Neuroprotective Roles of the Reverse Transsulfuration Pathway in Alzheimer’s Disease

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404 · see citing works

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431 · see citing works

Clinical and biomarker changes in dominantly inherited Alzheimer's disease

Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814 · see citing works

Oxidative Stress

Sies, H., Berndt, C., & Jones, D. P. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045037 · Cited by 3,520 · see citing works

Plasma Homocysteine as a Risk Factor for Dementia and Alzheimer's Disease

Seshadri, S., Beiser, A., Selhub, J., Jacques, P. F., Rosenberg, I. H., D'Agostino, R. B., Wilson, P. W. F., & Wolf, P. A. (2002) · New England Journal of Medicine · doi:10.1056/nejmoa011613 · Cited by 3,237 · see citing works

Alzheimer Disease: An Update on Pathobiology and Treatment Strategies

Long, J. M., & Holtzman, D. M. (2019) · Cell · doi:10.1016/j.cell.2019.09.001 · Cited by 3,204 · see citing works

Excitatory Amino Acids as a Final Common Pathway for Neurologic Disorders

Epstein, F. H., Lipton, S. A., & Rosenberg, P. A. (1994) · New England Journal of Medicine · doi:10.1056/nejm199403033300907 · Cited by 2,644 · see citing works

Alzheimer's disease

Lane, C. A., Hardy, J., & Schott, J. M. (2018) · European Journal of Neurology · doi:10.1111/ene.13439 · Cited by 2,616 · see citing works

2020 Alzheimer's disease facts and figures

(2020) · Alzheimer's & Dementia · doi:10.1002/alz.12068 · Cited by 2,353 · see citing works

H ₂ S as a Physiologic Vasorelaxant: Hypertension in Mice with Deletion of Cystathionine γ-Lyase

Yang, G., Wu, L., Jiang, B., Yang, W., Qi, J., Cao, K., Meng, Q., Mustafa, A. K., Mu, W., Zhang, S., et al. (2008) · Science · doi:10.1126/science.1162667 · Cited by 2,310 · see citing works

Amyloid β deposition, neurodegeneration, and cognitive decline in sporadic Alzheimer's disease: a prospective cohort study

Villemagne, V. L., Burnham, S., Bourgeat, P., Brown, B., Ellis, K. A., Salvado, O., Szoeke, C., Macaulay, S. L., Martins, R., Maruff, P., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70044-9 · Cited by 2,279 · see citing works

The possible role of hydrogen sulfide as an endogenous neuromodulator

Abe, K., & Kimura, H. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-03-01066.1996 · Cited by 2,216 · see citing works

Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed

Wang, R. (2012) · Physiological Reviews · doi:10.1152/physrev.00017.2011 · Cited by 1,939 · see citing works

Oxidative Damage Is the Earliest Event in Alzheimer Disease

Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885 · see citing works

Alzheimer's disease

Masters, C. L., Bateman, R., Blennow, K., Rowe, C. C., Sperling, R. A., & Cummings, J. L. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.56 · Cited by 1,853 · see citing works

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · see citing works

Alzheimer’s disease drug-development pipeline: Few candidates, frequent failures

Cummings, J. L., Morstorf, T., & Zhong, K. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt269 · Cited by 1,744 · see citing works

Blockade of N -Methyl-D-Aspartate Receptors May Protect Against Ischemic Damage in the Brain

Simon, R. P., Swan, J. H., Griffiths, T., & Meldrum, B. S. (1984) · Science · doi:10.1126/science.6093256 · Cited by 1,682 · see citing works

Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro

Imlay, J. A., Chin, S. M., & Linn, S. (1988) · Science · doi:10.1126/science.2834821 · Cited by 1,555 · see citing works

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · see citing works

Folate, Vitamin B12, and Serum Total Homocysteine Levels in Confirmed Alzheimer Disease

Clarke, R., Smith, A. D., Jobst, K. A., Refsum, H., Sutton, L., & Ueland, P. M. (1998) · Archives of Neurology · doi:10.1001/archneur.55.11.1449 · Cited by 1,408 · see citing works

Alzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis

Karch, C. M., & Goate, A. M. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.05.006 · Cited by 1,357 · see citing works

The role of oxidative stress in neurodegenerative diseases

Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works

H 2 S Signals Through Protein S-Sulfhydration

Mustafa, A. K., Gadalla, M. M., Sen, N., Kim, S., Mu, W., Gazi, S. K., Barrow, R. K., Yang, G., Wang, R., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.2000464 · Cited by 1,235 · see citing works

The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction

Huang, X., Atwood, C., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., Cuajungco, M. P., Gray, D. N., Lim, J. T., Moir, R. D., et al. (1999) · Biochemistry · doi:10.1021/bi990438f · Cited by 1,107 · see citing works

3-Mercaptopyruvate Sulfurtransferase Produces Hydrogen Sulfide and Bound Sulfane Sulfur in the Brain

Shibuya, N., Tanaka, M., Yoshida, M., Ogasawara, Y., Togawa, T., Ishii, K., & Kimura, H. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2253 · Cited by 920 · see citing works

H2S signalling through protein sulfhydration and beyond

Paul, B. D., & Snyder, S. H. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3391 · Cited by 849 · see citing works

Neurotoxicity associated with dual actions of homocysteine at the N -methyl- d -aspartate receptor

Lipton, S. A., Kim, W.-K., Choi, Y., Kumar, S., D’Emilia, D. M., Posina, V. R., Arnelle, D. R., & Stamler, J. S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5923 · Cited by 845 · see citing works

Homocysteine Elicits a DNA Damage Response in Neurons That Promotes Apoptosis and Hypersensitivity to Excitotoxicity

Kruman, I. I., Culmsee, C., Chan, S. L., Kruman, Y., Guo, Z., Penix, L., & Mattson, M. P. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-18-06920.2000 · Cited by 784 · see citing works

Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762 · see citing works

Effect of 3-year folic acid supplementation on cognitive function in older adults in the FACIT trial: A randomised, double blind, controlled trial

Durga, J., van Boxtel, M. P., Schouten, E. G., Kok, F. J., Jolles, J., Katan, M. B., & Verhoef, P. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60109-3 · Cited by 758 · see citing works

Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 749 · see citing works

Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat

Stipanuk, M. H., & Beck, P. W. (1982) · Biochemical Journal · doi:10.1042/bj2060267 · Cited by 710 · see citing works

Oxidative stress in the progression of Alzheimer disease in the frontal cortex

Ansari, M. A., & Scheff, S. W. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181cb5af4 · Cited by 605 · see citing works

Duration of preclinical, prodromal, and dementia stages of Alzheimer's disease in relation to age, sex, and <i>APOE</i> genotype

Vermunt, L., Sikkes, S. A. M., van den Hout, A., Handels, R., Bos, I., van der Flier, W. M., Kern, S., Ousset, P., Maruff, P., Skoog, I., et al. (2019) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2019.04.001 · Cited by 570 · see citing works

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

Shibuya, N., Koike, S., Tanaka, M., Ishigami‐Yuasa, M., Kimura, Y., Ogasawara, Y., Fukui, K., Nagahara, N., & Kimura, H. (2013) · Nature Communications · doi:10.1038/ncomms2371 · Cited by 558 · see citing works

Homocysteine, B Vitamins, and Cognitive Impairment

Smith, A. D., & Refsum, H. (2016) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071715-050947 · Cited by 524 · see citing works

Mechanisms of homocysteine neurotoxicity in neurodegenerative diseases with special reference to dementia

Obeid, R., & Herrmann, W. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.04.088 · Cited by 490 · see citing works

Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse

Aoyama, K., Suh, S. W., Hamby, A. M., Liu, J., Chan, W. Y., Chen, Y., & Swanson, R. A. (2006) · Nature Neuroscience · doi:10.1038/nn1609 · Cited by 484 · see citing works

Vitamin B 12 , folate, and the methionine remethylation cycle—biochemistry, pathways, and regulation

Froese, D. S., Fowler, B., & Baumgartner, M. R. (2019) · Journal of Inherited Metabolic Disease · doi:10.1002/jimd.12009 · Cited by 479 · see citing works

Alzheimer's disease: the two-hit hypothesis.

Zhu, X.-W., Raina, A., Perry, G., & Smith, M. A. (2004) · Lancet Neurology · doi:10.1016/s1474-4422(04)00707-0 · Cited by 449 · see citing works

H 2 S-Induced Sulfhydration of the Phosphatase PTP1B and Its Role in the Endoplasmic Reticulum Stress Response

Krishnan, N., Fu, C., Pappin, D., & Tonks, N. K. (2011) · Science Signaling · doi:10.1126/scisignal.2002329 · Cited by 447 · see citing works

Cystathionine γ-lyase deficiency mediates neurodegeneration in Huntington’s disease

Paul, B. D., Sbodio, J. I., Xu, R., Vandiver, M. S., Cha, J. Y., Snowman, A. M., & Snyder, S. H. (2014) · Nature · doi:10.1038/nature13136 · Cited by 407 · see citing works

Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration

Živanović, J., Kouroussis, E., Kohl, J. B., Adhikari, B., Bursać, B. N., Schott-Roux, S., Petrovic, D., Miljković, J. L., Thomas‐López, D., Jung, Y., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.10.007 · Cited by 396 · see citing works

Homocysteine and Dementia: An International Consensus Statement

Smith, A. D., Refsum, H., Bottiglieri, T., Fenech, M. F., Hooshmand, B., McCaddon, A., Miller, J. W., Rosenberg, I. H., & Obeid, R. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171042 · Cited by 363 · see citing works

Cysteine Metabolism in Neuronal Redox Homeostasis

Paul, B. D., Sbodio, J. I., & Snyder, S. H. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2018.02.007 · Cited by 356 · see citing works

Hydrogen Sulfide Induces Cyclic AMP and Modulates the NMDA Receptor

Kimura, H. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1915 · Cited by 347 · see citing works

Sulfhydration mediates neuroprotective actions of parkin

Vandiver, M. S., Paul, B. D., Xu, R., Karuppagounder, S. S., Rao, F., Snowman, A. M., Ko, H. S., Lee, Y. I., Dawson, V. L., Dawson, T. M., et al. (2013) · Nature Communications · doi:10.1038/ncomms2623 · Cited by 343 · see citing works

Brain Glutathione Levels – A Novel Biomarker for Mild Cognitive Impairment and Alzheimer’s Disease

Mandal, P. K., Saharan, S., Tripathi, M., & Murari, G. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2015.04.005 · Cited by 339 · see citing works

Production of the Neuromodulator H2S by Cystathionine β-Synthase via the Condensation of Cysteine and Homocysteine

Chen, X., Jhee, K.-H., & Kruger, W. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400481200 · Cited by 330 · see citing works

Macromolecular synthesis inhibitors prevent oxidative stress-induced apoptosis in embryonic cortical neurons by shunting cysteine from protein synthesis to glutathione

Ratan, R., Murphy, T., & Baraban, J. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-07-04385.1994 · Cited by 285 · see citing works

Effects of hydrogen sulfide on mitochondrial function and cellular bioenergetics

Paul, B. D., Snyder, S. H., & Kashfi, K. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101772 · Cited by 283 · see citing works

Hydrogen sulfide is neuroprotective in Alzheimer’s disease by sulfhydrating GSK3β and inhibiting Tau hyperphosphorylation

Giovinazzo, D., Bursać, B. N., Sbodio, J. I., Nalluru, S., Vignane, T., Snowman, A. M., Albacarys, L. M., Sedlak, T. W., Torregrossa, R., Whiteman, M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017225118 · Cited by 273 · see citing works

Brain S‐Adenosylmethionine Levels Are Severely Decreased in Alzheimer's Disease

Morrison, L. D., Smith, D. D., & Kish, S. J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031328.x · Cited by 266 · see citing works

Hydrogen sulfide slows down progression of experimental Alzheimer’s disease by targeting multiple pathophysiological mechanisms

Giuliani, D., Ottani, A., Zaffe, D., Galantucci, M., Strinati, F., Lodi, R., & Guarini, S. (2013) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2013.05.006 · Cited by 254 · see citing works

Gasotransmitter hydrogen sulfide signaling in neuronal health and disease

Paul, B. D., & Snyder, S. H. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.11.019 · Cited by 254 · see citing works

Hypoxic regulation of the cerebral microcirculation is mediated by a carbon monoxide-sensitive hydrogen sulfide pathway

Morikawa, T., Kajimura, M., Nakamura, T., Hishiki, T., Nakanishi, T., Yukutake, Y., Nagahata, Y., Ishikawa, M., Hattori, K., Takenouchi, T., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119658109 · Cited by 250 · see citing works

Cystathionine β‐synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia/astrocyte lineage of developing mouse CNS

Enokido, Y., Suzuki, E., Iwasawa, K., Namekata, K., Okazawa, H., & Kimura, H. (2005) · The FASEB Journal · doi:10.1096/fj.05-3724fje · Cited by 238 · see citing works

Peripheral Oxidative Stress Biomarkers in Mild Cognitive Impairment and Alzheimer's Disease

Torres, L. H., Quaglio, N. B., de Souza, G. T., Garcia, R. C. T., Dati, L. M. M., Moreira, W. L., Loureiro, A. P. D. M., Souza‐Talarico, J. N., Smid, J., Porto, C. S., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110284 · Cited by 235 · 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

Elevated levels of homocysteine compromise blood-brain barrier integrity in mice

Kamath, A. F., Chauhan, A. K., Kisucka, J., Dole, V. S., Loscalzo, J., Handy, D. E., & Wagner, D. D. (2005) · Blood · doi:10.1182/blood-2005-06-2506 · Cited by 213 · see citing works

Brain oxidative stress: Detection and mapping of anti-oxidant marker ‘Glutathione’ in different brain regions of healthy male/female, MCI and Alzheimer patients using non-invasive magnetic resonance spectroscopy

Mandal, P. K., Tripathi, M., & Sugunan, S. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.047 · Cited by 201 · see citing works

Amyloid-β and τ serve antioxidant functions in the aging and Alzheimer brain

Smith, M. A., Casadesús, G., Joseph, J. A., & Perry, G. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01021-3 · Cited by 189 · see citing works

Is Metabolic Evidence for Vitamin B-12 and Folate Deficiency More Frequent in Elderly Patients With Alzheimer's Disease?

Joosten, E., Lesaffre, E. M. E. H., Riezler, R., Ghekiere, V., Dereymaeker, L., Pelemans, W., & Dejaeger, E. W. (1997) · The Journals of Gerontology Series A · doi:10.1093/gerona/52a.2.m76 · Cited by 187 · see citing works

Hypoxia, Oxidative Stress, and Inflammation: Three Faces of Neurodegenerative Diseases

Merelli, A., Repetto, M. G., Lazarowski, A., & Auzmendi, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-201074 · Cited by 182 · see citing works

Amyloid-β is an antioxidant for lipoproteins in cerebrospinal fluid and plasma

Kontush, A., Berndt, C., Weber, W., Akopyan, V., Arlt, S., Schippling, S., & Beisiegel, U. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00458-5 · Cited by 180 · see citing works

Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells

Su, B., Wang, X., Lee, H., Tabaton, M., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.010 · Cited by 178 · see citing works

Amyloid-β: an antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer’s disease

Kontush, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00688-8 · Cited by 176 · see citing works

Peripheral levels of glutathione and protein oxidation as markers in the development of Alzheimer's disease from Mild Cognitive Impairment

Bermejo‐Bescós, P., Martín‐Aragón, S., Benedı́, J., Susín, C., Felici, E., Gil, P., Ribera, J. M., & Villar, Á. (2008) · Free Radical Research · doi:10.1080/10715760701861373 · Cited by 167 · see citing works

Functional methionine synthase deficiency (cblE and cblG): Clinical and biochemical heterogeneity

Watkin, D., & Rosenblatt, D. S. (1989) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320340320 · Cited by 164 · see citing works

Hydrogen Sulfide Ameliorates Homocysteine-Induced Alzheimer’s Disease-Like Pathology, Blood–Brain Barrier Disruption, and Synaptic Disorder

Kamat, P. K., Kyles, P., Kalani, A., & Tyagi, N. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9212-4 · Cited by 163 · see citing works

Magnetic resonance spectroscopic analysis of Alzheimer's disease mouse brain that express mutant human APP shows altered neurochemical profile

Dedeoglu, A., Choi, J., Cormier, K., Kowall, N. W., & Jenkins, B. G. (2004) · Brain Research · doi:10.1016/j.brainres.2004.02.079 · Cited by 160 · see citing works

Antioxidants can inhibit basal autophagy and enhance neurodegeneration in models of polyglutamine disease

Underwood, B. R., Imarisio, S., Fleming, A., Rose, C., Krishna, G., Heard, P. L., Quick, M., Korolchuk, V. I., Renna, M., Sarkar, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq253 · Cited by 158 · see citing works

Oxidative Imbalance in Alzheimer's Disease

Zhu, X., Lee, H., Casadesús, G., Ávila, J., Drew, K. L., Perry, G. L., & Smith, M. A. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:205 · Cited by 146 · see citing works

Betaine attenuates Alzheimer‐like pathological changes and memory deficits induced by homocysteine

Chai, G., Jiang, X., Ni, Z.-F., Ma, Z., Xie, A., Cheng, X., Wang, Q., Wang, J., & Liu, G. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12094 · Cited by 144 · see citing works

Production of the gaseous signal molecule hydrogen sulfide in mouse tissues

Linden, D. R., Sha, L., Mazzone, A., Stoltz, G. J., Bernard, C. E., Furne, J. K., Levitt, M. D., Farrugia, G., & Szurszewski, J. H. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05502.x · Cited by 141 · see citing works

Plasma Homocysteine and Serum Folate and Vitamin B12 Levels in Mild Cognitive Impairment and Alzheimer’s Disease: A Case-Control Study

Ma, F., Wu, T., Zhao, J., Ji, L., Song, A., Zhang, M., & Huang, G. (2017) · Nutrients · doi:10.3390/nu9070725 · Cited by 130 · see citing works

Golgi stress response reprograms cysteine metabolism to confer cytoprotection in Huntington’s disease

Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1717877115 · Cited by 121 · see citing works

Molecular Basis of Alzheimer’s Disease: Focus on Mitochondria

Oliver, D. M. A., & Reddy, P. H. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190048 · Cited by 120 · see citing works

Neuronal failure in Alzheimer’s disease: a view through the oxidative stress looking-glass

Bonda, D., Wang, X., Lee, H., Smith, M. A., Perry, G. L., & Zhu, X. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1424-x · Cited by 113 · see citing works

ELEVATED HOMOCYSTEINE LEVELS IN ALCOHOL WITHDRAWAL

Bleich, S. (2000) · Alcohol and Alcoholism · doi:10.1093/alcalc/35.4.351 · Cited by 113 · see citing works

5,10‐Methylenetetrahydrofolate reductase 677C→T and 1298A→C mutations are genetic determinants of elevated homocysteine

Castro, R., Rivera, I. A., Ravasco, P., Jakobs, C., Blom, H. J., Camilo, M., & de Almeida, I. T. (2003) · QJM · doi:10.1093/qjmed/hcg039 · Cited by 108 · see citing works

S-Adenosylmethionine Is Decreased in the Cerebrospinal Fluid of Patients with Alzheimer’s Disease

Linnebank, M., Popp, J., Smulders, Y. M., Smith, D. E. C., Semmler, A., Farkas, M., Kulic, L., Cvetanovska, G., Blom, H. J., Stoffel‐Wagner, B., et al. (2010) · Neurodegenerative Diseases · doi:10.1159/000309657 · Cited by 103 · see citing works

Soluble Oligomers of Amyloid-β Cause Changes in Redox State, DNA Methylation, and Gene Transcription by Inhibiting EAAT3 Mediated Cysteine Uptake

Hodgson, N., Trivedi, M. S., Muratore, C., Li, S., & Deth, R. C. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130101 · Cited by 92 · see citing works

Age-Dependent and Tissue-Related Glutathione Redox Status in a Mouse Model of Alzheimer's Disease

Zhang, C., Rodríguez, C., Spaulding, J., Aw, T. Y., & Feng, J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111244 · Cited by 89 · see citing works

AP39, a Mitochondria‐Targeted Hydrogen Sulfide Donor, Supports Cellular Bioenergetics and Protects against Alzheimer’s Disease by Preserving Mitochondrial Function in APP/PS1 Mice and Neurons

Zhao, F., Fang, F., Qiao, P., Yan, N., Gao, D., & Yan, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/8360738 · Cited by 88 · see citing works

[Plasma levels of endogenous hydrogen sulfide and homocysteine in patients with Alzheimer's disease and vascular dementia and the significance thereof].

Xq, L., Liu, X.-Q., Jiang, P., Huang, H., & Yan, Y. (2008) · PubMed · Cited by 85 · see citing works

Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease

Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · cited 1× · see citing works

Gender differences in glutathione metabolism in Alzheimer's disease

Liu, H., Harrell, L. E., Shenvi, S. V., Hagen, T. M., & Liu, R.-M. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20424 · Cited by 83 · see citing works

Transcriptional control of amino acid homeostasis is disrupted in Huntington’s disease

Sbodio, J. I., Snyder, S. H., & Paul, B. D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608264113 · Cited by 82 · see citing works

Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)

Wang, J., & Hegele, R. A. (2003) · Human Genetics · doi:10.1007/s00439-003-0906-8 · Cited by 80 · see citing works

Modes of Physiologic H 2 S Signaling in the Brain and Peripheral Tissues

Paul, B. D., & Snyder, S. H. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5917 · Cited by 76 · see citing works

Cognitive Improvement with Glutathione Supplement in Alzheimer’s Disease: A Way Forward

Mandal, P. K., Shukla, D., Tripathi, M., & Ersland, L. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181054 · Cited by 76 · see citing works

Dietary Supplementation with S-Adenosyl Methionine Delayed Amyloid-β and Tau Pathology in 3xTg-AD Mice

Lee, S., Lemere, C. A., Frost, J. L., & Shea, T. B. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111025 · Cited by 68 · see citing works

Cystathionine γ-lyase: Clinical, metabolic, genetic, and structural studies

Kraus, J. P., Hašek, J., Kožich, V., Collard, R., Venezia, S., Janošı́ková, B., Wang, J., Stabler, S. P., Allen, R. H., Jakobs, C., et al. (2009) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2009.04.001 · Cited by 68 · see citing works

Hydrogen sulfide ameliorates learning memory impairment in APP/PS1 transgenic mice: A novel mechanism mediated by the activation of Nrf2

Liu, Y., Deng, Y., Liu, H., Yin, C., Li, X., & Gong, Q. (2016) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2016.11.002 · Cited by 68 · see citing works

Mechanisms of Hydrogen Sulfide against the Progression of Severe Alzheimer’s Disease in Transgenic Mice at Different Ages

Vandini, E., Ottani, A., Zaffe, D., Calevro, A., Canalini, F., Cavallini, G. M., Rossi, R., Guarini, S., & Giuliani, D. (2018) · Pharmacology · doi:10.1159/000494113 · Cited by 67 · see citing works

Sodium Hydrosulfide Attenuates Beta-Amyloid-Induced Cognitive Deficits and Neuroinflammation via Modulation of MAPK/NF-κB Pathway in Rats

Liu, H., Deng, Y., Gao, J., Liu, Y., Li, W., Shi, J., & Gong, Q. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666150713102326 · Cited by 65 · see citing works

Cystathionine β-synthase mutations: effect of mutation topology on folding and activity

Kožich, V., Sokolová, J., Klatovská, V., Krijt, J., Jánošík, M., Jelı́nek, K., & Kraus, J. P. (2010) · Human Mutation · doi:10.1002/humu.21273 · Cited by 64 · see citing works

Amyloid-β 42 Activates the Expression of BACE1 Through the JNK Pathway

Guglielmotto, M., Monteleone, D., Giliberto, L., Fornaro, M., Borghi, R., Tamagno, E., & Tabaton, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110884 · Cited by 63 · see citing works

S-Adenosylhomocysteine increases β-amyloid formation in BV-2 microglial cells by increased expressions of β-amyloid precursor protein and presenilin 1 and by hypomethylation of these gene promoters

Lin, H., Hsieh, H.-M., Chen, Y.-H., & Hu, M. (2009) · NeuroToxicology · doi:10.1016/j.neuro.2009.03.011 · Cited by 62 · see citing works

Early Detection and Prevention of Alzheimer’s Disease: Role of Oxidative Markers and Natural Antioxidants

Arslan, J., Jamshed, H., & Qureshi, H. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00231 · Cited by 62 · see citing works

Single nucleotide polymorphism in CTH associated with variation in plasma homocysteine concentration

Wang, J., Huff, A., Spence, J. D., & Hegele, R. A. (2004) · Clinical Genetics · doi:10.1111/j.1399-0004.2004.00250.x · Cited by 61 · see citing works

Detergent‐Insoluble EAAC1/EAAT3 Aberrantly Accumulates in Hippocampal Neurons of Alzheimer's Disease Patients

Duerson, K. C., Woltjer, R. L., Mookherjee, P., Leverenz, J. B., Montine, T. J., Bird, T. D., Pow, D. V., Rauen, T., & Cook, D. G. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00186.x · Cited by 60 · see citing works

Vitamin B-6 Deficiency Suppresses the Hepatic Transsulfuration Pathway but Increases Glutathione Concentration in Rats Fed AIN-76A or AIN-93G Diets

Lima, C. P., Davis, S. R., Mackey, A. D., Scheer, J. B., Williamson, J., & Gregory, J. F. (2006) · Journal of Nutrition · doi:10.1093/jn/136.8.2141 · Cited by 58 · see citing works

Relationship of Cognitive Function with B Vitamin Status, Homocysteine, and Tissue Factor Pathway Inhibitor in Cognitively Impaired Elderly: A Cross-Sectional Survey

Kim, G., Kim, H., Kim, K. N., Son, J. I., Kim, S. Y., Tamura, T., & Chang, N. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121345 · Cited by 56 · see citing works

Vitamin B6 nutritional status and cellular availability of pyridoxal 5′-phosphate govern the function of the transsulfuration pathway's canonical reactions and hydrogen sulfide production via side reactions

Gregory, J. F., DeRatt, B., Rios‐Avila, L., Ralat, M. A., & Stacpoole, P. W. (2016) · Biochimie · doi:10.1016/j.biochi.2015.12.020 · Cited by 56 · see citing works

B-vitamins reduce plasma levels of beta amyloid

Flicker, L. A., Martins, R. N., Thomas, J., Acres, J. M., Taddei, K., Vasikaran, S. D., Norman, P. E., Jamrozik, K. D., & Almeida, O. P. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.007 · Cited by 51 · see citing works

Homocysteine concentrations in the cognitive progression of Alzheimer's disease

Farina, N., Jernerén, F., Turner, C., Hart, K. H., & Tabet, N. (2017) · Experimental Gerontology · doi:10.1016/j.exger.2017.10.008 · Cited by 51 · see citing works

Altered Redox State in Whole Blood Cells from Patients with Mild Cognitive Impairment and Alzheimer’s Disease

Martínez de Toda, I., Miguélez, L., Vida, C., Carro, E., & De la Fuente, M. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190198 · Cited by 40 · see citing works

Hyperhomocysteinämie und B-Vitaminmangel bei neurologischen und psychiatrischen Erkrankungen

Herrmann, W., Lorenzl, S., & Obeid, R. (2007) · Fortschritte der Neurologie · Psychiatrie · doi:10.1055/s-2007-980112 · Cited by 38 · see citing works

GluN2B-containing NMDA receptors contribute to the beneficial effects of hydrogen sulfide on cognitive and synaptic plasticity deficits in APP/PS1 transgenic mice

Yang, Y., Zhao, Y. H., Yu, B., Xu, G., Wang, W., Zhan, J., Tang, Z., Wang, T., & Wei, B. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.08.033 · Cited by 30 · see citing works

Correlation Between Serum Homocysteine Levels and Outcome of Patients with Severe Traumatic Brain Injury

Rahmani, A., Hatefi, M., Dastjerdi, M. M., Zare, M., Imani, A., & Shirazi, D. (2015) · World Neurosurgery · doi:10.1016/j.wneu.2015.09.016 · Cited by 22 · see citing works

Betaine is as effective as folate at re-synthesizing methionine for protein synthesis during moderate methionine deficiency in piglets

McBreairty, L. E., Robinson, J. L., Harding, S., Randell, E. W., Brunton, J. A., & Bertolo, R. F. P. (2015) · Zeitschrift für Ernährungswissenschaft · doi:10.1007/s00394-015-1049-0 · Cited by 20 · see citing works

Homocysteine contribution to DNA damage in cystathionine β-synthase-deficient patients

Vanzin, C. S., Manfredini, V., Marinho, A. E., Biancini, G. B., Ribas, G. S., Deon, M., Wyse, Â. T. D. S., Wajner, M., & Vargas, C. R. (2014) · Gene · doi:10.1016/j.gene.2014.02.015 · Cited by 19 · see citing works

Plasma homocysteine in Alzheimer's disease with or without co-morbid depressive symptoms.

Kitzlerová, E., Fišar, Z., Jirák, R., Zvěřová, M., Hroudová, J., Benaková, H., & Raboch, J. (2014) · PubMed · Cited by 17 · see citing works

Impaired Lysosomal Cobalamin Transport in Alzheimer's Disease

Zhao, H., Li, H., Ruberu, K. R., & Garner, B. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140681 · Cited by 12 · see citing works

Impaired PLP-dependent metabolism in brain samples from Huntington disease patients and transgenic R6/1 mice

Sorolla, M. A., Colman, M. J. R., Vall‐llaura, N., Vived, C., Fernández‐Nogales, M., Lucas, J. J., Ferrer, I., & Cabiscol, E. (2015) · Metabolic Brain Disease · doi:10.1007/s11011-015-9777-7 · Cited by 12 · see citing works

Abnormal Amino Acid Profiles of Blood and Cerebrospinal Fluid from Cystathionine β-Synthase-Deficient Mice, an Animal Model of Homocystinuria

Akahoshi, N., Yokoyama, A., Nagata, T., Miura, A., Kamata, S., & Ishii, I. (2019) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b19-00127 · Cited by 10 · see citing works

Redox imbalance links COVID-19 and myalgic encephalomyelitis/chronic fatigue syndrome

Paul, B. D., Lemle, M. D., Komaroff, A. L., & Snyder, S. H. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2024358118 · Cited by 271 · see citing works

Glutathione: A Samsonian life-sustaining small molecule that protects against oxidative stress, ageing and damaging inflammation

Labarrere, C. A., & Kassab, G. S. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1007816 · Cited by 146 · see citing works

One-Carbon Metabolism: Pulling the Strings behind Aging and Neurodegeneration

Lionaki, E., Ploumi, C., & Tavernarakis, N. (2022) · Cells · doi:10.3390/cells11020214 · Cited by 110 · see citing works

Integrated multi-omics analysis of Alzheimer’s disease shows molecular signatures associated with disease progression and potential therapeutic targets

Kodam, P., Sai Swaroop, R., Pradhan, S. S., Sivaramakrishnan, V., & Vadrevu, R. (2023) · Scientific Reports · doi:10.1038/s41598-023-30892-6 · Cited by 82 · see citing works

Protective Roles of Hydrogen Sulfide in Alzheimer’s Disease and Traumatic Brain Injury

Paul, B. D., & Pieper, A. A. (2023) · Antioxidants · doi:10.3390/antiox12051095 · Cited by 59 · see citing works

Hydrogen sulfide signalling in neurodegenerative diseases

Tripathi, S. J., Chakraborty, S., Miller, E., Pieper, A. A., & Paul, B. D. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16170 · Cited by 59 · see citing works

Increased Risk of Aging-Related Neurodegenerative Disease after Traumatic Brain Injury

Barker, S., Paul, B. D., & Pieper, A. A. (2023) · Biomedicines · doi:10.3390/biomedicines11041154 · Cited by 54 · see citing works

Heavy Metals and Essential Metals Are Associated with Cerebrospinal Fluid Biomarkers of Alzheimer’s Disease

Leko, M. B., Mihelčić, M., Jurasović, J., Perković, M. N., Španić, E., Sekovanić, A., Orct, T., Zubčić, K., Horvat, L. L., Pleić, N., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms24010467 · Cited by 51 · see citing works

Cysteine metabolism and hydrogen sulfide signaling in Huntington’s disease

Paul, B. D. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.05.005 · Cited by 46 · see citing works

Activatable NIR-II Fluorescence Probe for Highly Sensitive and Selective Visualization of Glutathione <i>In Vivo</i>

Pan, Y., Lei, S., Zhang, J., Qu, J., Huang, P., & Lin, J. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.1c04504 · Cited by 45 · see citing works

Design strategies and applications of smart optical probes in the second near-infrared window

Chang, B., Chen, J., Bao, J., Dong, K., Chen, S., & Cheng, Z. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114637 · Cited by 43 · see citing works

Neuroprotective signaling by hydrogen sulfide and its dysregulation in Alzheimer's disease

Paul, B. D., & Pieper, A. A. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2024.102511 · Cited by 37 · see citing works

A critical appraisal of ferroptosis in Alzheimer’s and Parkinson’s disease: new insights into emerging mechanisms and therapeutic targets

Soni, P., Kaidery, N. A., Sharma, S. M., Gazaryan, I. G., Nikulin, S. V., Hushpulian, D. M., & Thomas, B. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1390798 · Cited by 34 · see citing works

Sulfanegen stimulates 3-mercaptopyruvate sulfurtransferase activity and ameliorates Alzheimer's disease pathology and oxidative stress in vivo

Rao, S. P., Xie, W., Kwon, Y. I. C., Juckel, N., Xie, J., Dronamraju, V., Vince, R., Lee, M. K., & More, S. S. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102484 · Cited by 28 · see citing works

Decreased Plasma Hydrogen Sulfide Level Is Associated With the Severity of Depression in Patients With Depressive Disorder

Yang, Y., Chen, C., Zhan, J., Liu, Q.-S., Liu, Y., Jiang, S.-Z., & Wei, B. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.765664 · Cited by 20 · see citing works

Is There a Connection between the Metabolism of Copper, Sulfur, and Molybdenum in Alzheimer’s Disease? New Insights on Disease Etiology

Coelho, F. C., Cerchiaro, G., Araújo, S. E. S., Daher, J. P. L., Cardoso, S. A., Coelho, G. F., & Guimarães, A. G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147935 · Cited by 19 · see citing works

Intranasal administration of induced pluripotent stem cell-derived cortical neural stem cell-secretome as a treatment option for Alzheimer’s disease

Mo, H., Kim, J., Kim, J. Y., Kim, J. W., Han, H., Choi, S. H., Rim, Y. A., & Ju, J. H. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00384-8 · Cited by 20 · see citing works

Gut microbiota–derived metabolite trimethylamine N-oxide alters the host epigenome through inhibition of S-adenosylhomocysteine hydrolase

Han, J. H., Rey, F. E., & Denu, J. M. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110521 · Cited by 20 · see citing works

Altered levels of variant cholinesterase transcripts contribute to the imbalanced cholinergic signaling in Alzheimer’s and Parkinson’s disease

Gök, M., Madrer, N., Zorbaz, T., Bennett, E. R., Greenberg, D., Bennett, D. A., & Soreq, H. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.941467 · Cited by 17 · see citing works

Development and application of a fluorescence turn-on probe for the nanomolar cysteine detection in serum and milk samples

Yeom, G. S., Song, I., Park, S. J., Kuwar, A., & Nimse, S. B. (2022) · Journal of Photochemistry and Photobiology A Chemistry · doi:10.1016/j.jphotochem.2022.114074 · Cited by 17 · see citing works

Organic small-molecule NIR-II fluorophores for tumor phototheranostics

Xiang, D., Wang, Z., Zheng, H., Tang, Y., & Li, Q. (2026) · Light: Science &amp; Applications · doi:10.1038/s41377-026-02212-w · Cited by 22 · see citing works

Transsulfuration pathway: a targeting neuromodulator in Parkinson’s disease

Corona-Trejo, A., Gonsebatt, M. E., Trejo‐Solís, C., Campos‐Peña, V., Granados, L. I. Q., Villegas‐Vázquez, E. Y., Reyes‐Hernández, O. D., Hernández-Abad, V. J., Figueroa‐González, G., & Silva‐Adaya, D. (2023) · Reviews in the Neurosciences · doi:10.1515/revneuro-2023-0039 · Cited by 16 · see citing works

Mitochondria-Microbiota Interaction in Neurodegeneration

Krämer, P. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.776936 · Cited by 14 · see citing works

Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration

Filipović, M. R. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00726 · Cited by 13 · see citing works

Cystathionine γ-lyase is a major regulator of cognitive function through neurotrophin signaling and neurogenesis

Chakraborty, S., Tripathi, S. J., Vázquez‐Rosa, E., Chaubey, K., Fujioka, H., Miller, E., Tyagi, R., Vignane, T., Sharma, S. M., Thomas, B., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2528478122 · Cited by 12 · see citing works

Methionine gamma lyase: Structure-activity relationships and therapeutic applications

Raboni, S., Faggiano, S., Bettati, S., & Mozzarelli, A. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140991 · Cited by 11 · see citing works

Natural sulfur compounds in mental health and neurological disorders: insights from observational and intervention studies

Rana, A., Katiyar, A., Arun, A., Berríos, J. A. N., & Kumar, G. (2025) · Frontiers in Nutrition · doi:10.3389/fnut.2025.1534000 · Cited by 11 · see citing works

Inositol polyphosphate multikinase modulates redox signaling through nuclear factor erythroid 2-related factor 2 and glutathione metabolism

Tyagi, R., Chakraborty, S., Tripathi, S. J., Jung, I., Kim, S. F., Snyder, S. H., & Paul, B. D. (2023) · iScience · doi:10.1016/j.isci.2023.107199 · Cited by 8 · see citing works

Formation of CSE-YAP complex drives FOXD3-mediated transition of neurotoxic astrocytes in Parkinson’s disease

Zhu, R., Chen, Y.-H., Xia, X., Liu, T., Wang, C., Cao, L., Liu, Y., & Lu, M. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107507 · Cited by 8 · see citing works

Neuroprotective effects of empagliflozin against scopolamine-induced memory impairment and oxidative stress in rats

Anoush, M., Taghaddosi, N., Hosseini, Z. B., Rahmati, F., Bijani, S., Kalantari‐Hesari, A., & Hosseini, M. (2025) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2025.01.008 · Cited by 8 · see citing works

Design, Synthesis, and Neuroprotective Effects of H2S-Donor-Peptide Hybrids on Hippocampal Neuronal Cells

Jeong, E. K., Selvaraj, B., Clovis, S., Son, Y. J., Park, T. H., Ashokkumar, V., Kim, H.-I., Yoo, K., Lee, J. W., & Park, C. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.12.012 · Cited by 8 · see citing works

Reconnecting the roots of hydrogen sulfide (H2S) with medicinal chemistry: Lessons accomplished and challenges so far

Chahat, Kumar, B., Gupta, S., Wahajuddin, M., & Joshi, G. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108569 · Cited by 6 · see citing works

In silico metabolic modelling links microbiome-derived metabolites to risk factors of Alzheimer’s disease

Hensen, T., Ahmad, S., Kastenmüller, G., Kraaij, R., Ghanbari, M., Ikram, M. A., Kaddurah-Daouk, R. F., & Thiele, I. (2024) · Gut Microbes Reports · doi:10.1080/29933935.2024.2443171 · Cited by 5 · see citing works

Protein S-sulfhydration: Mechanisms and therapeutic implications in Alzheimer's disease and Parkinson's disease

Jinfen, G., Shi, C., Yu, C., Wang, Y., & He, M. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.01.033 · Cited by 4 · see citing works

7,8-Dihydroxyflavone is a direct inhibitor of human and murine pyridoxal phosphatase

Brenner, M., Zink, C., Witzinger, L., Keller, A., Hadamek, K., Bothe, S., Neuenschwander, M., Villmann, C., von Kries, J. P., Schindelin, H., et al. (2024) · eLife · doi:10.7554/elife.93094 · Cited by 4 · see citing works

The potential role of hydrogen sulfide-autophagy axis in diseases

Chu, T., Wang, Y.-W., Cao, L., Wang, X., Fan, Y.-Q., Chen, Y., Zhang, Y., Si, W.-R., Jiang, Q., & Wu, D. (2025) · Journal of Physiology and Biochemistry · doi:10.1007/s13105-025-01128-0 · Cited by 2 · see citing works

Aberrant Hydrogen Sulfide Signaling in A lzheimer's Disease

Paul, B. D. (2022) · doi:10.1002/9781119799900.ch18

Trypanosoma brucei proliferates normally even after losing all S-adenosylhomocysteine hydrolase genes

Nakanishi, M., Hino, M., & Nomoto, H. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.149152

7,8-Dihydroxyflavone is a direct inhibitor of pyridoxal phosphatasePreprint

Zink, C., Witzinger, L., Keller, A., Hadamek, K., Bothe, S., Neuenschwander, M., Villmann, C., von Kries, J. P., Schindelin, H., Jeanclos, E. M., et al. (2024) · eLife · doi:10.7554/elife.93094.1

7,8-Dihydroxyflavone is a direct inhibitor of pyridoxal phosphatasePreprint

Brenner, M., Zink, C., Witzinger, L., Keller, A., Hadamek, K., Bothe, S., Neuenschwander, M., Villmann, C., von Kries, J. P., Schindelin, H., et al. (2023) · eLife · doi:10.1101/2023.10.04.560852

7,8-Dihydroxyflavone is a direct inhibitor of human and murine pyridoxal phosphatase

Brenner, M., Zink, C., Witzinger, L., Keller, A., Hadamek, K., Bothe, S., Neuenschwander, M., Villmann, C., von Kries, J. P., Schindelin, H., et al. (2024) · eLife · doi:10.7554/elife.93094.3

Additional file 1 of Intranasal administration of induced pluripotent stem cell-derived cortical neural stem cell-secretome as a treatment option for Alzheimer’s disease

Mo, H., Kim, J., Kim, J. Y., Kim, J. W., Han, H., Choi, S. H., Rim, Y. A., & Ju, J. H. (2023) · Figshare · doi:10.6084/m9.figshare.24540589

Early Amyloid-β Toxicity Disrupts Nervous System Connectivity During Aging in Caenorhabditis elegansPreprint

Yadav, D. K., Connor, C. W., & Gabel, C. V. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.27.740981

A disease-modifying treatment for Alzheimer’s disease: focus on the trans-sulfuration pathway

Berry, T. M., Hamza, E. A., & Moustafa, A. A. (2019) · Reviews in the Neurosciences · doi:10.1515/revneuro-2019-0076 · Cited by 14 · see citing works

Mammalian Sulfur Amino Acid Metabolism: A Nexus Between Redox Regulation, Nutrition, Epigenetics, and Detoxification

Pajares, M. A., & Pérez‐Sala, D. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7237 · Cited by 48 · see citing works

S-Adenosylmethionine Alleviates Amyloid-β-Induced Neural Injury by Enhancing Trans-Sulfuration Pathway Activity in Astrocytes

Wan, X., Ma, B., Wang, X., Guo, C., Sun, J., Cui, J., & Li, L. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200103 · Cited by 14 · see citing works

Protein persulfidation: The missing link in Alzheimer's disease defense mechanisms

Ma, Y., Huang, X., Xia, Y., Song, P., & Hu, X. (2026) · Drug Discoveries & Therapeutics · doi:10.5582/ddt.2026.01004

Posttranslational Regulation of Mammalian Sulfur Amino Acid Metabolism

Pajares, M. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26062488 · Cited by 9 · see citing works