Alzheimer's APP mangles mitochondria

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · see citing works

Mitochondrial abnormalities in Alzheimer's disease

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ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease

Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · Cited by 1,104 · see citing works

Intraneuronal Aβ42 Accumulation in Human Brain

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Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction

Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works

Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells

Anandatheerthavarada, H. K., Biswas, G., Robin, M.-A., & Avadhani, N. G. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207030 · Cited by 571 · see citing works

Electron transport chain defects in Alzheimer's disease brain

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β‐Amyloid inhibits integrated mitochondrial respiration and key enzyme activities

Casley, C. S., Canevari, L., Land, J. M., Clark, J. B., & Sharpe, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00681.x · Cited by 485 · see citing works

Copper-Dependent Inhibition of Human Cytochrome<i>c</i>Oxidase by a Dimeric Conformer of Amyloid-β_1-42

Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327 · see citing works

β-Amyloid Accumulation Impairs Multivesicular Body Sorting by Inhibiting the Ubiquitin-Proteasome System

Almeida, C. G., Takahashi, R. H., & Gouras, G. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5078-05.2006 · Cited by 316 · see citing works

Nicastrin, Presenilin, APH-1, and PEN-2 Form Active γ-Secretase Complexes in Mitochondria

Hansson, C. A., Frykman, S., Farmery, M. R., Tjernberg, L. O., Nilsberth, C., Pursglove, S. E., Ito, A., Winblad, B., Cowburn, R. F., Thyberg, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404500200 · Cited by 256 · see citing works

Degradation of the Amyloid β-Protein by the Novel Mitochondrial Peptidasome, PreP

Falkevall, A., Alikhani, N., Bhushan, S., Pavlov, P. F., Busch, K., Johnson, K. A., Eneqvist, T., Tjernberg, L. O., Ankarcrona, M., & Glaser, E. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602532200 · Cited by 202 · see citing works

Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria

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Bimodal Targeting of Microsomal CYP2E1 to Mitochondria through Activation of an N-terminal Chimeric Signal by cAMP-mediated Phosphorylation

Robin, M., Anandatheerthavarada, H. K., Biswas, G., Sepuri, N. B. V., Gordon, D. M., Pain, D., & Avadhani, N. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203292200 · Cited by 147 · see citing works

Multi-target-Directed Ligands To Combat Neurodegenerative Diseases

Cavalli, A., Bolognesi, M. L., Minarini, A., Rosini, M., Tumiatti, V., Recanatini, M., & Melchiorre, C. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm7009364 · Cited by 1,152 · see citing works

Review Article: Genetics of Alzheimer Disease

Bekris, L. M., Yu, C.-E., Bird, T. D., & Tsuang, D. W. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383571 · Cited by 1,029 · see citing works

Mitochondrial Glutathione, a Key Survival Antioxidant

Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., & Fernández-Checa, J. C. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2695 · Cited by 986 · see citing works

Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease

Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · see citing works

Molecular mechanisms of neurodegeneration in Alzheimer's disease

Crews, L., & Masliah, E. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq160 · Cited by 772 · see citing works

Early deficits in synaptic mitochondria in an Alzheimer's disease mouse model

Du, H., Guo, L., Yan, S., Sosunov, A. A., McKhann, G. M., & ShiDu Yan, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006586107 · Cited by 704 · see citing works

Glutathione and mitochondria

Ribas, V., García‐Ruiz, C., & Fernández-Checa, J. C. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00151 · Cited by 572 · see citing works

Microglial cell dysregulation in brain aging and neurodegeneration

von Bernhardi, R., Eugenín-von Bernhardi, L., & Eugenín, J. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00124 · Cited by 556 · 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

Mitochondrial permeability transition pore is a potential drug target for neurodegeneration

Rao, V. K., Carlson, E. A., & Yan, S. S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.09.003 · Cited by 325 · see citing works

Aging and amyloid beta-induced oxidative DNA damage and mitochondrial dysfunction in Alzheimer's disease: Implications for early intervention and therapeutics

Mao, P., & Reddy, P. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.005 · Cited by 311 · see citing works

PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease

Du, F., Yu, Q., Yan, S., Hu, G., Lue, L., Walker, D., Wu, L., Yan, S. F., Tieu, K., & Yan, S. S. (2017) · Brain · doi:10.1093/brain/awx258 · Cited by 306 · see citing works

RAGE-mediated signaling contributes to intraneuronal transport of amyloid-β and neuronal dysfunction

Takuma, K., Fang, F., Zhang, W., Yan, S., Fukuzaki, E., Du, H., Sosunov, A., McKhann, G., Funatsu, Y., Nakamichi, N., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905686106 · Cited by 290 · see citing works

CORUM: the comprehensive resource of mammalian protein complexes–2022

Tsitsiridis, G., Steinkamp, R., Giurgiu, M., Brauner, B., Fobo, G., Frishman, G., Montrone, C., & Ruepp, A. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac1015 · Cited by 263 · see citing works

Dendritic spines: Revisiting the physiological role

Chidambaram, S. B., Rathipriya, A. G., Bolla, S. R., Bhat, A., Ray, B., Mahalakshmi, A. M., Manivasagam, T., Thenmozhi, A. J., Essa, M. M., Guillemin, G. J., et al. (2019) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2019.01.005 · Cited by 255 · see citing works

The role of mitochondrial dysfunction in age-related diseases

Lane, R. K., Hilsabeck, T., & Rea, S. L. (2015) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2015.05.021 · Cited by 205 · see citing works

Mitochondrial glutathione: Features, regulation and role in disease

Marı́, M., Morales, A., Colell, A., García‐Ruiz, C., Kaplowitz, N., & Fernández-Checa, J. C. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2012.10.018 · Cited by 205 · see citing works

Mitochondria and Cell Bioenergetics: Increasingly Recognized Components and a Possible Etiologic Cause of Alzheimer's Disease

Swerdlow, R. H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4149 · Cited by 203 · see citing works

Mitochondrial Etiology of Neuropsychiatric Disorders

Pei, L., & Wallace, D. C. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.018 · Cited by 196 · see citing works

Alzheimer's Disease: Redox Dysregulation As a Common Denominator for Diverse Pathogenic Mechanisms

Rommy von Bernhardi, M., & Eugenín, J. L. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4082 · Cited by 189 · see citing works

Protein aggregation and neurodegeneration in prototypical neurodegenerative diseases: Examples of amyloidopathies, tauopathies and synucleinopathies

Bourdenx, M., Koulakiotis, N. S., Sanoudou, D., Bézard, E., Dehay, B., & Tsarbopoulos, A. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.003 · Cited by 189 · see citing works

Inhibition of Amyloid-β (Aβ) Peptide-Binding Alcohol Dehydrogenase-Aβ Interaction Reduces Aβ Accumulation and Improves Mitochondrial Function in a Mouse Model of Alzheimer's Disease

Yao, J., Du, H., Yan, S., Fang, F., Wang, C., Lue, L., Guo, L., Chen, D., Stern, D. M., Gunn‐Moore, F. J., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4717-10.2011 · Cited by 184 · see citing works

Role of Mitochondrial Amyloid-β in Alzheimer's Disease

Chen, J. X., & Yan, S. S. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100357 · Cited by 181 · see citing works

Inhibition of ERK-DLP1 signaling and mitochondrial division alleviates mitochondrial dysfunction in Alzheimer's disease cybrid cell

Gan, X., Huang, S., Wu, L., Wang, Y., Hu, G., Li, G., Zhang, H., Yu, H., Swerdlow, R. H., Chen, J. X., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.11.009 · Cited by 181 · see citing works

Intracellular Cholesterol Trafficking and Impact in Neurodegeneration

Arenas, F., García‐Ruiz, C., & Fernández-Checa, J. C. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00382 · Cited by 161 · see citing works

From Cannabis sativa to Cannabidiol: Promising Therapeutic Candidate for the Treatment of Neurodegenerative Diseases

Cassano, T., Villani, R., Pace, L., Carbone, A., Bukke, V. N., Orkisz, S., Avolio, C., & Serviddio, G. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00124 · Cited by 148 · see citing works

Vitamin E–gene interactions in aging and inflammatory age-related diseases: Implications for treatment. A systematic review

Mocchegiani, E., Costarelli, L., Giacconi, R., Malavolta, M., Basso, A., Piacenza, F., Ostan, R., Cevenini, E., Gonos, E. S., Franceschi, C., et al. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.01.001 · Cited by 143 · see citing works

Mitochondrial DNA repair and association with aging – An update

Gredilla, R., Bohr, V. A., & Stevnsner, T. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.017 · Cited by 141 · see citing works

Pinocembrin protects against β-amyloid-induced toxicity in neurons through inhibiting receptor for advanced glycation end products (RAGE)-independent signaling pathways and regulating mitochondrion-mediated apoptosis

Liu, R., Wu, C., Zhou, D., Yang, F., Tian, S., Zhang, L., Zhang, T., & Du, G. (2012) · BMC Medicine · doi:10.1186/1741-7015-10-105 · Cited by 141 · see citing works

Nuclear but not mitochondrial‐encoded oxidative phosphorylation genes are altered in aging, mild cognitive impairment, and Alzheimer's disease

Mastroeni, D., Khdour, O. M., Delvaux, E., Nolz, J., Olsen, G., Berchtold, N. C., Cotman, C. W., Hecht, S. M., & Coleman, P. D. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.09.003 · Cited by 131 · see citing works

β-Amyloid and the Pathomechanisms of Alzheimer’s Disease: A Comprehensive View

Penke, B., Bogár, F., & Fülöp, L. (2017) · Molecules · doi:10.3390/molecules22101692 · Cited by 135 · see citing works

The role of amyloid-beta in the regulation of memory

Morley, J. E., & Farr, S. A. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.018 · Cited by 132 · see citing works

Alzheimer's disease: new approaches to drug discovery

Bolognesi, M. L., Matera, R., Minarini, A., Rosini, M., & Melchiorre, C. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.04.619 · Cited by 132 · see citing works

Review: Quantifying Mitochondrial Dysfunction in Complex Diseases of Aging

Horan, M. P., Pichaud, N., & Ballard, J. W. O. (2012) · The Journals of Gerontology Series A · doi:10.1093/gerona/glr263 · Cited by 125 · see citing works

Synapses and Dendritic Spines as Pathogenic Targets in Alzheimer’s Disease

Yu, W., & Lu, B. (2012) · Neural Plasticity · doi:10.1155/2012/247150 · Cited by 119 · see citing works

Mitochondrial γ‐secretase participates in the metabolism of mitochondria‐associated amyloid precursor protein

Pavlov, P. F., Wiehager, B., Sakai, J., Frykman, S., Behbahani, H., Winblad, B. G., & Ankarcrona, M. (2010) · The FASEB Journal · doi:10.1096/fj.10-157230 · Cited by 113 · see citing works

Recent advances in hydrogen peroxide imaging for biological applications

Guo, H., Aleyasin, H., Dickinson, B. C., Haskew-Layton, R. E., & Ratan, R. R. (2014) · Cell & Bioscience · doi:10.1186/2045-3701-4-64 · Cited by 114 · see citing works

Mitochondria Dysfunction and Neurodegenerative Disorders: Cause or Consequence

Morais, V. A., & Strooper, B. D. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100345 · Cited by 111 · see citing works

Mitochondria, Cybrids, Aging, and Alzheimer's Disease

Swerdlow, R. H., Koppel, S., Weidling, I., Hayley, C., Ji, Y., & Wilkins, H. M. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2016.12.017 · Cited by 106 · see citing works

Are oxidative stress and mitochondrial dysfunction the key players in the neurodegenerative diseases?

Carlo, M. D., Giacomazza, D., Picone, P., Nuzzo, D., & Biagio, P. L. S. (2012) · Free Radical Research · doi:10.3109/10715762.2012.714466 · Cited by 106 · see citing works

Quantitative Interaction Proteomics of Neurodegenerative Disease Proteins

Hosp, F., Voßfeldt, H., Heinig, M., Vasiljević, D., Arumughan, A., Wyler, E., Landthaler, M., Hübner, N., Wanker, E. E., Lannfelt, L., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.030 · Cited by 101 · see citing works

Alzheimer’s disease treated patients showed different patterns for oxidative stress and inflammation markers

Gubandru, M., Margina, D. M., Tsitsimpikou, C., Goutzourelas, N., Tsarouhas, K., Ilie, M., Tsatsakis, A. M., & Kouretas, D. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.07.013 · Cited by 102 · see citing works

Mitochondrial cholesterol in health and disease.

García‐Ruiz, C., Marı́, M., Colell, A., Morales, A., Caballero, F. G., Montero, J., Terrones, O., Basáñez, G., & Fernández-Checa, J. C. (2009) · PubMed · doi:10.14670/hh-24.117 · Cited by 101 · see citing works

New Evidence of Mitochondria Dysfunction in the Female Alzheimer's Disease Brain: Deficiency of Estrogen Receptor-β

Long, J., He, P., Shen, Y., & Li, R. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120283 · Cited by 100 · see citing works

Glutamatergic alterations and mitochondrial impairment in a murine model of Alzheimer disease

Cassano, T., Serviddio, G., Gaetani, S., Romano, A., Dipasquale, P., Cianci, S., Bellanti, F., Laconca, L., Romano, A. D., Padalino, I., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.021 · Cited by 99 · see citing works

Investigation of the Relationship Between H 2 O 2 and HClO in Living Cells by a Bifunctional, Dual-ratiometric Responsive Fluorescent Probe

Han, J., Liu, X., Xiong, H., Wang, J., Wang, B., Song, X., & Wang, W. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05604 · Cited by 96 · see citing works

Glutamate and Mitochondria: Two Prominent Players in the Oxidative Stress-Induced Neurodegeneration

Cassano, T., Pace, L., Bedse, G., Lavecchia, A. M., Marco, F. D., Gaetani, S., & Serviddio, G. (2015) · Current Alzheimer Research · doi:10.2174/1567205013666151218132725 · Cited by 95 · see citing works

A Randomized, Placebo-Controlled Trial of Latrepirdine in Huntington Disease

Kieburtz, K. D. (2010) · Archives of Neurology · doi:10.1001/archneurol.2009.334 · Cited by 92 · see citing works

A select combination of clinically relevant phytoestrogens enhances estrogen receptor beta-binding selectivity and neuroprotective activities in vitro and in vivo.

Zhao, L.-Q., Mao, Z.-S., & Brinton, R. (2009) · Endocrinology · doi:10.1210/en.2008-0715 · Cited by 96 · see citing works

Cyclophilin D deficiency rescues Aβ-impaired PKA/CREB signaling and alleviates synaptic degeneration

Du, H., Guo, L., Wu, X., Sosunov, A. A., McKhann, G. M., Chen, J. X., & Yan, S. S. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.03.004 · Cited by 86 · see citing works

Increased neuronal PreP activity reduces Aβ accumulation, attenuates neuroinflammation and improves mitochondrial and synaptic function in Alzheimer disease's mouse model

Du, F., Wang, Y., Zhang, Z., Du, H., Yan, S., Sun, Q., Zhong, C., Wu, L., Vangavaragu, J. R., Yan, S., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv241 · Cited by 86 · see citing works

Autophagy of Mitochondria: A Promising Therapeutic Target for Neurodegenerative Disease

Kamat, P. K., Kalani, A., Kyles, P., Tyagi, S. C., & Tyagi, N. (2014) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-014-0006-5 · Cited by 82 · see citing works

Aging: All roads lead to mitochondria

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Down‐regulation of the Notch pathway mediated by a γ‐secretase inhibitor induces anti‐tumour effects in mouse models of T‐cell leukaemia

Tammam, J. G., Ware, C., Efferson, C. L., O’Neil, J., Rao, S. S., Qu, X., Gorenstein, J., Angagaw, M. H., Kim, H., Kenific, C. M., et al. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00389.x · Cited by 75 · see citing works

Structure‐Based Design and Synthesis of Benzothiazole Phosphonate Analogues with Inhibitors of Human ABAD‐Aβ for Treatment of Alzheimer’s Disease

Valasani, K. R., Hu, G., Chaney, M. O., & Yan, S. S. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12068 · Cited by 75 · see citing works

New cyclophilin D inhibitor rescues mitochondrial and cognitive function in Alzheimer’s disease

Samanta, S., Akhter, F., Roy, A., Chen, D., Turner, B., Wang, Y., Clemente, N., Wang, C., Swerdlow, R. H., Battaile, K. P., et al. (2023) · Brain · doi:10.1093/brain/awad432 · Cited by 62 · see citing works

Potentiation of Brain Mitochondrial Function by S-equol and R/S-equol Estrogen Receptor β Selective PhytoSERM Treatments

Yao, J., Zhao, L.-Q., Mao, Z.-S., Chen, S.-H., Wong, K., To, J., & Brinton, R. (2013) · Brain Research · doi:10.1016/j.brainres.2013.02.021 · Cited by 61 · see citing works

Molecular Dysfunctions of Mitochondria-Associated Membranes (MAMs) in Alzheimer’s Disease

Eysert, F., Kinoshita, P. F., Mary, A., Vaillant-Beuchot, L., Checler, F., & Chami, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249521 · Cited by 61 · see citing works

Emerging Proof of Protein Misfolding and Interactions in Multifactorial Alzheimer's Disease

Uddin, M. S., Mamun, A. A., Rahman, M. A., Behl, T., Perveen, A., Hafeez, A., Bin-Jumah, M. N., Abdel‐Daim, M. M., & Ashraf, G. M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200601161703 · Cited by 59 · see citing works

3‐nitropropionic acid‐induced mitochondrial permeability transition: Comparative study of mitochondria from different tissues and brain regions

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Metabolic disorder in Alzheimer’s disease

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Synapses, synaptic activity and intraneuronal Aβ in Alzheimer’s disease

Tampellini, D. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00013 · Cited by 54 · see citing works

Possible role of amyloid-beta, adenine nucleotide translocase and cyclophilin-D interaction in mitochondrial dysfunction of Alzheimer's disease

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CuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function

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A reaction based one- and two-photon fluorescent probe for selective imaging H2O2 in living cells and tissues

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Mesenchymal stromal cells for the treatment of Alzheimer’s disease: Strategies and limitations

Regmi, S., Liu, D. D., Shen, M., Kevadiya, B. D., Ganguly, A., Primavera, R., Chetty, S. S., Yarani, R., & Thakor, A. S. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1011225 · Cited by 52 · see citing works

A message emerging from development: the repression of mitochondrial β-F1-ATPase expression in cancer

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New therapeutic activity of metabolic enhancer piracetam in treatment of neurodegenerative disease: Participation of caspase independent death factors, oxidative stress, inflammatory responses and apoptosis

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