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00340-2 · Cited by 715 · see citing works

A Diet Enriched with the Omega-3 Fatty Acid Docosahexaenoic Acid Reduces Amyloid Burden in an Aged Alzheimer Mouse Model

Lim, G. P., Calon, F., Morihara, T., Yang, F., Teter, B., Ubeda, O. J., Salem, N., Frautschy, S. A., & Cole, G. M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4225-04.2005 · Cited by 687 · see citing works

Decoding Alzheimer's disease from perturbed cerebral glucose metabolism: Implications for diagnostic and therapeutic strategies

Chen, Z., & Zhong, C. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.06.004 · Cited by 671 · see citing works

Ceramide activates heterotrimeric protein phosphatase 2A

Dobrowsky, R. T., Kamibayashi, C., Mumby, M. C., & Hannun, Y. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82288-8 · Cited by 666 · see citing works

Substantial sulfatide deficiency and ceramide elevation in very early Alzheimer's disease: potential role in disease pathogenesis

Han, X., M. Holtzman, D., W. McKeel, D., Kelley, J., & Morris, J. C. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00997.x · Cited by 626 · see citing works

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608 · see citing works

Lipid Rafts in the Maintenance of Synapses, Dendritic Spines, and Surface AMPA Receptor Stability

Hering, H., Lin, C.-C., & Sheng, M. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-08-03262.2003 · Cited by 602 · see citing works

Cell death and diseases related to oxidative stress: 4-hydroxynonenal (HNE) in the balance

Dalleau, S., Baradat, M., Guéraud, F., & Huc, L. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2013.138 · Cited by 580 · see citing works

Chemistry and biochemistry of lipid peroxidation products

Guéraud, F., Atalay, M., Bresgen, N., Gašparović, A. Č., Eckl, P., Laurence Therese, H. U. C., Jouanin, I., Siems, W., & Uchida, K. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498477 · Cited by 556 · see citing works

Amyloid β-Peptide Impairs Glucose Transport in Hippocampal and Cortical Neurons: Involvement of Membrane Lipid Peroxidation

Mark, R. J., Pang, Z., Geddes, J. W., Uchida, K., & Mattson, M. P. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-03-01046.1997 · Cited by 551 · see citing works

Amyloid <i>β</i> -Peptide (1–42)-Induced Oxidative Stress in Alzheimer Disease: Importance in Disease Pathogenesis and Progression

Butterfield, D. A., Swomley, A. M., & Sultana, R. (2013) · Antioxidants &amp; Redox Signaling · doi:10.1089/ars.2012.5027 · Cited by 526 · see citing works

Deregulation of sphingolipid metabolism in Alzheimer’s disease

He, X., Huang, Y., Li, B., Gong, C.-X., & Schuchman, E. H. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.05.010 · Cited by 516 · see citing works

The Alzheimer's Aβ peptide induces neurodegeneration and apoptotic cell death in transgenic mice

LaFerla, F. M., Tinkle, B. T., Bieberich, C. J., Haudenschild, C. C., & Jay, G. (1995) · Nature Genetics · doi:10.1038/ng0195-21 · Cited by 513 · see citing works

Exosome reduction in vivo is associated with lower amyloid plaque load in the 5XFAD mouse model of Alzheimer's disease

Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., & Bieberich, E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.012 · Cited by 494 · see citing works

Evidence for Apoptotic Cell Death in Alzheimer's Disease

Smale, G., Nichols, N. R., Brady, D. R., Finch, C. E., & Horton, W. E. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1025 · Cited by 488 · see citing works

β-Amyloid Induces Neuronal Apoptosis Via a Mechanism that Involves the c-Jun N-Terminal Kinase Pathway and the Induction of Fas Ligand

MORISHIMA, Y., Gotoh, Y., Zieg, J., Barrett, T., Takano, H., Flavell, R. A., Davis, R. J., Shirasaki, Y., & Greenberg, M. E. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07551.2001 · Cited by 484 · see citing works

Oxidative stress in Alzheimer disease: A possibility for prevention

Bonda, D., Wang, X., Perry, G. L., Nunomura, A., Tabaton, M., Zhu, X., & Smith, M. A. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.04.005 · Cited by 481 · see citing works

Lipid peroxidation triggers neurodegeneration: A redox proteomics view into the Alzheimer disease brain

Sultana, R., Perluigi, M., & Butterfield, D. A. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.09.027 · Cited by 478 · see citing works

Activation of Akt/PKB, increased phosphorylation of Akt substrates and loss and altered distribution of Akt and PTEN are features of Alzheimer’s disease pathology

Griffin, R. J., Moloney, A., Kelliher, M., Johnston, J. A., Ravid, R., Dockery, P., O'Connor, R., & O'Neill, C. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02949.x · Cited by 459 · see citing works

Trace amounts of copper in water induce β-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease

Sparks, D. L., & Schreurs, B. G. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1832769100 · Cited by 455 · see citing works

Regulation of cholesterol and sphingomyelin metabolism by amyloid-β and presenilin

Grimm, M. O. W., Grimm, H. S., Pätzold, A. J., Zinser, E. G., Halonen, R., Duering, M., Tschäpe, J., Strooper, B. D., Müller, U., Shen, J., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1313 · Cited by 446 · see citing works

Impairment of Glucose and Glutamate Transport and Induction of Mitochondrial Oxidative Stress and Dysfunction in Synaptosomes by Amyloid β‐Peptide: Role of the Lipid Peroxidation Product 4‐Hydroxynonenal

Keller, J. N., Pang, Z., Geddes, J. W., Begley, J. G., Germeyer, A., Waeg, G., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010273.x · Cited by 439 · see citing works

Liver cell death and anemia in Wilson disease involve acid sphingomyelinase and ceramide

Lang, P. A., Schenck, M., Nicolay, J. P., Becker, J. U., Kempe, D. S., Lupescu, A., Koka, S., Eisele, K., Klarl, B. A., Rubben, H., et al. (2007) · Nature Medicine · doi:10.1038/nm1539 · Cited by 438 · see citing works

Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death

Darios, F. D. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg044 · Cited by 401 · see citing works

Ceramide Channels Increase the Permeability of the Mitochondrial Outer Membrane to Small Proteins

Siskind, L. J., Kolesnick, R., & Colombini, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200754200 · Cited by 390 · see citing works

Comparison of Neurodegenerative Pathology in Transgenic Mice Overexpressing V717F β-Amyloid Precursor Protein and Alzheimer’s Disease

Masliah, E., Sisk, A., Mallory, M. E., Mucke, L., Schenk, D., & Games, D. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05795.1996 · Cited by 387 · see citing works

Antioxidants and Free Radical Scavengers for the Treatment Of Stroke, Traumatic Brain Injury and Aging

Weber, J. T., Slemmer, J. E., Shacka, J. J., & Sweeney, M. I. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708783497337 · Cited by 386 · see citing works

FAN, a Novel WD-Repeat Protein, Couples the p55 TNF-Receptor to Neutral Sphingomyelinase

Adam‐Klages, S., Adam, D., Wiegmann, K., Struve, S., Kolanus, W., Schneider‐Mergener, J., & Krönke, M. (1996) · Cell · doi:10.1016/s0092-8674(00)80169-5 · Cited by 381 · see citing works

Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease

Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372 · see citing works

Inhibitors of Brain Phospholipase A2 Activity: Their Neuropharmacological Effects and Therapeutic Importance for the Treatment of Neurologic Disorders

Farooqui, A. A., Ong, W., & Horrocks, L. A. (2006) · Pharmacological Reviews · doi:10.1124/pr.58.3.7 · Cited by 368 · see citing works

Regulation of Phosphorylation of Thr-308 of Akt, Cell Proliferation, and Survival by the B55α Regulatory Subunit Targeting of the Protein Phosphatase 2A Holoenzyme to Akt

Kuo, Y.-C., Huang, K.-Y., Yang, C.-H., Yang, Y.-S., Lee, W.-Y., & Chiang, C.-W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709585200 · Cited by 367 · see citing works

Soluble Aβ oligomer production and toxicity

Larson, M. E., & Lesné, S. E. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07478.x · Cited by 356 · see citing works

Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein

Cordy, J. M., Hussain, I., Dingwall, C., Hooper, N. M., & Turner, A. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1635130100 · Cited by 356 · see citing works

Inhibition of Akt Kinase by Cell-permeable Ceramide and Its Implications for Ceramide-induced Apoptosis

Zhou, H., Summers, S. A., Birnbaum, M. J., & Pittman, R. N. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16568 · Cited by 347 · see citing works

Acid and neutral sphingomyelinases: roles and mechanisms of regulation

Marchesini, N., & Hannun, Y. A. (2004) · Biochemistry and Cell Biology · doi:10.1139/o03-091 · Cited by 342 · see citing works

Ceramide Induces Bcl2 Dephosphorylation via a Mechanism Involving Mitochondrial PP2A

Ruvolo, P. P., Deng, X., Ito, T., Carr, B. K., & May, W. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20296 · Cited by 338 · see citing works

Fibrillar Amyloid-β Peptides Activate Microglia via TLR2: Implications for Alzheimer’s Disease

Jana, M., Palencia, C. A., & Pahan, K. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.10.7254 · Cited by 330 · see citing works

Inhibition of the Neutral Magnesium-dependent Sphingomyelinase by Glutathione

Liu, B., & Hannun, Y. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16281 · Cited by 304 · see citing works

The many “faces” of copper in medicine and treatment

Hordyjewska, A., Popiołek, Ł. P., & Kocot, J. (2014) · BioMetals · doi:10.1007/s10534-014-9736-5 · Cited by 301 · see citing works

Long Chain Ceramides Activate Protein Phosphatase-1 and Protein Phosphatase-2A

Chalfant, C. E., Kishikawa, K., Mumby, M. C., Kamibayashi, C., Bielawska, A. E., & Hannun, Y. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20313 · Cited by 300 · see citing works

Free radicals and brain aging

Poon, H. F., Calabrese, V., Scapagnini, G., & Butterfield, D. A. (2004) · Clinics in Geriatric Medicine · doi:10.1016/j.cger.2004.02.005 · Cited by 292 · see citing works

High fat diet increases hippocampal oxidative stress and cognitive impairment in aged mice: implications for decreased Nrf2 signaling

Morrison, C. D., Pistell, P. J., Ingram, D. K., Johnson, W. D., Liu, Y., Fernandez‐Kim, S. O., White, C. L., Purpera, M. N., Uranga, R. M., Bruce‐Keller, A. J., et al. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06865.x · Cited by 291 · see citing works

Minocycline Attenuates Neuronal Cell Death and Improves Cognitive Impairment in Alzheimer's Disease Models

Choi, Y., Kim, H., Shin, K. Y., Kim, E., Kim, M., Kim, H.-S., Park, C. H., Jeong, Y. H., Yoo, J., Lee, J., et al. (2007) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301377 · Cited by 290 · see citing works

Amyloid-β peptide induces oligodendrocyte death by activating the neutral sphingomyelinase–ceramide pathway

Lee, J.-T., Xu, J., Lee, J.-M., Ku, G., Han, X., Yang, D.-I., Chen, S., & Hsu, C. Y. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307017 · Cited by 280 · see citing works

Roles and regulation of secretory and lysosomal acid sphingomyelinase

Jenkins, R. W., Canals, D., & Hannun, Y. A. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.01.026 · Cited by 276 · see citing works

Roles for dysfunctional sphingolipid metabolism in Alzheimer's disease neuropathogenesis

Haughey, N. J., Bandaru, V. V. R., Bae, M. H., & Mattson, M. P. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.05.003 · Cited by 271 · see citing works

Aβ and Tau Toxicities in Alzheimer's Are Linked via Oxidative Stress-Induced P38 Activation: Protective Role of Vitamin E

Giraldo, E., Lloret, A., Fuchsberger, T., & Viña, J. (2014) · Redox Biology · doi:10.1016/j.redox.2014.03.002 · Cited by 268 · see citing works

Ceramide Induces Cytochrome c Release from Isolated Mitochondria

Ghafourifar, P., Klein, S. D., Schucht, O., Schenk, U., Pruschy, M. N., Rocha, S., & Richter, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6080 · Cited by 266 · see citing works

Increased ceramide in brains with Alzheimer's and other neurodegenerative diseases

Filippov, V., Song, M. A., Zhang, K., Vinters, H. V., Tung, S., Kirsch, W. M., Yang, J., & Duerksen-Hughes, P. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111202 · Cited by 264 · see citing works

Ceramide function in the brain: when a slight tilt is enough

Mencarelli, C., & Martínez‐Martínez, P. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1038-x · Cited by 261 · see citing works

Apoptosis in Alzheimer's disease—an update

Shimohama, S. (2000) · APOPTOSIS · doi:10.1023/a:1009625323388 · Cited by 255 · see citing works

Gene Expression Alterations in the Sphingolipid Metabolism Pathways during Progression of Dementia and Alzheimer’s Disease: A Shift Toward Ceramide Accumulation at the Earliest Recognizable Stages of Alzheimer’s Disease?

Katsel, P., Li, C., & Haroutunian, V. H. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9297-x · Cited by 240 · see citing works

Ceramide and neurodegeneration: Susceptibility of neurons and oligodendrocytes to cell damage and death

Jana, A., Hogan, E. L., & Pahan, K. (2009) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2008.12.010 · Cited by 233 · see citing works

β-Amyloid-Induced Neuronal Apoptosis Involves c-Jun N-Terminal Kinase-Dependent Downregulation of Bcl-w

Yao, M., Nguyen, T. V., & Pike, C. J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4736-04.2005 · Cited by 233 · see citing works

4-Hydroxynonenal in the Pathogenesis and Progression of Human Diseases

Shoeb, M., Ansari, N., Srivastava, S., & Ramana, K. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990181 · Cited by 230 · see citing works

Serum ceramides increase the risk of Alzheimer disease

Mielke, M. M., Bandaru, V. V. R., Haughey, N. J., Xia, J., Fried, L. P., Yaşar, S., Albert, M., Varma, V. R., Harris, G., Schneider, E. B., et al. (2012) · Neurology · doi:10.1212/wnl.0b013e318264e380 · Cited by 223 · see citing works

Dietary fat composition and dementia risk

Morris, M. C., & Tangney, C. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.03.038 · Cited by 222 · see citing works

Spatial Segregation of γ-Secretase and Substrates in DistinctMembraneDomains

Vetrivel, K. S., Cheng, H., Kim, S.-H., Chen, Y., Barnes, N. Y., Parent, A., Sisodia, S. S., & Thinakaran, G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503570200 · Cited by 220 · see citing works

Alzheimer´s Disease and Oxidative Stress: A Review

Pohanka, M. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113206660258 · Cited by 219 · see citing works

The release of calcium from the endoplasmic reticulum induced by amyloid-beta and prion peptides activates the mitochondrial apoptotic pathway

Ferreiro, E. B., Oliveira, C. R., & Pereira, C. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.02.003 · Cited by 219 · see citing works

Lipid Rafts: Linking Alzheimer′s Amyloid‐βProduction, Aggregation, and Toxicity at Neuronal Membranes

Rushworth, J. V., & Hooper, N. M. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/603052 · Cited by 218 · see citing works

Soluble oligomers of amyloid-β peptide induce neuronal apoptosis by activating a cPLA2-dependent sphingomyelinase-ceramide pathway

Malaplate, C., Florent‐Béchard, S., Youssef, I., Koziel, V., Sponne, I., Kriem, B., Leininger‐Muller, B., Olivier, J. L., Oster, T., & Pillot, T. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.02.010 · Cited by 213 · see citing works

Direct interaction between the inhibitor 2 and ceramide via sphingolipid‐protein binding is involved in the regulation of protein phosphatase 2A activity and signaling

Mukhopadhyay, A., Saddoughi, S. A., Song, P., Sultan, I. Y., Ponnusamy, S., Senkal, C. E., Snook, C. F., Arnold, H., Sears, R. C., Hanniui, Y. A., et al. (2008) · The FASEB Journal · doi:10.1096/fj.08-120550 · Cited by 208 · see citing works

Decreased thioredoxin and increased thioredoxin reductase levels in alzheimer’s disease brain

Lovell, M. A., Xie, C., Gabbita, S. P., & Markesbery, W. R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00258-0 · Cited by 202 · see citing works

JNK pathway: diseases and therapeutic potential

Cui, J., Zhang, M., Zhang, Y., & Xu, Z. (2007) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2007.00579.x · Cited by 202 · see citing works

Inhibition of PKB/Akt1 by C2-Ceramide Involves Activation of Ceramide-Activated Protein Phosphatase in PC12 Cells

Salinas, M., López‐Valdaliso, R., Martı́n, D., Alvarez, A. M., & Cuadrado, A. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0813 · Cited by 199 · see citing works

Changes in mitochondrial membrane potential during oxidative stress-induced apoptosis in PC12 cells

Satoh, T., Enokido, Y., Aoshima, H., Uchiyama, Y., & Hatanaka, H. (1997) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19971101)50:3 · Cited by 196 · see citing works

Emotional and Behavioral Symptoms in Neurodegenerative Disease: A Model for Studying the Neural Bases of Psychopathology

LEVENSON, R. W., Sturm, V. E., & Haase, C. M. (2014) · Annual Review of Clinical Psychology · doi:10.1146/annurev-clinpsy-032813-153653 · Cited by 193 · see citing works

The role of inflammasome in Alzheimer's disease

Liu, L., & Chan, C. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2013.12.007 · Cited by 192 · see citing works

Sphingolipid Metabolic Pathway: An Overview of Major Roles Played in Human Diseases

Rao, R. P., Vaidyanathan, N., Rengasamy, M., Oommen, A. M., Somaiya, N., & Jagannath, M. R. (2013) · Journal of Lipids · doi:10.1155/2013/178910 · Cited by 192 · see citing works

Serum sphingomyelins and ceramides are early predictors of memory impairment

Mielke, M. M., Bandaru, V. V. R., Haughey, N. J., Rabins, P. V., Lyketsos, C. G., & Carlson, M. C. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.03.011 · Cited by 188 · see citing works

Fibrillar Amyloid-β Peptides Kill Human Primary Neurons via NADPH Oxidase-mediated Activation of Neutral Sphingomyelinase

Jana, A., & Pahan, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404635200 · Cited by 184 · see citing works

Amyloid Beta: Multiple Mechanisms of Toxicity and Only Some Protective Effects?

Carrillo‐Mora, P., Luna, R., & Colín-Barenque, L. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/795375 · Cited by 184 · see citing works

Mitochondrial Free Radical Signal in Ceramide‐Dependent Apoptosis: A Putative Mechanism for Neuronal Death in Parkinson's Disease

France‐Lanord, V., Brugg, B., Michel, P. P., Agid, Y., & Ruberg, M. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69041612.x · Cited by 182 · see citing works

Cholesterol Level and Statin Use in Alzheimer Disease

Shepardson, N. E. (2011) · Archives of Neurology · doi:10.1001/archneurol.2011.242 · Cited by 181 · see citing works

DHA Improves Cognition and Prevents Dysfunction of Entorhinal Cortex Neurons in 3xTg-AD Mice

Arsenault, D., Julien, C., Tremblay, C., & Calon, F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017397 · Cited by 177 · see citing works

Altered mitochondria, energy metabolism, voltage-dependent anion channel, and lipid rafts converge to exhaust neurons in Alzheimer’s disease

Ferrer, I. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9243-5 · Cited by 172 · see citing works

Ceramide and Reactive Oxygen Species Generated by H2O2 Induce Caspase-3-independent Degradation of Akt/Protein Kinase B

Martı́n, D., Salinas, M., Fujita, N., Tsuruo, T., & Cuadrado, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201070200 · Cited by 168 · see citing works

Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER

Vacaru, A. M., Tafesse, F., Ternes, P., Kondylis, V., Hermansson, M., Brouwers, J. F. H. M., Somerharju, P. J., Rabouille, C., & Holthuis, J. C. M. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903152 · Cited by 168 · see citing works

Chronic copper exposure exacerbates both amyloid and tau pathology and selectively dysregulates cdk5 in a mouse model of AD

Kitazawa, M., Cheng, D., & LaFerla, F. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05901.x · Cited by 165 · see citing works

Altered lipid composition in cortical lipid rafts occurs at early stages of sporadic Alzheimer's disease and facilitates APP/BACE1 interactions

Fabelo, N., Martín, M. V., Marín, R., Moreno, D., Ferrer, I., & Díaz, M. L. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.005 · Cited by 164 · see citing works

Ceramide-induced neuronal apoptosis is associated with dephosphorylation of Akt, BAD, FKHR, GSK-3β, and induction of the mitochondrial-dependent intrinsic caspase pathway

Stoica, B. A., Movsesyan, V. A., Lea, P. M., & Faden, A. I. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(02)00028-3 · Cited by 160 · see citing works

Plasma Sphingomyelins are Associated with Cognitive Progression in Alzheimer's Disease

Mielke, M. M., Haughey, N. J., Bandaru, V. V. R., Weinberg, D. D., Darby, E. J., Zaidi, N., Pavlik, V., Doody, R. S., & Lyketsos, C. G. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110405 · Cited by 158 · see citing works

4-Hydroxy-2-Nonenal Pyrrole Adducts in Human Neurodegenerative Disease

Montine, K. S., KIM, P. J., Olson, S. J., Markesbery, W. R., & Montine, T. J. (1997) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199708000-00004 · Cited by 158 · see citing works

Oxidative Stress and Cell Membranes in the Pathogenesis of Alzheimer's Disease

Axelsen, P. H., Komatsu, H., & Murray, I. V. J. (2011) · Physiology · doi:10.1152/physiol.00024.2010 · Cited by 158 · see citing works

Ceramide and the mitochondrial respiratory chain

Kogot‐Levin, A., & Saada, A. (2013) · Biochimie · doi:10.1016/j.biochi.2013.07.027 · Cited by 156 · see citing works

Hepatic Ceramide May Mediate Brain Insulin Resistance and Neurodegeneration in Type 2 Diabetes and Non-alcoholic Steatohepatitis

Lyn‐Cook, L. E., Lawton, M., Tong, M., Silbermann, E., Longato, L., Jiao, P., Mark, P., Wands, J. R., Xu, H., & de la Monte, S. M. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0984 · Cited by 149 · see citing works

A TrkA-to-p75NTR molecular switch activates amyloid β-peptide generation during aging

Costantini, C., Weindruch, R. H., Valle, G. D., & Puglielli, L. (2005) · Biochemical Journal · doi:10.1042/bj20050700 · Cited by 148 · see citing works

Oxidative Stress and Metabolic Syndrome: Cause or Consequence of Alzheimer's Disease?

Contreras, D. L., Carvajal, K., Toral-Ríos, D., Franco-Bocanegra, D., & Campos‐Peña, V. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/497802 · Cited by 148 · see citing works

Personality changes in Alzheimer's disease: a systematic review

Wahlin, T. R., & Byrne, G. J. (2010) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.2655 · Cited by 147 · see citing works

Alterations of the Sphingolipid Pathway in Alzheimer’s Disease: New Biomarkers and Treatment Targets?

Mielke, M. M., & Lyketsos, C. G. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8121-y · Cited by 141 · see citing works

GSK-3β acts downstream of PP2A and the PI 3-kinase-Akt pathway, and upstream of caspase-2 in ceramide-induced mitochondrial apoptosis

Lin, C., Chen, C., Chiang, C.-W., Jan, M., Huang, W., & Lin, Y.-S. (2007) · Journal of Cell Science · doi:10.1242/jcs.03473 · Cited by 141 · see citing works

The structural requirements for ceramide activation of serine-threonine protein phosphatases

Chalfant, C. E., Szulc, Z. M., Roddy, P. L., Bielawska, A. E., & Hannun, Y. A. (2004) · Journal of Lipid Research · doi:10.1194/jlr.m300347-jlr200 · Cited by 141 · see citing works

Ceramide channels and their role in mitochondria-mediated apoptosis

Colombini, M. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.01.021 · Cited by 139 · see citing works

Lipid Integration in Neurodegeneration: An Overview of Alzheimer’s Disease

Yadav, R. S., & Tiwari, N. K. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8661-5 · Cited by 134 · see citing works

Dietary fatty acids intake: possible role in cognitive decline and dementia

Solfrizzi, V., D’Introno, A., Colacicco, A. M., Capurso, C. A., DelParigi, A., Capurso, S. A., Gadaleta, A., Capurso, A., & Panza, F. (2005) · Experimental Gerontology · doi:10.1016/j.exger.2005.01.001 · Cited by 132 · see citing works

The Role of the Ceramide Acyl Chain Length in Neurodegeneration: Involvement of Ceramide Synthases

Ben‐David, O., & Futerman, A. H. (2010) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8114-x · Cited by 130 · see citing works

Impaired brain glucose metabolism leads to Alzheimer neurofibrillary degeneration through a decrease in tau O-GlcNAcylation

Gong, C., Liu, F., Grundke-Iqbal, I., & Iqbal, K. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9101 · Cited by 128 · see citing works

Ceramide‐induced apoptosis in cortical neurons is mediated by an increase in p38 phosphorylation and not by the decrease in ERK phosphorylation

Willaime‐Morawek, S., Vanhoutte, P., Caboche, J., Lemaigre‐Dubreuil, Y., Mariani, J., & Brugg, B. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01581.x · Cited by 127 · see citing works

Involvement of astroglial ceramide in palmitic acid‐induced Alzheimer‐like changes in primary neurons

Patil, S. P., Melrose, J., & Chan, C. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05797.x · Cited by 126 · see citing works

Sphingosine-1-phosphate: the Swiss army knife of sphingolipid signaling

Maceyka, M. W., Milstien, S., & Spiegel, S. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800065-jlr200 · Cited by 124 · see citing works

Inhibition of Glycosphingolipid Biosynthesis Reduces Secretion of the β-Amyloid Precursor Protein and Amyloid β-Peptide*[boxs]

Tamboli, I. Y., Prager, K., Barth, E., Heneka, M. T., Sandhoff, K., & Walter, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414525200 · Cited by 122 · see citing works

Immunohistochemical investigation of the brain of aged dogs. I. Detection of neurofibrillary tangles and of 4-hydroxynonenal protein, an oxidative damage product, in senile plaques

Papaioannou, N. G., Tooten, P. C. J., van Ederen, A. M., Böhl, J., Rofina, J., Tsangaris, T., & Gruys, E. (2001) · Amyloid · doi:10.3109/13506120108993810 · Cited by 121 · see citing works

Phosphoprotein Phosphatase 2A: A Novel Druggable Target for Alzheimer’s Disease

Voronkov, M. V., Braithwaite, S. P., & Stock, J. B. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.47 · Cited by 121 · see citing works

The case for soluble Aβ oligomers as a drug target in Alzheimer's disease

Hefti, F. F., Goure, W. F., Jerecı̀ć, J., Iverson, K. S., Walicke, P. A., & Krafft, G. A. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.03.002 · Cited by 119 · see citing works

The Magnitude of Brain Lipid Peroxidation Correlates with the Extent of Degeneration but Not with Density of Neuritic Plaques or Neurofibrillary Tangles or with APOE Genotype in Alzheimer's Disease Patients

Montine, T. J., Markesbery, W. R., Zackert, W. E., Sanchez, S. C., Roberts, L. J., & Morrow, J. D. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65185-1 · Cited by 116 · see citing works

Purification and Characterization of a Membrane Bound Neutral pH Optimum Magnesium-dependent and Phosphatidylserine-stimulated Sphingomyelinase from Rat Brain

Liu, B., Hassler, D. F., Smith, G. K., Weaver, K. L., & Hannun, Y. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.51.34472 · Cited by 115 · see citing works

Clinical utility of copper, ceruloplasmin, and metallothionein plasma determinations in human neurodegenerative patients and their first-degree relatives

Arnal, N., Cristalli, D. O., de Alaniz, M. J. T., & Marra, C. A. (2009) · Brain Research · doi:10.1016/j.brainres.2009.11.085 · Cited by 113 · see citing works

Ceramidase Regulates Synaptic Vesicle Exocytosis and Trafficking

Rohrbough, J. C., Rushton, E., Musselman, L. P., Woodruff, E. A., Matthies, H. J. G., Acharya, U. R., Acharya, J., & Broadie, K. S. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.1146-04.2004 · Cited by 104 · see citing works

Elevated cerebrospinal fluid sphingomyelin levels in prodromal Alzheimer's disease

Košiček, M., Zetterberg, H., Andreasen, N., Peter‐Katalinić, J., & Hecimovic, S. K. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.04.019 · Cited by 102 · see citing works

Diet‐induced elevations in serum cholesterol are associated with alterations in hippocampal lipid metabolism and increased oxidative stress

Stranahan, A. M., Cutler, R. G., Button, C., Telljohann, R., & Mattson, M. P. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07351.x · Cited by 100 · see citing works

Ceramide induces neuronal apoptosis through the caspase-9/caspase-3 pathway

Movsesyan, V. A., Yakovlev, A. G., Dabaghyan, E. A., Stoica, B. A., & Faden, A. I. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02593-7 · Cited by 99 · see citing works

Asiatic acid protects primary neurons against C2-ceramide-induced apoptosis

Zhang, X., Wu, J., Dou, Y., Xia, B., Rong, W., Rimbach, G., & Lou, Y. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.01.006 · Cited by 99 · see citing works

N‐Acetyl‐ l ‐cysteine protects SHSY5Y neuroblastoma cells from oxidative stress and cell cytotoxicity: effects on β‐amyloid secretion and tau phosphorylation

Olivieri, G., Baysang, G., Meier, F., Müller-Spahn, F., Stähelin, H. B., Brockhaus, M., & Brack, C. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00090.x · Cited by 98 · see citing works

Ceramide induces neuronal apoptosis through mitogen-activated protein kinases and causes release of multiple mitochondrial proteins

Stoica, B. A., Movsesyan, V. A., Knoblach, S. M., & Faden, A. I. (2005) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2005.02.009 · Cited by 98 · see citing works

Protective effects of S-nitrosoglutathione against amyloid β-peptide neurotoxicity

Ju, T., Chen, S., Liu, C.-C., & Yang, D. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.019 · Cited by 96 · see citing works

Opposite regulation of the mitochondrial apoptotic pathway by C2‐ceramide and PACAP through a MAP‐kinase‐dependent mechanism in cerebellar granule cells

Falluel‐Morel, A., Aubert, N., Vaudry, D., Basille, M., Fontaine, M., Fournier, A., Vaudry, H., & Gonzalez, B. J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02810.x · Cited by 95 · see citing works

Palmitic acid-treated astrocytes induce BACE1 upregulation and accumulation of C-terminal fragment of APP in primary cortical neurons

Patil, S. P., Sheng, L., Masserang, A., & Chan, C. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.07.015 · Cited by 93 · see citing works

Expression of apoptosis related proteins in brains of patients with Alzheimer's disease

Engidawork, E., Gulesserian, T., Seidl, R., Cairns, N., & Lubec, G. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01618-4 · Cited by 91 · see citing works

Ceramide in the Molecular Mechanisms of Neuronal Cell Death. The Role of Sphingosine-1-Phosphate

Czubowicz, K., & Strosznajder, R. P. (2014) · Molecular Neurobiology · doi:10.1007/s12035-013-8606-4 · Cited by 89 · see citing works

Dietary fats, cerebrovasculature integrity and Alzheimer’s disease risk

Takechi, R., Galloway, S., Pallebage‐Gamarallage, M. M., Lam, V., & Mamo, J. C. L. (2009) · Progress in Lipid Research · doi:10.1016/j.plipres.2009.10.004 · Cited by 88 · see citing works

Connection of lipid peroxide oxidation with the sphingomyelin pathway in the development of Alzheimer's disease

Alessenko, A. V., Бугрова, А. Е., & Дудник, Л. Б. (2004) · Biochemical Society Transactions · doi:10.1042/bst0320144 · Cited by 88 · see citing works

Intersection between metabolic dysfunction, high fat diet consumption, and brain aging

Uranga, R. M., Bruce‐Keller, A. J., Morrison, C. D., Fernandez‐Kim, S. O., Ebenezer, P. J., Zhang, L., Dasuri, K., & Keller, J. N. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06803.x · Cited by 87 · see citing works

Morphological and biochemical assessment of DNA damage and apoptosis in Down syndrome and Alzheimer disease, and effect of postmortem tissue archival on TUNEL

Anderson, A. J., Stoltzner, S., Lai, F., Su, J. H., & Nixon, R. A. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00126-3 · Cited by 87 · see citing works

Amyloid‐β peptide enhances tumor necrosis factor‐α‐induced iNOS through neutral sphingomyelinase/ceramide pathway in oligodendrocytes

Zeng, C., Lee, J. T., Chen, H., Chen, S., Hsu, C. Y., & Xu, J. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03217.x · Cited by 80 · see citing works

Neutral sphingomyelinases and nSMase2: Bridging the gaps

Clarke, C. J., & Hannun, Y. A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.06.025 · Cited by 80 · see citing works

Sphingolipid and Ceramide Homeostasis: Potential Therapeutic Targets

Young, S. A., Mina, J. G., Denny, P. W., & Smith, T. (2012) · Biochemistry Research International · doi:10.1155/2012/248135 · Cited by 77 · see citing works

Nutrient intake and plasma β-amyloid

Gu, Y., Schupf, N., Cosentino, S., Luchsinger, J. A., & Scarmeas, N. (2012) · Neurology · doi:10.1212/wnl.0b013e318258f7c2 · Cited by 77 · see citing works

Cross-talk of membrane lipids and Alzheimer-related proteins

Walter, J., & van Echten‐Deckert, G. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-34 · Cited by 77 · see citing works

Biophysical Alterations in Lipid Rafts from Human Cerebral Cortex Associate with Increased BACE1/AβPP Interaction in Early Stages of Alzheimer's Disease

Díaz, M. L., Fabelo, N., Martín, M. V., Ferrer, I., Gómez, T., & Marín, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-141146 · Cited by 75 · see citing works

Palmitate-activated astrocytes via serine palmitoyltransferase increase BACE1 in primary neurons by sphingomyelinases

Liu, L., Martin, R., & Chan, C. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.05.017 · Cited by 72 · see citing works

Aβ1–42 modulation of Akt phosphorylation via α7 nAChR and NMDA receptors

Abbott, J. J., Howlett, D. R., Francis, P. T., & Williams, R. J. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.01.003 · Cited by 71 · see citing works

C-jun N-terminal kinases/c-Jun and p38 pathways cooperate in ceramide-induced neuronal apoptosis

Willaime‐Morawek, S., Brami‐Cherrier, K., Mariani, J., Caboche, J., & Brugg, B. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00996-x · Cited by 71 · see citing works

Ceramide‐induced cell death in primary neuronal cultures: Upregulation of ceramide levels during neuronal apoptosis

Toman, R. E., Movsesyan, V. A., Murthy, S. K., Milstien, S., Spiegel, S., & Faden, A. I. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10190 · Cited by 70 · see citing works

Ceramides and sphingomyelinases in senile plaques

Panchal, M., Gaudin, M., Lazar, A. N., Salvati, E., Rivals, I., Ayciriex, S., Dauphinot, L., Dargère, D., Auzeil, N., Masserini, M., et al. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.01.010 · Cited by 68 · see citing works

The 5XFAD Mouse Model of Alzheimer’s Disease Exhibits an Age-Dependent Increase in Anti-Ceramide IgG and Exogenous Administration of Ceramide Further Increases Anti-Ceramide Titers and Amyloid Plaque Burden

Dinkins, M. B., Dasgupta, S., Wang, G., Zhu, G., He, Q., Kong, J. N., & Bieberich, E. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150088 · Cited by 68 · see citing works

Protection of Flupirtine on β‐Amyloid‐Induced Apoptosis in Neuronal Cells In Vitro: Prevention of Amyloid‐Induced Glutathione Depletion

Müller, W. E. G., Romero, F. J., Perovic, S., Pergande, G., & Pialoglou, P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68062371.x · Cited by 67 · see citing works

Ceramide increases mitochondrial free calcium levels via caspase 8 and Bid: role in initiation of cell death

Darios, F. D., Lambeng, N., Troadec, J., Michel, P. P., & Ruberg, M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01590.x · Cited by 64 · see citing works

Involvement of sphingomyelinases in TNF signaling pathways

Krönke, M. (1999) · Chemistry and Physics of Lipids · doi:10.1016/s0009-3084(99)00084-5 · Cited by 64 · see citing works

Oxidative Stress and Amyloid Beta Toxicity in Alzheimer’s Disease: Intervention in a Complex Relationship by Antioxidants

Chakrabarti, S., Sinha, M., Thakurta, I. G., Banerjee, P., & Chattopadhyay, M. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990152 · Cited by 63 · see citing works

Ceramide and mitochondria in ischemic brain injury.

Novgorodov, S. A., & Gudz, T. I. (2011) · Europe PMC (PubMed Central) · Cited by 62 · see citing works

Potential protection of curcumin against intracellular amyloid β-induced toxicity in cultured rat prefrontal cortical neurons

Qin, X., Cheng, Y., & Yu, L. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.05.062 · Cited by 62 · see citing works

Possible involvement of cytochrome c release and sequential activation of caspases in ceramide-induced apoptosis in SK-N-MC cells

Ito, A., Uehara, T., Tokumitsu, A., Okuma, Y., & Nomura, Y. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00131-7 · Cited by 61 · see citing works

Protective effects of S-nitrosoglutathione against amyloid beta-peptide neurotoxicity

Jü, Chert, Sd, Liu, Yang, Y., & Di (2006) · 中国生物学文摘 · Cited by 60 · see citing works

Accumulation of Exogenous Amyloid- Beta Peptide in Hippocampal Mitochondria Causes Their Dysfunction: A Protective Role for Melatonin

Rosales‐Corral, S., Acuña-Castroviejo, D., Tan, D. X., López-Armas, G. D. C., Cruz-Ramos, J. A., Munoz, R., Melnikov, V., Manchester, L. C., & Reiter, R. J. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/843649 · Cited by 59 · see citing works

Anti-apoptotic and anti-oxidative mechanisms of minocycline against sphingomyelinase/ceramide neurotoxicity: implication in Alzheimer's disease and cerebral ischemia

Chen, S., Yin, J., Hwang, C., Tang, C.-M., & Yang, D. (2012) · Free Radical Research · doi:10.3109/10715762.2012.674640 · Cited by 59 · see citing works

Critical Role for Sphingosine Kinase-1 in Regulating Survival of Neuroblastoma Cells Exposed to Amyloid-β Peptide

Gomez‐Brouchet, A., Pchejetski, D., Brizuela, L., Garcia, V., Altié, M.-F., Maddelein, M., Delisle, M., & Cuvillier, O. (2007) · Molecular Pharmacology · doi:10.1124/mol.106.033738 · Cited by 59 · see citing works

Role of glutathione in intracellular amyloid‐α precursor protein/carboxy‐terminal fragment aggregation and associated cytotoxicity

Woltjer, R. L., Nghiem, W., Maezawa, I., Milatović, D., Vaisar, T., Montine, K. S., & Montine, T. J. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03109.x · Cited by 58 · see citing works

Lithium Inhibits Ceramide- and Etoposide-Induced Protein Phosphatase 2A Methylation, Bcl-2 Dephosphorylation, Caspase-2 Activation, and Apoptosis

Chen, C., Lin, C., Chiang, C.-W., Jan, M., & Lin, Y.-S. (2006) · Molecular Pharmacology · doi:10.1124/mol.106.024059 · Cited by 58 · see citing works

Could plasma sphingolipids be diagnostic or prognostic biomarkers for Alzheimer’s disease?

Mielke, M. M., & Haughey, N. J. (2012) · Clinical Lipidology · doi:10.2217/clp.12.59 · Cited by 56 · see citing works

Neutral sphingomyelinase activation precedes NADPH oxidase‐dependent damage in neurons exposed to the proinflammatory cytokine tumor necrosis factor‐α

Barth, B. M., Gustafson, S. J., & Kuhn, T. B. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22748 · Cited by 53 · see citing works

Dementia, Diabetes, Alzheimer's Disease, and Insulin Resistance in the Brain: Progress, Dilemmas, New Opportunities, and a Hypothesis to Tackle Intersecting Epidemics

Kuljiš, R. O., & Šalković‐Petrišić, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101392 · Cited by 52 · see citing works

Inhibition of serine palmitoyltransferase reduces Aβ and tau hyperphosphorylation in a murine model: a safe therapeutic strategy for Alzheimer's disease

Geekiyanage, H., Upadhye, A., & Chan, C. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.02.001 · Cited by 51 · see citing works

Inhibition of sphingomyelinase activity helps to prevent neuron death caused by ischemic stress

SOEDA, S. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2004.04.001 · Cited by 48 · see citing works

Mitochondrial free calcium levels (Rhod-2 fluorescence) and ultrastructural alterations in neuronally differentiated PC12 cells during ceramide-dependent cell death

Muriel, M., Lambeng, N., Darios, F. D., Michel, P. P., Hirsch, É. C., Agid, Y., & Ruberg, M. (2000) · The Journal of Comparative Neurology · doi:10.1002/1096-9861(20001016)426:2 · Cited by 46 · see citing works

Rapid cognitive decline in Alzheimer's disease: a literature review

Sona, A., Ellis, K. A., & Ames, D. J. (2013) · International Review of Psychiatry · doi:10.3109/09540261.2013.859128 · Cited by 45 · see citing works

Tumor Necrosis Factor-α Induces Apoptosis in Immortalized Hypothalamic Neurons: Involvement of Ceramide-Generating Pathways

Sortino, M. A., Condorelli, F., Vancheri, C., & Canonico, P. L. (1999) · Endocrinology · doi:10.1210/endo.140.10.7062 · Cited by 45 · see citing works

Erythropoietin prevents PC12 cells from beta-amyloid-induced apoptosis via PI3K⁄Akt pathway

Sun, Z., Yang, H., Wang, Z., Jing, P., Zhen, H., & Sheng-Di, C. (2012) · Translational Neurodegeneration · doi:10.1186/2047-9158-1-7 · Cited by 42 · see citing works

Mechanisms of apoptosis in PC12 cells irreversibly differentiated with nerve growth factor and cyclic AMP

Lambeng, N., Michel, P. P., Brugg, B., Agid, Y., & Ruberg, M. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01061-6 · Cited by 40 · see citing works

Age-related changes in neutral sphingomyelin-specific phospholipase C activity in striatum, hippocampus, and frontal cortex: Implication for sensitivity to stress and inflammation

Crivello, N. A., Rosenberg, I. H., Dallal, G. E., Bielinski, D. F., & Joseph, J. A. (2005) · Neurochemistry International · doi:10.1016/j.neuint.2005.06.011 · Cited by 40 · see citing works

PKB/Akt inhibits ceramide‐induced apoptosis in neuroblastoma cells by blocking apoptosis‐inducing factor (AIF) translocation

Kim, N. H., Kim, K., Park, W. S., Son, H. S., & Bae, Y. M. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21344 · Cited by 39 · see citing works

Different protection of K252a and N‐acetyl‐ L ‐cysteine against amyloid‐β peptide–induced cortical neuron apoptosis involving inhibition of MLK3–MKK7–JNK3 signal cascades

Xu, Y., Hou, X., Liu, Y. U., & Zong, Y. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21909 · Cited by 39 · see citing works

Synthetic ceramide analogues increase amyloid-β 42 production by modulating γ-secretase activity

Takasugi, N., Sasaki, T., Shinohara, M., Iwatsubo, T., & Tomita, T. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.12.087 · Cited by 37 · see citing works

Tanshinone IIA protects PC12 cells from β-amyloid25–35-induced apoptosis via PI3K/Akt signaling pathway

Dong, H., Mao, S., Wei, J., Liu, B., Zhang, Z., Zhang, Q., & Yan, M. (2012) · Molecular Biology Reports · doi:10.1007/s11033-012-1477-3 · Cited by 35 · see citing works

Amyloid beta peptide increases DP5 expression via activation of neutral sphingomyelinase and JNK in oligodendrocytes

Chen, S., Lee, J., Zeng, C., Chen, H., Hsu, C. Y., & Xu, J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03774.x · Cited by 34 · see citing works

Effects of copper overload in P19 neurons: impairment of glutathione redox homeostasis and crosstalk between caspase and calpain protease systems in ROS-induced apoptosis

Jembrek, M. J., Vlainić, J., Radovanović, V., Erhardt, J., & Oršolić, N. (2014) · BioMetals · doi:10.1007/s10534-014-9792-x · Cited by 32 · see citing works

Ceramide elevates 12-hydroxyeicosatetraenoic acid levels and upregulates 12-lipoxygenase in rat primary hippocampal cell cultures containing predominantly astrocytes

Prasad, V. V. T. S., Nithipatikom, K., & Harder, D. R. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.07.002 · Cited by 30 · see citing works

Mitochondria morphology and DNA content upon sublethal exposure to beta-amyloid(1-42) peptide.

Diana, A., Šimić, G., Sinforiani, E., Orrù, N., Pichiri, G., & Bono, G. G. (2008) · PubMed · Cited by 28 · see citing works

Hyperphosphorylation of tau by GSK-3β in Alzheimer’s disease: The interaction of Aβ and sphingolipid mediators as a therapeutic target

Jembrek, M. J., Leko, M. B., Pivac, N., Hof, P. R., & Šimić, G. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0144-z · Cited by 25 · see citing works

Neutral sphingomyelinase-2 is a redox sensitive enzyme: role of catalytic cysteine residues in regulation of enzymatic activity through changes in oligomeric state

Dotson, P. P., Karakashian, A., & Nikolova‐Karakashian, M. (2014) · Biochemical Journal · doi:10.1042/bj20140665 · Cited by 23 · see citing works

Modulation of amyloid precursor protein processing by synthetic ceramide analogues

Li, H., Kim, W. S., Guillemin, G. J., Hill, A. F., Evin, G. M., & Garner, B. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2010.05.012 · Cited by 20 · see citing works

PTEN: A molecular target for neurodegenerative disorders

Ismail, A., Ning, K., Al‐Hayani, A., Sharrack, B., & Azzouz, M. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0018-9 · Cited by 19 · see citing works

Cytoskeletal changes as an alternative view on pathogenesis of Alzheimer's disease

Šimić, G., Gnjidić, M., & Kostović, I. (1998) · Periodicum Biologorum · Cited by 19 · see citing works

Neuroprotective mechanisms of minocycline against sphingomyelinase/ceramide toxicity: Roles of Bcl-2 and thioredoxin

Tang, C.-M., Hwang, C., Chen, S., & Yang, D. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.024 · Cited by 16 · see citing works

Volume and number of neurons of the human hippocampal formation in normal aging and Alzheimer’s disease

?imi?, G., Kostovi?, I., Winblad, B., & Bogdanovi?, N. (1997) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19970324)379:4

Regulation of apoptosis in health and disease: the balancing act of BCL-2 family proteins

Singh, R., Letai, A., & Sarosiek, K. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0089-8 · Cited by 2,111 · see citing works

NOX4 promotes ferroptosis of astrocytes by oxidative stress-induced lipid peroxidation via the impairment of mitochondrial metabolism in Alzheimer’s diseases

Park, M. W., Cha, H. W., Kim, J., Kim, J. H., Yang, H., Yoon, S., Boonpraman, N., Yi, S. S., Yoo, I. D., & Moon, J.-S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101947 · Cited by 683 · see citing works

Activation of microglia and astrocytes: a roadway to neuroinflammation and Alzheimer’s disease

Kaur, D., Sharma, V., & Deshmukh, R. R. (2019) · Inflammopharmacology · doi:10.1007/s10787-019-00580-x · Cited by 493 · see citing works

Lipids and Alzheimer’s Disease

Kao, Y.-C., Ho, P.-C., Tu, Y.-K., Jou, I.-M., & Tsai, K.-J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041505 · Cited by 485 · see citing works

Brain and blood metabolite signatures of pathology and progression in Alzheimer disease: A targeted metabolomics study

Varma, V. R., Oommen, A. M., Varma, S., Casanova, R., An, Y., Andrews, R. M., O’Brien, R., Pletniková, O., Troncoso, J. C., Toledo, J. B., et al. (2018) · PLoS Medicine · doi:10.1371/journal.pmed.1002482 · Cited by 464 · see citing works

Lipid metabolism and Alzheimer's disease: clinical evidence, mechanistic link and therapeutic promise

Yin, F. (2023) · The FEBS Journal · doi:10.1111/febs.16344 · Cited by 441 · see citing works

The Role of Ceramide and Sphingosine-1-Phosphate in Alzheimer’s Disease and Other Neurodegenerative Disorders

Czubowicz, K., Jęśko, H. M., Wencel, P. L., Lukiw, W. J., & Strosznajder, R. P. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1448-3 · Cited by 296 · see citing works

The brain as an insulin-sensitive metabolic organ

Milstein, J. L., & Ferris, H. A. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101234 · Cited by 269 · see citing works

Insulin Resistance and Oxidative Stress in the Brain: What’s New?

Maciejczyk, M., Żebrowska, E., & Chabowski, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20040874 · Cited by 262 · see citing works

The Role of Lipids in Parkinson’s Disease

Xicoy, H., Wieringa, B., & Martens, G. J. M. (2019) · Cells · doi:10.3390/cells8010027 · Cited by 255 · see citing works

Altered glucose metabolism in Alzheimer's disease: Role of mitochondrial dysfunction and oxidative stress

Dewanjee, S., Chakraborty, P., Bhattacharya, H., Chacko, L., Singh, B., Chaudhary, A., Javvaji, K., Pradhan, S. R., Vallamkondu, J., Dey, A., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.09.032 · Cited by 235 · see citing works

The mTOR/GCLc/GSH Pathway Mediates the Dose-Dependent Bidirectional Regulation of ROS Induced by TiO2NPs in Neurogenic Cells

Mao, Z., Li, S., Zhang, L., Yao, M., Zhou, Z., & Chen, M. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/7621561 · Cited by 217 · see citing works

Apoptotic Pathways and Alzheimer’s Disease: Probing Therapeutic Potential

Sharma, V., Singh, T. G., Singh, S., Garg, N., & Dhiman, S. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03418-7 · Cited by 197 · see citing works

A multiomics approach to heterogeneity in Alzheimer’s disease: focused review and roadmap

Badhwar, A., McFall, G. P., Sapkota, S., Black, S. E., Chertkow, H. M., Duchesne, S., Masellis, M., Li, L., Dixon, R. A., & Bellec, P. (2019) · Brain · doi:10.1093/brain/awz384 · Cited by 168 · see citing works

Glial cells in Alzheimer’s disease: From neuropathological changes to therapeutic implications

Uddin, M. S., & Lim, L. W. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101622 · Cited by 149 · see citing works

Role of Ceramidases in Sphingolipid Metabolism and Human Diseases

Parveen, F., Bender, D. A., Law, S., Mishra, V. K., Chen, C.-C., & Ke, L. (2019) · Cells · doi:10.3390/cells8121573 · Cited by 147 · see citing works

Research Progress in the Pathogenesis of Alzheimer's Disease

Chen, Y. (2018) · Chinese Medical Journal · doi:10.4103/0366-6999.235112 · Cited by 139 · see citing works

Lipid Profiling of Alzheimer’s Disease Brain Highlights Enrichment in Glycerol(phospho)lipid, and Sphingolipid Metabolism

Akyol, S., Ugur, Z., Yılmaz, A., Ustun, I., Gorti, S. K. K., Oh, K., McGuinness, B., Passmore, P., Kehoe, P. G., Maddens, M. E., et al. (2021) · Cells · doi:10.3390/cells10102591 · Cited by 132 · see citing works

Targeted lipidomics reveal derangement of ceramides in major depression and bipolar disorder

Brunkhorst-Kanaan, N., Klatt‐Schreiner, K., Hackel, J., Schröter, K., Trautmann, S., Hahnefeld, L., Wicker, S., Reif, A., Thomas, D., Geißlinger, G., et al. (2019) · Metabolism · doi:10.1016/j.metabol.2019.04.002 · Cited by 132 · see citing works

Review: Impact of Helicobacter pylori on Alzheimer's disease: What do we know so far?

Doulberis, M., Kotronis, G., Thomann, R., Pοlyzos, S. A., Boziki, M. K., Gialamprinou, D., Deretzi, G., Katsinelos, P., & Kountouras, J. (2017) · Helicobacter · doi:10.1111/hel.12454 · Cited by 127 · see citing works

Anti-Alzheimers molecular mechanism of icariin: insights from gut microbiota, metabolomics, and network pharmacology

Liu, Y., Li, H., Wang, X., Huang, J., Zhao, D. S., Tan, Y., Zhang, Z., Zhang, Z., Zhu, L., Wu, B., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04137-z · Cited by 124 · see citing works

Insights into myalgic encephalomyelitis/chronic fatigue syndrome phenotypes through comprehensive metabolomics

Nagy-Szakal, D., Barupal, D. K., Lee, B., Che, X., Williams, B. L., Kahn, E. J. R., Ukaigwe, J. E., Bateman, L., Klimas, N. G., Komaroff, A. L., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-28477-9 · Cited by 120 · see citing works

Nanoparticles as potential clinical therapeutic agents in Alzheimer’s disease: focus on selenium nanoparticles

Nazıroğlu, M., Muhamad, S., & Pecze, L. (2017) · Expert Review of Clinical Pharmacology · doi:10.1080/17512433.2017.1324781 · Cited by 118 · see citing works

Omega-3 fatty acids, lipids, and apoE lipidation in Alzheimer's disease: a rationale for multi-nutrient dementia prevention

Grimm, M. O. W., Michaelson, D. M., & Hartmann, T. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r076331 · Cited by 110 · see citing works

Sphingosine 1-Phosphate Receptors and Metabolic Enzymes as Druggable Targets for Brain Diseases

Grassi, S., Mauri, L., Prioni, S., Cabitta, L., Sonnino, S., Prinetti, A., & Giussani, P. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00807 · Cited by 109 · see citing works

Promising Metabolite Profiles in the Plasma and CSF of Early Clinical Parkinson's Disease

Stoessel, D., Schulte, C., dos Santos, M. C. T., Scheller, D., Rebollo‐Mesa, I., Deuschle, C., Walther, D., Schauer, N., Berg, D., da Costa, A. N., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00051 · Cited by 104 · see citing works

The interactions of p53 with tau and Aß as potential therapeutic targets for Alzheimer’s disease

Jembrek, M. J., Slade, N., Hof, P. R., & Šimić, G. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.001 · Cited by 99 · see citing works

Crocus sativus Extract Tightens the Blood-Brain Barrier, Reduces Amyloid β Load and Related Toxicity in 5XFAD Mice

Batarseh, Y. S., Bharate, S. S., Kumar, V., Kumar, A., Vishwakarma, R. A., Bharate, S. B., & Kaddoumi, A. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00101 · Cited by 99 · see citing works

Anti-Oxidative, Anti-Inflammatory and Anti-Apoptotic Effects of Flavonols: Targeting Nrf2, NF-κB and p53 Pathways in Neurodegeneration

Jembrek, M. J., Oršolić, N., Mandić, L., Sadžak, A., & Šegota, S. (2021) · Antioxidants · doi:10.3390/antiox10101628 · Cited by 99 · see citing works

A neurodegenerative cellular stress response linked to dark microglia and toxic lipid secretion

Flury, A. G., Aljayousi, L., Park, H.-J., Khakpour, M., Mechler, J., Aziz, S., McGrath, J. D., Deme, P., Sandberg, C., Ibáñez, F. G., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.11.018 · Cited by 98 · see citing works

Inflammasome-mediated innate immunity in Alzheimer’s disease

Venegas, C., & Heneka, M. T. (2019) · The FASEB Journal · doi:10.1096/fj.201900439 · Cited by 93 · see citing works

Neurodegenerative Pathways in Alzheimer’s Disease: A Review

Ramachandran, A. K., Das, S., Joseph, A., Shenoy, G. G., Alex, A. T., & Mudgal, J. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200807130637 · Cited by 94 · see citing works

The Cross-Talk Between Sphingolipids and Insulin-Like Growth Factor Signaling: Significance for Aging and Neurodegeneration

Jęśko, H. M., Stępień, A., Lukiw, W. J., & Strosznajder, R. P. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1286-3 · Cited by 85 · see citing works

Defective Sphingosine-1-phosphate metabolism is a druggable target in Huntington’s disease

Pardo, A. D., Amico, E., Basit, A., Armirotti, A., Joshi, P. K., Neely, M. D., Vuono, R., Castaldo, S., Digilio, A. F., Scalabrì, F., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05709-y · Cited by 81 · see citing works

Sphingolipids in neuroinflammation: a potential target for diagnosis and therapy

Lee, J. Y., Jin, H. K., & Bae, J.-S. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.1.278 · Cited by 80 · see citing works

Accumulation of saposin in dystrophic neurites is linked to impaired lysosomal functions in Alzheimer’s disease brains

Sharoar, M. G., Palko, S., Ge, Y., Saido, T. C., & Yan, R. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00464-1 · Cited by 78 · see citing works

Schisandra chinensis Fructus and Its Active Ingredients as Promising Resources for the Treatment of Neurological Diseases

Zhang, M., Xu, L., & Yang, H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071970 · Cited by 77 · see citing works

Cardiolipin promotes electron transport between ubiquinone and complex I to rescue PINK1 deficiency

Vos, M. H., Geens, A., Böhm, C., Deaulmerie, L., Swerts, J., Rossi, M., Craessaerts, K., Leites, E. P., Seibler, P., Raković, A., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201511044 · Cited by 77 · see citing works

On the role of sphingolipids in cell survival and death

Iessi, E., Marconi, M., Manganelli, V., Sorice, M., Malorni, W., Garofalo, T., & Matarrese, P. (2020) · International review of cytology · doi:10.1016/bs.ircmb.2020.02.004 · Cited by 74 · see citing works

Integrative metabolomics science in Alzheimer’s disease: Relevance and future perspectives

Lista, S., González‐Domínguez, R., López‐Ortiz, S., González‐Domínguez, Á., Menéndez, H., Martín-Hernández, J., Lucía, A., Emanuele, E., Centonze, D., Imbimbo, B. P., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101987 · Cited by 75 · see citing works

Icariin targets p53 to protect against ceramide-induced neuronal senescence: Implication in Alzheimer's disease

Wu, B., Xiao, Q., Zhu, L., Tang, H., & Peng, W. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.08.031 · Cited by 74 · see citing works

Protective effect of rutin against carbon tetrachloride-induced oxidative stress, inflammation and apoptosis in mouse kidney associated with the ceramide, MAPKs, p53 and calpain activities

Ma, J., Liu, C., & Yang, W. (2018) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2018.03.003 · Cited by 72 · see citing works

Nervonic acid and its sphingolipids: Biological functions and potential food applications

Phung, N. V., Rong, F., Xia, W.-Y., Fan, Y., Li, X. Y., Wang, S. A., & Li, F. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2203753 · Cited by 72 · see citing works

Steroid and Xenobiotic Receptor Signalling in Apoptosis and Autophagy of the Nervous System

Wnuk, A., & Kajta, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112394 · Cited by 71 · see citing works

Silencing of LncRNA BDNF-AS attenuates Aβ25-35-induced neurotoxicity in PC12 cells by suppressing cell apoptosis and oxidative stress

Guo, C.-C., Jiao, C., & Gao, Z.-M. (2018) · Neurological Research · doi:10.1080/01616412.2018.1480921 · Cited by 70 · see citing works

Lipids in Pathophysiology and Development of the Membrane Lipid Therapy: New Bioactive Lipids

Torres, M., Parets, S., Fernández-Díaz, J., Beteta-Göbel, R., Rodríguez-Lorca, R., Román, R., Lladó, V., Rosselló, C. A., Fernández‐García, P., & Escribá, P. V. (2021) · Membranes · doi:10.3390/membranes11120919 · Cited by 70 · see citing works

The Role of Copper in Tau-Related Pathology in Alzheimer’s Disease

Zubčić, K., Hof, P. R., Šimić, G., & Jembrek, M. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.572308 · Cited by 69 · see citing works

Properties and molecular mechanisms underlying geniposide-mediated therapeutic effects in chronic inflammatory diseases

Deng, R., Wu, H., Yan, W., & Mengdie, W. (2021) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2021.113958 · Cited by 69 · see citing works

Insulin signaling: An opportunistic target to minify the risk of Alzheimer’s disease

Pardeshi, R., Bolshette, N. B., Gadhave, K., Ahire, A., Ahmed, S., Cassano, T., Gupta, V. B., & Lahkar, M. (2017) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2017.05.004 · Cited by 65 · see citing works

Intracellular Molecular Targets and Signaling Pathways Involved in Antioxidative and Neuroprotective Effects of Cannabinoids in Neurodegenerative Conditions

Tadijan, A., Vlašić, I., Vlainić, J., Đikić, D., Oršolić, N., & Jembrek, M. J. (2022) · Antioxidants · doi:10.3390/antiox11102049 · Cited by 64 · see citing works

Ceramides and diabetes mellitus: an update on the potential molecular relationships

Yaribeygi, H., Bo, S., Ruscica, M., & Sahebkar, A. (2019) · Diabetic Medicine · doi:10.1111/dme.13943 · Cited by 64 · see citing works

Lipid metabolism and oxidative stress in patients with Alzheimer's disease and amnestic mild cognitive impairment

Nie, Y., Chu, C., Qin, Q., Shen, H., Wen, L., Tang, Y., & Qu, M. (2023) · Brain Pathology · doi:10.1111/bpa.13202 · Cited by 63 · see citing works

Targeted Metabolomic Analysis in Alzheimer’s Disease Plasma and Brain Tissue in Non-Hispanic Whites

Kalecký, K., German, D. C., Montillo, A., & Bottiglieri, T. (2022) · Journal of Alzheimer s Disease · doi:10.3233/jad-215448 · Cited by 62 · see citing works

Death-associated protein kinase 1 phosphorylates NDRG2 and induces neuronal cell death

You, M., Kim, B. M., Chen, C.-H., Begley, M. J., Cantley, L. C., & Lee, T. H. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.114 · Cited by 61 · see citing works

Suppression of lncRNA-ATB prevents amyloid-β-induced neurotoxicity in PC12 cells via regulating miR-200/ZNF217 axis

Wang, J., Zhou, T.-T., Wang, T., & Wang, B. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.08.155 · Cited by 57 · see citing works

Aging membranes: Unexplored functions for lipids in the lifespan of the central nervous system

Skowronska‐Krawczyk, D., & Budin, I. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110817 · Cited by 55 · see citing works

Lipidomic analysis of serum samples from migraine patients

Ren, C., Liu, J., Zhou, J., Liang, H., Wang, Y., Sun, Y., Ma, B., & Yin, Y. (2018) · Lipids in Health and Disease · doi:10.1186/s12944-018-0665-0 · Cited by 53 · see citing works

The Protective Effect of Baicalin Against Lead-Induced Renal Oxidative Damage in Mice

Zhang, Z., Gao, X., Guo, M., Jiang, H., Cao, Y., & Zhang, N. (2016) · Biological Trace Element Research · doi:10.1007/s12011-016-0731-2 · Cited by 51 · see citing works

Cardiolipin in Central Nervous System Physiology and Pathology

Pointer, C. B., & Klegeris, A. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-016-0458-9 · Cited by 51 · see citing works

Novelty of Sphingolipids in the Central Nervous System Physiology and Disease: Focusing on the Sphingolipid Hypothesis of Neuroinflammation and Neurodegeneration

Ayub, M., Jin, H.-K., & Bae, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147353 · Cited by 51 · see citing works

The Role of Mitochondrial Quality Control in Cognitive Dysfunction in Diabetes

Luo, J.-S., Ning, J., Chen, Z.-Y., Li, W., Zhou, R., Yan, R., Chen, M., & Ding, L.-L. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03631-y · Cited by 50 · see citing works

Lysophospholipids and Their G-Coupled Protein Signaling in Alzheimer’s Disease: From Physiological Performance to Pathological Impairment

Hao, Y., Guo, M., Feng, Y., Dong, Q., & Cui, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00058 · Cited by 48 · see citing works

Geniposide ameliorates chronic unpredictable mild stress induced depression-like behavior through inhibition of ceramide-PP2A signaling via the PI3K/Akt/GSK3β axis

Wang, M., Yang, L., Chen, Z., Dai, L., Xi, C., Wu, X., Wu, G., Wang, Y., & Hu, J. (2021) · Psychopharmacology · doi:10.1007/s00213-021-05895-8 · Cited by 48 · see citing works

Diverse roles of ceramide in the progression and pathogenesis of Alzheimer's disease

(2022) · doi:10.3390/biomedicines10081956 · Cited by 47 · see citing works

Ceramides and mitochondrial homeostasis

Ding, S. Z., Li, G., Fu, T., Zhang, T., Lu, X., Li, N., & Geng, Q. (2024) · Cellular Signalling · doi:10.1016/j.cellsig.2024.111099 · Cited by 48 · see citing works

The role of mitochondrial defects and oxidative stress in Alzheimer’s disease

Islam, B. U., Jabir, N. R., & Tabrez, S. S. M. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1584808 · Cited by 48 · see citing works

Isoalantolactone induces apoptosis in human breast cancer cells via ROS-mediated mitochondrial pathway and downregulation of SIRT1

Li, Z., Qin, B., Qi, X., Mao, J., & Wu, D. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0815-8 · Cited by 45 · see citing works

Type 2 Diabetes and Alzheimer’s Disease: The Emerging Role of Cellular Lipotoxicity

Marrano, N., Biondi, G., Borrelli, A., Rella, M., Zambetta, T., Gioia, L. D., Caporusso, M., Logroscino, G., Perrini, S., Giorgino, F., et al. (2023) · Biomolecules · doi:10.3390/biom13010183 · Cited by 44 · see citing works

A review of the mechanisms of abnormal ceramide metabolism in type 2 diabetes mellitus, Alzheimer’s disease, and their co-morbidities

Pan, Y., Li, J., Lin, P., Wan, L., Qu, Y., Cao, L., & Wang, L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1348410 · Cited by 49 · see citing works

Metabolomic‐guided discovery of Alzheimer's disease biomarkers from body fluid

Ady, C. N. A. E., Lim, S. M., Teh, L. K., Salleh, M. Z., Chin, A., Tan, M. P., Poi, P. J. H., Kamaruzzaman, S. B., Majeed, A. B. A., & Ramasamy, K. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24048 · Cited by 41 · see citing works

Recent Development in the Understanding of Molecular and Cellular Mechanisms Underlying the Etiopathogenesis of Alzheimer’s Disease

Afsar, A., Castro, M. D. C. C., Soladogun, A. S., & Li, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087258 · Cited by 42 · see citing works

Oxidative Stress and Natural Antioxidants: Back and Forth in the Neurological Mechanisms of Alzheimer’s Disease

Mani, S., Dubey, R., Lai, I., Babu, M. A., Tyagi, S., Swargiary, G., Mody, D., Singh, M., Agarwal, S., Iqbal, D., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220700 · Cited by 40 · see citing works

Recent advances from metabolomics and lipidomics application in alzheimer’s disease inspiring drug discovery

Čuperlović‐Culf, M., & Badhwar, A. (2019) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1674808 · Cited by 40 · see citing works

The Role of Sphingolipids and Specialized Pro-Resolving Mediators in Alzheimer’s Disease

de Wit, N. M., Mol, K., Rodríguez‐Lorenzo, S., de Vries, H. E., & Kooij, G. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.620348 · Cited by 39 · see citing works

Therapeutic potential of plant iridoids in depression: a review

Kou, Y., Li, Z.-H., Yang, T.-G., Shen, X., Wang, X., Li, H.-P., Zhou, K., Li, L., Xia, Z., Zheng, X.-O., et al. (2022) · Pharmaceutical Biology · doi:10.1080/13880209.2022.2136206 · Cited by 34 · see citing works

Analysis of urinary sphingolipids using liquid chromatography‐tandem mass spectrometry in diabetic nephropathy

Morita, Y., Kurano, M., Sakai, E., Nishikawa, T., Nishikawa, M., Sawabe, M., Aoki, J., & Yatomi, Y. (2019) · Journal of Diabetes Investigation · doi:10.1111/jdi.13154 · Cited by 37 · see citing works

MicroRNA-338-5p alleviates neuronal apoptosis via directly targeting BCL2L11 in APP/PS1 mice.

Li, J., Li, D., Zhou, H., Wu, G., He, Z., Liao, W., Li, Y., & Zhi, Y. (2020) · Aging · doi:10.18632/aging.104005 · Cited by 35 · see citing works

To be or not to be: PP2A as a dual player in CNS functions, its role in neurodegeneration, and its interaction with brain insulin signaling

Javadpour, P., Dargahi, L., Ahmadiani, A., & Ghasemi, R. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03063-y · Cited by 35 · see citing works

Plasma Lipidomics Approach in Early and Specific Alzheimer’s Disease Diagnosis

Peña‐Bautista, C., Álvarez‐Sánchez, L., Roca, M., García, L., Baquero, M., & Cháfer‐Pericás, C. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11175030 · Cited by 34 · see citing works

Fingolimod Affects Transcription of Genes Encoding Enzymes of Ceramide Metabolism in Animal Model of Alzheimer’s Disease

Jęśko, H. M., Wencel, P. L., Wójtowicz, S., Strosznajder, J. B., Lukiw, W. J., & Strosznajder, R. P. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01908-3 · Cited by 34 · see citing works

Cerebrospinal Fluid C18 Ceramide Associates with Markers of Alzheimer’s Disease and Inflammation at the Pre- and Early Stages of Dementia

Teitsdottir, U. D., Halldórsson, S., Rolfsson, Ó., Lund, S. H., Jónsdóttir, M. K., Snædal, J., & Petersen, P. H. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200964 · Cited by 37 · see citing works

Poria cocos polysaccharide attenuates damage of nervus in Alzheimer’s disease rat model induced by D-galactose and aluminum trichloride

Zhou, X., Zhang, Y., Jiang, Y., Zhou, C., & Ling, Y. (2021) · Neuroreport · doi:10.1097/wnr.0000000000001648 · Cited by 33 · see citing works

Oleanolic acid alleviates oxidative stress in Alzheimer’s disease by regulating stanniocalcin‐1 and uncoupling protein‐2 signalling

Guo, Q., He, J., Zhang, H., Li, Y., & Li, H. (2020) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13292 · Cited by 32 · see citing works

The protective mechanism of Ginkgolides and Ginkgo flavonoids on the TNF-α induced apoptosis of rat hippocampal neurons and its mechanisms in vitro

Guo, M., Suo, Y., Gao, Q., Du, H., Zeng, W., Wang, Y., Hu, X., & Jiang, X. (2015) · Heliyon · doi:10.1016/j.heliyon.2015.e00020 · Cited by 32 · see citing works

Status of Metabolomic Measurement for Insights in Alzheimer’s Disease Progression—What Is Missing?

Yin, C., Harms, A. C., Hankemeier, T., Kindt, A. S. D., & de Lange, E. C. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054960 · Cited by 32 · see citing works

Potential Role of Phosphoglycerol Dihydroceramide Produced by Periodontal Pathogen Porphyromonas gingivalis in the Pathogenesis of Alzheimer’s Disease

Yamada, C., Akkaoui, J., Ho, A., Duarte, C. L., Deth, R. C., Kawai, T., Nichols, F. C., Lakshmana, M. K., & Movilă, A. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.591571 · Cited by 31 · see citing works

Sphingolipids as Regulators of Neuro-Inflammation and NADPH Oxidase 2

Arsenault, E. J., McGill, C. M., & Barth, B. M. (2021) · NeuroMolecular Medicine · doi:10.1007/s12017-021-08646-2 · Cited by 31 · see citing works

Altered Sphingolipid Balance in Capillary Cerebral Amyloid Angiopathy

de Wit, N. M., Snkhchyan, H., den Hoedt, S., Wattimena, D. J. L., de Vos, R., Mulder, M. T., Walter, J., Martínez‐Martínez, P., Hoozemans, J. J. M., Rozemüller, A. J. M., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160551 · Cited by 30 · see citing works

Protective effects of grape seed proanthocyanidins against iron overload-induced renal oxidative damage in rats

Yun, S., Chu, D., He, X., Zhang, W., & Feng, C. (2019) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2019.126407 · Cited by 30 · see citing works

Revealing the Molecular Mechanisms of Alzheimer’s Disease Based on Network Analysis

Bayraktar, A., Lam, S. C. C., Altay, Ö., Li, X., Yuan, M., Zhang, C., Arif, M., Türkez, H., Uhlén, M., Shoaie, S., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111556 · Cited by 30 · see citing works

Endothelial Senescence and Its Impact on Angiogenesis in Alzheimer’s Disease

Georgieva, I., Tchekalarova, J. D., Iliev, D. B., & Tzoneva, R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411344 · Cited by 29 · see citing works

Ambient PM particles reach mouse brain, generate ultrastructural hallmarks of neuroinflammation, and stimulate amyloid deposition, tangles, and plaque formation

Hameed, S., Zhao, J., & Zare, R. N. (2020) · Talanta Open · doi:10.1016/j.talo.2020.100013 · Cited by 29 · see citing works

MiR-191-5p Attenuates Tau Phosphorylation, Aβ Generation, and Neuronal Cell Death by Regulating Death-Associated Protein Kinase 1

Wang, L., Shui, X., Zhang, M., Mei, Y., Xia, Y., Lan, G., Hu, L., Gan, C., Tian, Y., Li, R., et al. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00423 · Cited by 29 · see citing works

Melatonin decreases brain apoptosis, oxidative stress, and CD200 expression and increased survival rate in mice infected by Venezuelan equine encephalitis virus

Montiel, M., Bonilla, E., Valero, N. J., Mosquera, J., Espina, L. M., Quiroz, Y., & Álvarez‐Mon, M. (2015) · Antiviral chemistry & chemotherapy · doi:10.1177/2040206616660851 · Cited by 29 · see citing works

TUFM is involved in Alzheimer’s disease-like pathologies that are associated with ROS

Zhong, B., Zhou, G., Song, L., Wen, Q., Deng, X., Ma, Y., Hu, L., & Chen, G. (2021) · The FASEB Journal · doi:10.1096/fj.202002461r · Cited by 28 · see citing works

Inhibitory Effect of Lychee Seed Saponins on Apoptosis Induced by Aβ25-35 through Regulation of the Apoptotic and NF-κB Pathways in PC12 Cells

Wang, X., Zhang, H., Liu, J., Chen, R., Tang, Y., Chen, H., Gu, L., Mao, L., Cao, S., Qin, D., et al. (2017) · Nutrients · doi:10.3390/nu9040337 · Cited by 27 · see citing works

Mitochondrial methionine sulfoxide reductase B2 links oxidative stress to Alzheimer's disease-like pathology

Xiang, X., Li, S., Deng, X., Tang, Y., Min, Z., Luo, B., Wen, Q., Li, K., Chen, J., Ma, Y., et al. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.05.006 · Cited by 26 · see citing works

Selective autophagy: The new player in the fight against neurodegenerative diseases?

Wu, M.-Y., Song, J., Wang, S.-F., Cai, C.-Z., Li, M., & Lu, J. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.11.009 · Cited by 27 · see citing works

Intracellular Lipid Accumulation and Mitochondrial Dysfunction Accompanies Endoplasmic Reticulum Stress Caused by Loss of the Co-chaperone DNAJC3

Jennings, M. J., Hathazi, D., Nguyen, C., Munro, B., Münchberg, U., Ahrends, R., Schenck, A., Eidhof, I., Freier, E., Synofzik, M., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.710247 · Cited by 26 · see citing works

Review Article Ceramides in Alzheimer’s Disease: Key Mediators of Neuronal Apoptosis Induced by Oxidative Stress and A

Jembrek, M. J., Hof, P. R., & Šimit, G. (2016)

Involvement of oxidative stress-induced abnormalities in ceramide and cholesterol metabolism in brain aging and Alzheimer's disease

Cutler, R. G., Kelly, J., Storie, K., Pedersen, W. A., Tammara, A., Hatanpaa, K. J., Troncoso, J. C., & Mattson, M. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305799101 · Cited by 1,135 · see citing works

Assessing the critical role of ceramide in the pathogenesis of Alzheimer's disease and its clinical significance

Huang, Y., Chan, H., Khoo, J.-Y., Chan, M.-L., Bender, D. A., Ponnusamy, V. K., Belaidi, A. A., & Ke, L. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2025.106104 · Cited by 4 · see citing works

Ceramides may Play a Central Role in the Pathogenesis of Alzheimer’s Disease: a Review of Evidence and Horizons for Discovery

Kalkman, H. O., & Smigielski, L. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04989-0 · Cited by 29 · see citing works

Ceramide: a central regulator in Alzheimer’s disease pathogenesis

Choudhary, P., Kumari, S., Bagri, K., & Deshmukh, R. R. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01719-9 · Cited by 10 · see citing works