Nitric oxide S -nitrosylates serine racemase, mediating feedback inhibition of d -serine formation
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Serine racemase (SR) generates D-serine, a coagonist with glutamate at NMDA receptors. We show that SR is physiologically S-nitrosylated leading to marked inhibition of enzyme activity. Inhibition involves interactions with the cofactor ATP reflecting juxtaposition of the ATP-binding site and cysteine-113 (C113), the site for physiological S-nitrosylation. NMDA receptor physiologically enhances SR S-nitrosylation by activating neuronal nitric-oxide synthase (nNOS). These findings support a model whereby postsynaptic stimulation of nitric-oxide (NO) formation feeds back to presynaptic cells to S-nitrosylate SR and decrease D-serine availability to postsynaptic NMDA receptors.
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Several proteins related to glutamatergic neurotransmission contain modulatory redox sites, including glutamine synthase, serine racemase, and NMDARs.
“Several proteins related to glutamatergic neurotransmission contain modulatory redox sites, including glutamine synthase (Mustafa et al., 2007), serine racemase (responsible for synthesis of glycine, a NMDAR co-agonist, (Pinteaux et al., 1996)), and NMDARs (Choi et al., 2001).”
From Redox dysregulation, neuroinflammation, and NMDA receptor hypofunction: A “central hub” in schizophrenia pathophysiology? (2016) · cites this paper as Mustafa et al., 2007
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A synaptic model of memory: long-term potentiation in the hippocampus
Bliss, T. V. P., & Collingridge, G. L. (1993) · Nature · doi:10.1038/361031a0 · Cited by 11,566 · see citing works
Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.
Bredt, D. S., & Snyder, S. H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.2.682 · Cited by 3,308 · see citing works
Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
Bredt, D. S., Hwang, P. M., Glatt, C. E., Lowenstein, C. J., Reed, R. R., & Snyder, S. H. (1991) · Nature · doi:10.1038/351714a0 · Cited by 2,354 · see citing works
Nitric oxide mediates glutamate-linked enhancement of cGMP levels in the cerebellum.
Bredt, D. S., & Snyder, S. H. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.9030 · Cited by 1,849 · see citing works
Boehning, D. F., & Snyder, S. H. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131047 · Cited by 1,235 · see citing works
D-serine is an endogenous ligand for the glycine site of the N-methyl-D-aspartate receptor.
Mothet, J., Parent, A., Wolosker, H., Brady, R., Linden, D. J., Ferris, C., Rogawski, M., & Snyder, S. (2000) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.97.9.4926 · Cited by 1,164 · see citing works
Glia-Derived d-Serine Controls NMDA Receptor Activity and Synaptic Memory
Panatier, A., Theodosis, D. T., Mothet, J.-P., Touquet, B., Pollegioni, L., Poulain, D. A., & Oliet, S. H. R. (2006) · Cell · doi:10.1016/j.cell.2006.02.051 · Cited by 934 · see citing works
Wolosker, H., Blackshaw, S., & Snyder, S. H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.23.13409 · Cited by 811 · see citing works
(S)NO Signals: Translocation, Regulation, and a Consensus Motif
Stamler, J. S., Toone, E. J., Lipton, S. A., & Sucher, N. J. (1997) · Neuron · doi:10.1016/s0896-6273(00)80310-4 · Cited by 674 · see citing works
Arancio, O., Kiebler, M., Lee, C. J., Lev-Ram, V., Tsien, R. Y., Kandel, E. R., & Hawkins, R. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81797-3 · Cited by 357 · see citing works
Neuron-derived D-Serine Release Provides a Novel Means to Activate N-Methyl-D-aspartate Receptors
Kartvelishvily, E., Shleper, M., Balan, L., Dumin, E., & Wolosker, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512927200 · Cited by 277 · see citing works
Miranda, J. D., Panizzutti, R., Foltyn, V. N., & Wolosker, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222421299 · Cited by 221 · see citing works
Serine Racemase Modulates Intracellular D-Serine Levels through an α,β-Elimination Activity
Foltyn, V. N., Bendikov, I., Miranda, J. D., Panizzutti, R., Dumin, E., Shleper, M., Li, P., Toney, M. D., Kartvelishvily, E., & Wolosker, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405726200 · Cited by 219 · see citing works
Erwin, P. A., Lin, A. J., Golan, D. E., & Michel, T. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413058200 · Cited by 215 · see citing works
Kim, P. M., Aizawa, H., Kim, P. S., Huang, A. S., Wickramasinghe, S. R., Kashani, A., Barrow, R., Huganir, R., Ghosh, A., & Snyder, S. (2005) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0409723102 · Cited by 214 · see citing works
Silver, I. A., Deas, J., & Erecińska, M. (1997) · Neuroscience · doi:10.1016/s0306-4522(96)00600-8 · Cited by 206 · see citing works
Kluge, I., Gutteck‐Amsler, U., Zollinger, M., & Kim, Q. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69062599.x · Cited by 174 · see citing works
IV. Nitric oxide synthase gene knockout mice
Mashimo, H. L., & Goyal, R. K. (1999) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.1999.277.4.g745 · Cited by 140 · see citing works
Retrograde messengers, long-term potentiation and memory
MEDINA, J., & Izquierdo, I. (1995) · Brain Research Reviews · doi:10.1016/0165-0173(95)00013-5 · Cited by 123 · see citing works
Regulation of serine racemase activity by d-serine and nitric oxide in human glioblastoma cells
Shoji, K., Mariotto, S., Ciampa, A. R., & Suzuki, H. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.08.063 · Cited by 39 · see citing works
Mutual regulation between serine and nitric oxide metabolism in human glioblastoma cells
Shoji, K., Mariotto, S., Ciampa, A. R., & Suzuki, H. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.10.064 · Cited by 29 · see citing works
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Ketamine-Induced Loss of Phenotype of Fast-Spiking Interneurons Is Mediated by NADPH-Oxidase
Behrens, M. M., Ali, S. S., Dao, D. N., Lucero, J., Shekhtman, G., Quick, K. L., & Dugan, L. L. (2007) · Science · doi:10.1126/science.1148045 · Cited by 585 · see citing works
Mustafa, A. K., Gadalla, M. M., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.268re2 · Cited by 491 · see citing works
S-nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons
Nott, A., Watson, P. M., Robinson, J. D., Crepaldi, L., & Riccio, A. (2008) · Nature · doi:10.1038/nature07238 · Cited by 429 · see citing works
Redox Signaling Mediated by Thioredoxin and Glutathione Systems in the Central Nervous System
Ren, X., Zou, L., Zhang, X., Branco, V., Wang, J., Carvalho, C. M. L., Holmgren, A., & Lu, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6925 · Cited by 365 · see citing works
Aberrant Protein S-Nitrosylation in Neurodegenerative Diseases
Nakamura, T., Tu, S., Akhtar, M. W., Sunico, C. R., Okamoto, S., & Lipton, S. A. (2013) · Neuron · doi:10.1016/j.neuron.2013.05.005 · Cited by 355 · see citing works
Detection of protein S-nitrosylation with the biotin-switch technique
Forrester, M. T., Foster, M. W., Benhar, M., & Stamler, J. S. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.09.034 · Cited by 298 · see citing works
Steullet, P., Cabungcal, J. H., Monin, A., Dwir, D., O'Donnell, P., Cuenod, M., & Do, K. Q. (2016) · Schizophrenia Research · doi:10.1016/j.schres.2014.06.021 · Cited by 262 · see citing works
Serine racemase is predominantly localized in neurons in mouse brain
Miya, K., Inoue, R., Takata, Y., Abe, M., Natsume, R., Sakimura, K., Hongou, K., Miyawaki, T., & Mori, H. (2008) · The Journal of Comparative Neurology · doi:10.1002/cne.21822 · Cited by 243 · see citing works
Interleukin-6 Mediates the Increase in NADPH-Oxidase in the Ketamine Model of Schizophrenia
Behrens, M. M., Ali, S. S., & Dugan, L. L. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4457-08.2008 · Cited by 241 · see citing works
NMDA- and β-Amyloid1–42-Induced Neurotoxicity Is Attenuated in Serine Racemase Knock-Out Mice
Inoue, R., Hashimoto, K., Harai, T., & Mori, H. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.5034-08.2008 · Cited by 171 · see citing works
Behrens, M. M., & B, T. J. S. A. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.06.002 · Cited by 160 · see citing works
Serine racemase and the serine shuttle between neurons and astrocytes
Wolosker, H. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.01.001 · Cited by 163 · see citing works
M, T., Abazyan, S., Abazyan, B. N., Nomura, J., Yang, C., Seshadri, S., Sawa, A., Snyder, S. H., & Pletnikov, M. V. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.97 · Cited by 151 · see citing works
Regulation of N-methyl-d-aspartate receptors by astrocytic d-serine
Oliet, S. H. R., & Mothet, J. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.071 · Cited by 149 · see citing works
Drug Discovery Targeting Amino Acid Racemases
Conti, P., Tamborini, L., Pinto, A., Blondel, A., Minoprio, P. M. C., Mozzarelli, A., & Micheli, C. D. (2011) · Chemical Reviews · doi:10.1021/cr2000702 · Cited by 142 · see citing works
D-Serine: Potential Therapeutic Agent and/or Biomarker in Schizophrenia and Depression?
MacKay, M.-A. B., Kravtsenyuk, M., Thomas, R. K., Mitchell, N., Dursun, S. M., & Baker, G. B. (2019) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2019.00025 · Cited by 128 · see citing works
Metabolism of the neuromodulator d-serine
Pollegioni, L., & Sacchi, S. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0307-9 · Cited by 128 · see citing works
Regulation of brain glutamate metabolism by nitric oxide and S-nitrosylation
Raju, K., Doulias, P., Evans, P., Krizman, E. N., Jackson, J. G., Horyn, O., Daikhin, Y., Nissim, I. B., Yudkoff, M., Nissim, I., et al. (2015) · Science Signaling · doi:10.1126/scisignal.aaa4312 · Cited by 124 · see citing works
Contributions of the d-serine pathway to schizophrenia
Labrie, V., Wong, A. H. C., & Roder, J. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.030 · Cited by 118 · see citing works
Cattane, N., Richetto, J., & Cattaneo, A. (2018) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2018.07.001 · Cited by 118 · see citing works
Labrie, V., & Roder, J. (2009) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2009.08.002 · Cited by 116 · see citing works
Nakamura, T., Cho, D., & Lipton, S. A. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.032 · Cited by 113 · see citing works
Serine Racemase Deletion Protects Against Cerebral Ischemia and Excitotoxicity
Mustafa, A. K., Ahmad, A. S., Zeynalov, E., Gazi, S. K., Sikka, G., Ehmsen, J. T., Barrow, R. K., Coyle, J. T., Snyder, S. H., & Doré, S. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4297-09.2010 · Cited by 110 · see citing works
Cell-type specific mechanisms of D-serine uptake and release in the brain
Martineau, M., Parpura, V., & Mothet, J. (2014) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2014.00012 · Cited by 108 · see citing works
Redox Signaling in Neurotransmission and Cognition During Aging
Kumar, A., Yegla, B., & Foster, T. C. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7111 · Cited by 104 · see citing works
Wolosker, H., & Balu, D. T. (2020) · Translational Psychiatry · doi:10.1038/s41398-020-00870-x · Cited by 102 · see citing works
Ohide, H., Miyoshi, Y., Maruyama, R., Hamase, K., & Konno, R. (2011) · Journal of Chromatography B · doi:10.1016/j.jchromb.2011.06.028 · Cited by 96 · see citing works
Turpin, F. R., Potier, B., Dulong, J., Sinet, P., Alliot, J., Oliet, S. H. R., Dutar, P., Epelbaum, J., Mothet, J., & Billard, J. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.09.001 · Cited by 95 · see citing works
Haxaire, C., Turpin, F. R., Potier, B., Kervern, M., Sinet, P., Barbanel, G., Mothet, J., Dutar, P., & Billard, J. (2012) · Aging Cell · doi:10.1111/j.1474-9726.2012.00792.x · Cited by 88 · see citing works
Encoding of the cough reflex in anesthetized guinea pigs
Canning, B. J., & Mori, N. (2010) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00044.2010 · Cited by 85 · see citing works
Wolosker, H., & Radzishevsky, I. S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130220 · Cited by 84 · see citing works
Central regulation of the cough reflex: Therapeutic implications
Canning, B. J. (2009) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2009.01.003 · Cited by 84 · see citing works
Nitric Oxide Signaling and Nitrosative Stress in Neurons: Role for S -Nitrosylation
Shahani, N., & Sawa, A. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3580 · Cited by 79 · see citing works
Balan, L., Foltyn, V. N., Zehl, M., Dumin, E., Dikopoltsev, E., Knoh, D., Ohno, Y., Kihara, A., Jensen, O. N., Radzishevsky, I. S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809442106 · Cited by 74 · see citing works
Serine racemase: an unconventional enzyme for an unconventional transmitter
Wolosker, H., & Mori, H. (2012) · Amino Acids · doi:10.1007/s00726-012-1370-3 · Cited by 67 · see citing works
The Neurobiology of d -Serine Signaling
Wolosker, H. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.08.010 · Cited by 65 · see citing works
Glutamatergic regulation of serine racemase via reversal of PIP2 inhibition
Mustafa, A. K., van Rossum, D. B., Patterson, R. L., Maag, D., Ehmsen, J. T., Gazi, S. K., Chakraborty, A., Barrow, R. K., Amzel, L. M., & Snyder, S. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813105106 · Cited by 64 · see citing works
Xu, L., Han, C. L., Lim, K., & Wu, T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.a115.705709 · Cited by 60 · see citing works
RetractedActivation of Cytosolic Phospholipase A2α through Nitric Oxide-induced S-Nitrosylation
Xu, L., Han, C. L., Lim, K., & Wu, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705709200 · Cited by 59 · see citing works
RetractedSNO-ing at the Nociceptive Synapse?
Tegeder, I., Scheving, R., Wittig, I., & Geißlinger, G. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.004200 · Cited by 57 · see citing works
Dun, Y., Duplantier, J., Roon, P., Martin, P. M., Ganapathy, V., & Smith, S. B. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05015.x · Cited by 56 · see citing works
Protein modifications involved in neurotransmitter and gasotransmitter signaling
Sen, N., & Snyder, S. H. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.07.004 · Cited by 53 · see citing works
Inhibition of Human Serine Racemase, an Emerging Target for Medicinal Chemistry
Jirásková-Vaníčková, J., Ettrich, R. H., Vorlová, B., Hoffman, H. E., Lepšı́k, M., Jansa, P., & Konvalinka, J. (2011) · Current Drug Targets · doi:10.2174/138945011795677755 · Cited by 53 · see citing works
Maucler, C., Pernot, P., Vasylieva, N., Pollegioni, L., & Marinesco, S. (2013) · ACS Chemical Neuroscience · doi:10.1021/cn4000549 · Cited by 52 · see citing works
d ‐Amino acids in the brain: the biochemistry of brain serine racemase
Baumgart, F., & Rodríguez‐Crespo, I. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06517.x · Cited by 51 · see citing works
Nitric oxide-mediated modulation of calcium/calmodulin-dependent protein kinase II
Song, T., Hatano, N., Kambe, T., Miyamoto, Y., Ihara, H., Yamamoto, H., Sugimoto, K., Kume, K., Yamaguchi, F., Tokuda, M., et al. (2008) · Biochemical Journal · doi:10.1042/bj20071195 · Cited by 50 · see citing works
Bodner, O., Radzishevsky, I., Foltyn, V. N., Touitou, A., Valenta, A. C., Rangel, I. F., Panizzutti, R., Kennedy, R. T., Billard, J. M., & Wolosker, H. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.0801-20.2020 · Cited by 49 · see citing works
Zoubovsky, S. P., Pogorelov, V. M., Taniguchi, Y., Kim, S.-H., Yoon, P., Nwulia, E. A., Sawa, A., Pletnikov, M. V., & Kamiya, A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.097 · Cited by 48 · see citing works
Suzuki, M., Sasabe, J., Miyoshi, Y., Kuwasako, K., Muto, Y., Hamase, K., Matsuoka, M., Imanishi, N., & Aiso, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1416117112 · Cited by 48 · see citing works
Wang, X., Pinto-Duarte, A., Sejnowski, T. J., & Behrens, M. M. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4907 · Cited by 46 · see citing works
Cerebrospinal fluid biomarker candidates of schizophrenia: where do we stand?
Vasić, N., Connemann, B. J., Wolf, R. C., Tumani, H., & Brettschneider, J. (2011) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/s00406-011-0280-9 · Cited by 46 · see citing works
Serine Racemase Regulated by Binding to Stargazin and PSD-95
Ma, T. M., Paul, B. D., Fu, C., Hu, S., Zhu, H., Blackshaw, S., Wolosker, H., & Snyder, S. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.571604 · Cited by 44 · see citing works
Billard, J. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00315.x · Cited by 43 · see citing works
d-serine in physiological and pathological brain aging
Ploux, E., Fréret, T., & Billard, J. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140542 · Cited by 42 · see citing works
d-Serine in the aging hippocampus
Billard, J. (2015) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2015.02.013 · Cited by 41 · see citing works
Zaręba-Kozioł, M., Szwajda, A., Dadlez, M., Wysłouch-Cieszyńska, A., & Lalowski, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036079 · Cited by 39 · see citing works
“(28), and serine racemase (29), has been related to severe”
BackgroundBortolanza, M., Bariotto‐dos‐Santos, K., Pereira, M. D. S., da-Silva, C. A., & Bel, E. A. D. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9618-4 · Cited by 38 · see citing works
d-Serine: The right or wrong isoform?
Fuchs, S. A., Berger, R., & de Koning, T. J. (2011) · Brain Research · doi:10.1016/j.brainres.2011.05.039 · Cited by 36 · see citing works
The Energy Landscape of Human Serine Racemase
Raboni, S., Marchetti, M., Faggiano, S., Campanini, B., Bruno, S., Marchesani, F., Margiotta, M., & Mozzarelli, A. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00112 · Cited by 37 · see citing works
Protein kinase C activity regulates d-serine availability in the brain
Vargas-Lopes, C., Madeira, C., Kahn, S. A., do Couto, I. A., Bado, P., Houzel, J., Miranda, J. D., de Freitas, M. S., Ferreira, S. T., & Panizzutti, R. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07102.x · Cited by 36 · see citing works
The plastic d-serine signaling pathway: Sliding from neurons to glia and vice-versa
Ivanov, A. D., & Mothet, J. (2018) · Neuroscience Letters · doi:10.1016/j.neulet.2018.05.039 · Cited by 34 · see citing works
Serine racemase as a prime target for age‐related memory deficits
Billard, J. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12226 · Cited by 34 · see citing works
Li, Y., Wu, P., Chen, J., Wang, S., Han, Q.-Q., Li, D., Wang, W., Guan, X., Li, D., Long, L., et al. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6936 · Cited by 33 · see citing works
Takarada, T., Takahata, Y., Takarada‐Iemata, M., Hinoi, E., Uno, K., Hirai, T., Yamamoto, T. M., & Yoneda, Y. (2009) · Journal of Cellular Physiology · doi:10.1002/jcp.21821 · Cited by 33 · see citing works
Mori, H., & Inoue, R. (2010) · Chemistry & Biodiversity · doi:10.1002/cbdv.200900293 · Cited by 33 · see citing works
ATP binding to human serine racemase is cooperative and modulated by glycine
Marchetti, M., Bruno, S., Campanini, B., Peracchi, A., Mai, N., & Mozzarelli, A. (2013) · FEBS Journal · doi:10.1111/febs.12510 · Cited by 33 · see citing works
Glycine site agonists of the N‐methyl‐ d ‐aspartate receptor and Parkinson's disease: A hypothesis
Heresco‐Levy, U., Shoham, S., & Javitt, D. C. (2013) · Movement Disorders · doi:10.1002/mds.25306 · Cited by 33 · see citing works
d -serine and schizophrenia: an update
Nunes, E. A., MacKenzie, E. M., Rossolatos, D., Perez-Parada, J., Baker, G. B., & Dursun, S. M. (2012) · Expert Review of Neurotherapeutics · doi:10.1586/ern.12.65 · Cited by 32 · see citing works
Modulation of Ionotropic Glutamate Receptors and Acid-Sensing Ion Channels by Nitric Oxide
Wang, J. Q., Chu, X., Guo, M., Jin, D.-Z., Xue, B., Berry, T. J., Fibuch, E. E., & Mao, L. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00164 · Cited by 30 · see citing works
Methods for detection and characterization of protein S-nitrosylation
Chen, Y., Ching, W.-C., Lin, Y., & Chen, Y. (2013) · Methods · doi:10.1016/j.ymeth.2013.04.016 · Cited by 28 · see citing works
Serine racemase: a key player in apoptosis and necrosis
Canu, N., Ciotti, M. T., & Pollegioni, L. (2014) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2014.00009 · Cited by 28 · see citing works
Jiang, H., Wu, M., Liu, Y., Song, L., Li, S., Wang, X., Zhang, Y. F., Fang, J., & Wu, S. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14214 · Cited by 28 · see citing works
Billard, J. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00106 · Cited by 28 · see citing works
S‐nitrosation and neuronal plasticity
Santos, A. I., Martı́nez-Ruiz, A., & Araújo, I. M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12827 · Cited by 25 · see citing works
Serine racemase suppresses chondrogenic differentiation in cartilage in a Sox9‐dependent manner
Takarada, T., Hinoi, E., Takahata, Y., & Yoneda, Y. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21310 · Cited by 25 · see citing works
Acuña, L. R., Back, F., Barp, C. G., Bortoloci, J. G. T., Assreuy, J., & Carobrez, A. P. (2023) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2023.107735 · Cited by 24 · see citing works
Nuclear Compartmentalization of Serine Racemase Regulates d-Serine Production
Kolodney, G., Dumin, E., Safory, H., Rosenberg, D., Mori, H., Radzishevsky, I. S., & Wolosker, H. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.699496 · Cited by 24 · see citing works
Sikka, P., Walker, R. M., Cockayne, R., Wood, M. J. A., Harrison, P. J., & Burnet, P. W. J. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22332 · Cited by 23 · see citing works
Retinal NMDA receptor function and expression are altered in a mouse lacking d -amino acid oxidase
Gustafson, E. C., Morgans, C. W., Tekmen, M., Sullivan, S. J., Esguerra, M., Konno, R., & Miller, R. F. (2013) · Journal of Neurophysiology · doi:10.1152/jn.00310.2013 · Cited by 22 · see citing works
Regulation of human serine racemase activity and dynamics by halides, ATP and malonate
Marchetti, M., Bruno, S., Campanini, B., Bettati, S., Peracchi, A., & Mozzarelli, A. (2014) · Amino Acids · doi:10.1007/s00726-014-1856-2 · Cited by 22 · see citing works
Metal ion dependency of serine racemase from Dictyostelium discoideum
Ito, T., Murase, H., Maekawa, M., Goto, M., Hayashi, S., Saito, H., Maki, M., Hemmi, H., & Yoshimura, T. (2012) · Amino Acids · doi:10.1007/s00726-012-1232-z · Cited by 21 · see citing works
Jonkman, K., van der Schrier, R. M., van Velzen, M., Aarts, L. P. H. J., Olofsen, E., Sarton, E. Y., Niesters, M., & Dahan, A. (2018) · British Journal of Anaesthesia · doi:10.1016/j.bja.2018.01.022 · Cited by 21 · see citing works
Femmer, C., Bechtold, M., Roberts, T. M., & Panke, S. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-7729-8 · Cited by 20 · see citing works
Osteoclastogenesis is negatively regulated by D ‐serine produced by osteoblasts
Takarada, T., Takarada‐Iemata, M., Takahata, Y., Yamada, D., Yamamoto, T. M., Nakamura, Y., Hinoi, E., & Yoneda, Y. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.24048 · Cited by 19 · see citing works
Dikopoltsev, E., Foltyn, V. N., Zehl, M., Jensen, O. N., Mori, H., Radzishevsky, I. S., & Wolosker, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.618405 · Cited by 17 · see citing works
der Auwera, S. V., Teumer, A., Hertel, J., Homuth, G., Völker, U., Lucht, M. J., Degenhardt, F., Schulze, T. G., Rietschel, M., Nöthen, M. M., et al. (2016) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2016.03.019 · Cited by 15 · see citing works
田端, 彩., Inoue, R., & Mori, H. (2014) · PLoS ONE · doi:10.1371/journal.pone.0105282 · Cited by 15 · see citing works
Serine Racemase Expression Differentiates Aging from Alzheimer’s Brain
Wu, S., Zhou, J., Zhang, H., & Barger, S. W. (2022) · Current Alzheimer Research · doi:10.2174/1567205019666220805105106 · Cited by 14 · see citing works
Cross‐linking of serine racemase dimer by reactive oxygen species and reactive nitrogen species
Wang, W., & Barger, S. W. (2012) · Journal of Neuroscience Research · doi:10.1002/jnr.22832 · Cited by 14 · see citing works
Roles of quaternary structure and cysteine residues in the activity of human serine racemase
Wang, W., & Barger, S. W. (2011) · BMC Biochemistry · doi:10.1186/1471-2091-12-63 · Cited by 14 · see citing works
Yamagata, K., Yamamoto, M., Kawakami, K., Ohara, H., & Nabika, T. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.02.039 · Cited by 13 · see citing works
Zhang, H., Kuang, X., Chang, Y., Lu, J., Jiang, H., & Wu, S. (2015) · Brain Research · doi:10.1016/j.brainres.2015.10.034 · Cited by 13 · see citing works
TGFβ1-Smad3 signaling mediates the formation of a stable serine racemase dimer in microglia.
Beltrán-Castillo, S., Triviño, J. J., Eugenín, J. L., & Rommy von Bernhardi, M. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140447 · Cited by 12 · see citing works
Marchesani, F., Gianquinto, E., Autiero, I., Michielon, A., Campanini, B., Faggiano, S., Bettati, S., Mozzarelli, A., Spyrakis, F., & Bruno, S. (2020) · FEBS Journal · doi:10.1111/febs.15645 · Cited by 12 · see citing works
D-Serine Production, Degradation, and Transport in ALS: Critical Role of Methodology
Crow, J. P., Marecki, J. C., & Thompson, M. M. (2012) · Neurology Research International · doi:10.1155/2012/625245 · Cited by 11 · see citing works
Human serine racemase is nitrosylated at multiple sites
Marchesani, F., Bruno, S., Paredi, G., Raboni, S., Campanini, B., & Mozzarelli, A. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.01.009 · Cited by 11 · see citing works
Paradox of schizophrenia genetics: is a paradigm shift occurring?
Doi, N., Hoshi, Y., Itokawa, M., Yoshikawa, T., Ichikawa, T., Arai, M., Usui, C., & Tachikawa, H. (2012) · Behavioral and Brain Functions · doi:10.1186/1744-9081-8-28 · Cited by 10 · see citing works
Yin, Y., Hu, J., Wu, H., Yang, X., Qi, J., Huang, L., Luo, Z.-Y., Jin, S., Hu, N.-Y., Luo, Z.-C., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.07.034 · Cited by 7 · see citing works
Koulouris, C. R., Gardiner, S. E., Harris, T. K., Elvers, K. T., Roe, S. M., Gillespie, J. A., Ward, S. E., Grubisha, O., Nicholls, R. A., Atack, J. R., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03264-5 · Cited by 6 · see citing works
The Role of Astrocytes in the Pathophysiology of Schizophrenia.
Steffek, A. E. (2007) · Deep Blue (University of Michigan) · Cited by 6 · see citing works
- Authors
- Mustafa, A. K., Kumar, M., Selvakumar, B., Ho, G. P. H., Ehmsen, J. T., Barrow, R. K., Amzel, L. M., & Snyder, S. H.
- Affiliations
- *Solomon H. Snyder Department of Neuroscience and
- Departments of †Biophysics and Biophysical Chemistry,
- Johns Hopkins University (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-02-20
- Volume
- 104
- Issue
- 8
- Pages
- 2950-2955
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1815287
- OpenAlex
- W2147808921
- Cited by
- 136
- References
- 21
- Citations by year
- 2026: 2 · 2025: 1 · 2023: 1 · 2022: 6 · 2021: 3 · 2020: 6 · 2019: 3 · 2018: 8 · 2017: 7 · 2016: 9 · 2015: 8 · 2014: 12 · 2013: 12 · 2012: 13
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Mental Health (R01MH018501, R37MH018501, MH-18501)
- National Institute on Drug Abuse (DA 00074, K05DA000074)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- serine racemase, S-nitrosylation, D-serine, NMDA receptor co-agonist, product inhibition, ATP binding site, neuronal nitric oxide synthase, nitric oxide, presynaptic modulation
- MeSH terms
- Serine Racemase, Adenosine Triphosphate, Amino Acid Sequence, Animals, Coenzymes, Cysteine, Enzyme Activation, Humans, Models, Molecular, Models, Neurological, Molecular Sequence Data, Nitric Oxide, Serine, Receptors, N-Methyl-D-Aspartate, Racemases and Epimerases, Feedback, Physiological, S-Nitrosoglutathione, Mice, Nitric Oxide Synthase Type I
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