Global analysis of S-nitrosylation sites in the wild type (APP) transgenic mouse brain: Clues for synaptic pathology
Open accessAbstract
Alzheimer's disease (AD) is characterized by an early synaptic loss, which strongly correlates with the severity of dementia. The pathogenesis and causes of characteristic AD symptoms are not fully understood. Defects in various cellular cascades were suggested, including the imbalance in production of reactive oxygen and nitrogen species. Alterations in S-nitrosylation of several proteins were previously demonstrated in various AD animal models and patients. In this work, using combined biotin-switch affinity/nano-LC-MS/MS and bioinformatic approaches we profiled endogenous S-nitrosylation of brain synaptosomal proteins from wild type and transgenic mice overexpressing mutated human Amyloid Precursor Protein (hAPP). Our data suggest involvement of S-nitrosylation in the regulation of 138 synaptic proteins, including MAGUK, CamkII, or synaptotagmins. Thirty-eight proteins were differentially S-nitrosylated in hAPP mice only. Ninety-five S-nitrosylated peptides were identified for the first time (40% of total, including 33 peptides exclusively in hAPP synaptosomes). We verified differential S-nitrosylation of 10 (26% of all identified) synaptosomal proteins from hAPP mice, by Western blotting with specific antibodies. Functional enrichment analysis linked S-nitrosylated proteins to various cellular pathways, including: glycolysis, gluconeogenesis, calcium homeostasis, ion, and vesicle transport, suggesting a basic role of this post-translational modification in the regulation of synapses. The linkage of SNO-proteins to axonal guidance and other processes related to APP metabolism exclusively in the hAPP brain, implicates S-nitrosylation in the pathogenesis of Alzheimer's disease.
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Selected studies of the S-nitrosylation proteome in AD identified key proteins with altered functions associated with antioxidant, glycolysis, mitochondrial export, calcium homeostasis, synapses, apoptosis, mitochondrial dynamics, protein folding, and neuroinflammation.
“Selected studies of the S-nitrosylation proteome in AD identified key proteins with altered functions associated with antioxidant, glycolysis, mitochondrial export, calcium homeostasis, synapses, apoptosis, mitochondrial dynamics, protein folding, and neuroinflammation, among other functions [113,114,115,116].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [114]
The study’s results and Discussion (page not provided) identify differentially S-nitrosylated synaptic and metabolic proteins and link S-nitrosylated proteins to glycolysis and calcium homeostasis. The paper discusses apoptosis, protein misfolding, and mitochondrial fragmentation, but does not establish the full list of claimed functional categories—particularly mitochondrial export and neuroinflammation—as findings of its proteomic study. It also identifies altered S-nitrosylation rather than demonstrating altered function for all identified proteins. (LLM, conf=0.85)
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BackgroundCofilin-mediated neurodegeneration in alzheimer’s disease and other amyloidopathies
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S-nitrosylation: A radical way to protect the heart
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Amyloid Precursor Protein Is Trafficked and Secreted via Synaptic Vesicles
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Aβ1-42 stimulates actin polymerization in hippocampal neurons through Rac1 and Cdc42 Rho GTPases
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Nitric Oxide and Cancer: The Emerging Role of S-Nitrosylation
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“The role of protein S-nitrosylation underlying pathology of various diseases, including cancer (9, 10), heart condition”
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Protein S-nitrosylation and cancer
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“The role of protein S-nitrosylation underlying pathology of various diseases, including cancer (9, 10), heart condition”
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S-nitrosylation regulates mitochondrial quality control via activation of parkin
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S -nitrosylation/activation of COX-2 mediates NMDA neurotoxicity
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“genase (19), cyclo-oxygenase-2 (20), N-ethylmaleimide sen-”
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High Degree of Heterogeneity in Alzheimer's Disease Progression Patterns
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Differential S-nitrosylation of proteins in Alzheimer’s disease
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“(92), to study differentially S-nitrosylated proteins in”
Mice as models: Transgenic approaches and Alzheimer's disease
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“nisms underlying disease pathology (48, 49).”
Morciano, M., Beckhaus, T., Karas, M., Zimmermann, H., & Volknandt, W. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05824.x · Cited by 90 · cited 1× · see citing works
“Synaptosomes are a well-recognized model for studies of synaptic complexity in the brain (86, 87).”
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“(28), and serine racemase (29), has been related to severe”
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“to an inhibition of the Rac1 activation (126).”
BackgroundModulation by nitric oxide of metalloprotein regulatory activities
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“It readily reacts with various endogenous substrates forming that is, iron and copper adducts in prosthetic groups of proteins (4), peroxynitrite in the reaction with reactive oxygen species, ROS (5), and S-nitrosothiols with endogenous low-molecular weight thiols like cysteine and glutathione (6).”
BackgroundNitric oxide in the cerebral cortex of amyloid-precursor protein (SW) Tg2576 transgenic mice
Rodrigo, J., Fernández‐Vizarra, P., Castro‐Blanco, S., Bentura, M. L., Nieto, M., Gómez‐Isla, T., Martínez‐Murillo, R., Martı́nez, A., Serrano, J., & Fernández, A. P. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.06.030 · Cited by 70 · cited 1× · see citing works
“and related to cortical neurons and microglial cells (101).”
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Pivotal role of the RanBP9-cofilin pathway in Aβ-induced apoptosis and neurodegeneration
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Identification of S-nitrosylated proteins in endotoxin-stimulated RAW264.7 murine macrophages
Gao, C., Guo, H., Wei, J., Mi, Z., Wai, P. Y., & Kuo, P. C. (2004) · Nitric Oxide · doi:10.1016/j.niox.2004.11.006 · Cited by 68 · see citing works
A pilot proteomic study of amyloid precursor interactors in Alzheimer's disease
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“Actb/ACTB ( -actin) has been detected as part of the same molecular complex with APP (74).”
BackgroundDetection of Protein S-Nitrosation using Irreversible Biotinylation Procedures (IBP)
Huang, B., & Chen, C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.05.001 · Cited by 67 · see citing works
Regulation and Specificity of S-Nitrosylation and Denitrosylation
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“and its unknown levels of nitrosylating compounds (55).”
BackgroundProteomic analysis of protein S ‐nitrosylation
Torta, F. T., Usuelli, V., Malgaroli, A., & Bachi, A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800089 · Cited by 63 · see citing works
Jeon, G. S., Nakamura, T., Lee, J.-S., Choi, W.-J., Ahn, S., Lee, K., Sung, J., & Lipton, S. A. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8562-z · Cited by 63 · see citing works
Site-Specific Proteomics Approach for Study Protein S-Nitrosylation
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Ubiquitination and cysteine nitrosylation during aging and Alzheimer's disease
Riederer, I. M., Schiffrin, M., Kövari, E., Bouras, C., & Riederer, B. M. (2009) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2009.04.018 · Cited by 60 · see citing works
Urine proteome of autosomal dominant polycystic kidney disease patients
Bakun, M., Niemczyk, M., Domański, D., Jaźwiec, R., Perzanowska, A., Niemczyk, S., Kistowski, M., Fabijańska, A., Borowiec, A., Pączek, L., et al. (2012) · Clinical Proteomics · doi:10.1186/1559-0275-9-13 · Cited by 58 · see citing works
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“Moreover, freezing and thawing of tissues leads to artifacts in tyrosine nitration and cysteine nitrosylation if homogenization is not performed in the presence of thiol blocking agents (94).”
BackgroundKins, S., Lauther, N., Szodorai, A., & Beyreuther, K. T. (2006) · Neurodegenerative Diseases · doi:10.1159/000095259 · Cited by 54 · see citing works
Amyloid Precursor Protein Is an Autonomous Growth Cone Adhesion Molecule Engaged in Contact Guidance
Sosa, L. J., Bergman, J., Estrada-Bernal, A., Glorioso, T. J., Kittelson, J. M., & Pfenninger, K. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064521 · Cited by 53 · see citing works
von Eichborn, J., Dunkel, M., Gohlke, B.-O., Preissner, S. C., Hoffmann, M. F., Bauer, J. M. J., Armstrong, J. D., Schaefer, M. H., Andrade-Navarro, M. A., Novère, N. G. L., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1040 · Cited by 52 · cited 1× · see citing works
“de/synsys/ (68) and SynaptomeDB; http://psychiatry.”
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Bakun, M., Karczmarski, J., Poznański, J. T., Rubel, T., Rózga, M., Malinowska, A., Sands, D., Hennig, E. E., Olędzki, J., Ostrowski, J., et al. (2009) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200800111 · Cited by 50 · cited 1× · see citing works
“The quantitative LC-MS runs were converted into 2D heat-maps (with retention time and m/z as vertical and horizontal axes, respectively) using in-house designed finnigan2Pipe data conversion tool (59, 60).”
MethodAltered NCAM Expression Associated with the Cholinergic System in Alzheimer's Disease
Aisa, B., Gil-Bea, F. J., Solas, M., Garcı́a-Alloza, M., Chen, C., Lai, M. K. P., Francis, P. T., & Ramírez, M. J. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1398 · Cited by 46 · see citing works
Rudinskiy, N., Grishchuk, Y., Vaslin, A., Puyal, J., Delacourte, A., Hirling, H., Clarke, P. G. H., & Luthi‐Carter, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m804740200 · Cited by 45 · see citing works
Tello, D., Tarín, C., Ahicart, P., Bretón‐Romero, R., Lamas, S., & Martı́nez-Ruiz, A. (2009) · PROTEOMICS · doi:10.1002/pmic.200900070 · Cited by 45 · see citing works
Suppression of APP‐containing vesicle trafficking and production of β‐amyloid by AID/DHHC‐12 protein
Mizumaru, C., Saito, Y., Ishikawa, T., Yoshida, T., Yamamoto, T., Nakaya, T., & Suzuki, T. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06399.x · Cited by 43 · see citing works
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Strategies and tools to explore protein S-nitrosylation
Raju, K., Doulias, P., Τενοπούλου, Μ., Greene, J. L., & Ischiropoulos, H. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.05.009 · Cited by 39 · see citing works
Mikuła, M., Gaj, P., Dzwonek, K., Rubel, T., Karczmarski, J., Paziewska, A., Dzwonek, A., Brągoszewski, P., Dadlez, M., & Ostrowski, J. (2010) · DNA Research · doi:10.1093/dnares/dsq016 · Cited by 37 · see citing works
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Cathepsin D deficiency induces cytoskeletal changes and affects cell migration pathways in the brain
Koch, S., Scifo, E., Rokka, A., Trippner, P., Lindfors, M., Korhonen, R., Corthals, G. L., Virtanen, I., Lalowski, M. M., & Tyynelä, J. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.10.004 · Cited by 25 · see citing works
Involvement of S-Nitrosylation of Actin in Inhibition of Neurotransmitter Release by Nitric Oxide
Lu, J., Katano, T., Okuda‐Ashitaka, E., Oishi, Y., Urade, Y., & Ito, S. (2009) · Molecular Pain · doi:10.1186/1744-8069-5-58 · Cited by 25 · cited 1× · see citing works
“network and inhibited dopamine release (120).”
Silva, O. A. B. D. C. E., Henriques, A. G., Domingues, S. C., & Silva, E. F. D. C. E. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710793237458 · Cited by 22 · see citing works
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“screening of affected pathways in the brain (90, 91).”
BackgroundCognition: The brain's decline
Abbott, A. (2012) · Nature · doi:10.1038/492s4a · Cited by 18 · see citing works
Magdesian, M. H., Gralle, M., Guerreiro, L. H., Beltrão, P. J., Carvalho, M., Santos, L. E., Mello, F. G. D., Reis, R. A. D. M., & Ferreira, S. T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022857 · Cited by 16 · see citing works
A new strategy for gene targeting and functional proteomics using the DT40 cell line
Orlowska, K. P., Kłosowska-Kosicka, K., Szczęsny, R. J., Cysewski, D., Krawczyk, P. S., & Dziembowski, A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt650 · Cited by 16 · see citing works
Involvement of membrane GABA transporter in α-latrotoxin-stimulated [3H]GABA release
Linetska, M. V., Storchak, L. G., Tarasenko, A. S., & Himmelreich, N. H. (2003) · Neurochemistry International · doi:10.1016/j.neuint.2003.07.003 · Cited by 13 · see citing works
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Involvement of S-nitrosylation of actin in inhibition of neurotransmitter release by nitric oxide
陸, 景. (2010) · Medical Entomology and Zoology · Cited by 8 · see citing works
Phenylarsine oxide is able to dissipate synaptic vesicle acidic pool
Tarasenko, A. S., KOSTRZHEVSKA, O., Storchak, L. G., Linetska, M. V., Borisova, Т., & Himmelreich, N. H. (2005) · Neurochemistry International · doi:10.1016/j.neuint.2005.02.004 · Cited by 7 · see citing works
Yeast prion [PSI] lowers the levels of mitochondrial prohibitins
Sikora, J. W., Towpik, J., Graczyk, D., Kistowski, M., Rubel, T., Poznański, J. T., Langridge, J., Hughes, C. J., Dadlez, M., & Boguta, M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.08.003 · Cited by 7 · see citing works
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Target-Selective Protein S-Nitrosylation by Sequence Motif Recognition
Jia, J., Arif, A., Terenzi, F., Willard, B. B., Plow, E. F., Hazen, S. L., & Fox, P. L. (2014) · Cell · doi:10.1016/j.cell.2014.09.032 · Cited by 176 · see citing works
Zhang, H., Gong, W., Wu, S., & Perrett, S. (2022) · Cells · doi:10.3390/cells11050829 · Cited by 139 · see citing works
Nitrosative stress in Parkinson’s disease
Stykel, M. G., & Ryan, S. D. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00370-3 · Cited by 97 · see citing works
Keshet, R., Lee, J. S., Adler, L. N., Iraqi, M., Ariav, Y., Lim, L. Q. J., Lerner, S., Rabinovich, S., Oren, R., Katzir, R., et al. (2020) · Nature Cancer · doi:10.1038/s43018-020-0106-7 · Cited by 98 · see citing works
S -nitrosation of proteins relevant to Alzheimer’s disease during early stages of neurodegeneration
Seneviratne, U. I., Nott, A., Bhat, V. B., Ravindra, K. C., Wishnok, J. S., Tsai, L., & Tannenbaum, S. R. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1521318113 · Cited by 97 · see citing works
Identification of S-nitroso-CoA reductases that regulate protein S-nitrosylation
Anand, P., Hausladen, A., Wang, Y., Zhang, G., Stomberski, C. T., Brunengraber, H., Hess, D. T., & Stamler, J. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417816112 · Cited by 93 · see citing works
“Acetoacetyl-CoA thiolase has also been identified by proteomic analysis as an endogenous SNOprotein in mammals (17, 18).”
BackgroundMitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease
Butterfield, D. A., & Boyd-Kimball, D. (2020) · Antioxidants · doi:10.3390/antiox9090818 · Cited by 85 · see citing works
Yang, H., Oh, C.-K., Amal, H., Wishnok, J. S., Lewis, S., Schahrer, E., Trudler, D., Nakamura, T., Tannenbaum, S. R., & Lipton, S. A. (2022) · Science Advances · doi:10.1126/sciadv.ade0764 · Cited by 70 · see citing works
“One enrichment approach for SNO analysis involves indirect detection via the biotin-switch technique ( 31 – 33 ), which requires blocking of free thiols, followed by selective reduction with ascorbate of SNO-Cys residues that are then biotinylated.”
Type III intermediate filaments as targets and effectors of electrophiles and oxidants
Viedma-Poyatos, Á., Pajares, M. A., & Pérez‐Sala, D. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101582 · Cited by 56 · see citing works
Stress-induced Changes in the S-palmitoylation and S-nitrosylation of Synaptic Proteins*[S]
Zaręba-Kozioł, M., Bartkowiak-Kaczmarek, A., Figiel, I., Krzystyniak, A., Wójtowicz, T., Bijata, M., & Włodarczyk, J. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001581 · Cited by 58 · see citing works
“Synaptoneurosomes Isolation—Synaptoneurosomes were prepared from the brains of control and stressed mice as previously described (21).”
MethodQuantitative proteomics of synaptosome <i>S</i>‐nitrosylation in Alzheimer’s disease
Wijasa, T. S., Sylvester, M., Brocke‐Ahmadinejad, N., Schwartz, S., Santarelli, F., Gieselmann, V., Klockgether, T., Brosseron, F., & Heneka, M. T. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14870 · Cited by 41 · see citing works
Gu, L., & Robinson, R. A. S. (2016) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201600015 · Cited by 38 · see citing works
The roles of S-nitrosylation and S-glutathionylation in Alzheimer's disease
Dyer, R. R., Ford, K. I., & Robinson, R. A. S. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.08.004 · Cited by 37 · see citing works
Thioredoxin-mimetic peptides as catalysts of S-denitrosylation and anti-nitrosative stress agents
Kronenfeld, G., Engelman, R., Weisman-Shomer, P., Atlas, D., & Benhar, M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.11.021 · Cited by 34 · see citing works
“Other studies have documented elevated nitrosylation of multiple members of the Prx family under conditions related to neurodegenerative diseases [29,30].”
BackgroundGu, L., & Robinson, R. A. S. (2016) · The Analyst · doi:10.1039/c6an00417b · Cited by 34 · see citing works
Profiling of post-translational modifications by chemical and computational proteomics
Yang, F., & Wang, C. (2020) · Chemical Communications · doi:10.1039/d0cc05447j · Cited by 29 · see citing works
Fransen, M., & Lismont, C. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-2233-4_19 · Cited by 25 · see citing works
H2S- and NO-Signaling Pathways in Alzheimer's Amyloid Vasculopathy: Synergism or Antagonism?
Salmina, A. B., Komleva, Y. K., Szijártó, I. A., Gorina, Y. V., Lopatina, O. L., Gertsog, G. E., Filipović, M. R., & Gollasch, M. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00361 · Cited by 24 · see citing works
“However, the wide spectrum of S-nitrosated proteins seen in AD (Zahid et al., 2014; Zaręba-Kozioł et al., 2014) and very recent data on the inhibitory action of H2S-donor on RyR activity do not rule out this possibility (Tomasova et al.”
BackgroundQuantitative Proteomic Approaches for Analysis of Protein S-Nitrosylation
Qu, Z., Greenlief, C. M., & Gu, Z. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00857 · Cited by 21 · see citing works
An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein
Bajor, M., Zaręba-Kozioł, M., Zhukova, L., Goryca, K., Poznański, J. T., & Wysłouch‐Cieszyńska, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0154822 · Cited by 18 · see citing works
“Total protein concentration of the lysate was adjusted to 1 mg/ml. Obtained cell lysates were treated using BST as previously described [37, 44].”
Villar, M. F. Z., Hanotte, J. L., Crespo, R., Pardo, J., & Reggiani, P. C. (2021) · Hippocampus · doi:10.1002/hipo.23379 · Cited by 18 · see citing works
Gu, L., & Robinson, R. A. S. (2016) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-016-9307-4 · Cited by 18 · see citing works
“, S-nitrosylation, S-glutathionylation) in AD have been reported, most of these studies were focused on brain tissue and used gel-based methods [13, 14, 17, 46–48].”
BackgroundMethodInfluentialThe Potential of Proteomics in Understanding Neurodegeneration
Pal, R., Larsen, J. P., & Møller, S. G. (2015) · International review of neurobiology · doi:10.1016/bs.irn.2015.05.002 · Cited by 17 · see citing works
Zaręba-Kozioł, M., Bartkowiak, A., Roszkowska, M., Bijata, K., Figiel, I., Halder, A. K., Kamińska, P., Müller, F. E., Basu, S., Zhang, W., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126253 · Cited by 14 · see citing works
“Synaptoneurosomes were prepared from the brains of WT and DHHC7 KO (males and females Nmice/group = 3) as previously described [30,96].”
MethodRecent advances in applying mass spectrometry and systems biology to determine brain dynamics
Scifo, E., Calza, G., Fuhrmann, M., Soliymani, R., Baumann, M., & Lalowski, M. M. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1335200 · Cited by 13 · see citing works
“should allow for more sensitive assays of PTM (including previously uncharacterized ones) in the brain, under health or disease states [177].”
BackgroundThe Human Brain Proteome Project: Biological and Technological Challenges
Fernández‐Irigoyen, J., Corrales, F. J., & Santamaría, E. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9706-0_1 · Cited by 9 · see citing works
Bączyńska, E., Zaręba-Kozioł, M., Ruszczycki, B., Krzystyniak, A., Wójtowicz, T., Bijata, K., Pochwat, B., Magnowska, M., Roszkowska, M., Figiel, I., et al. (2024) · Neurobiology of Stress · doi:10.1016/j.ynstr.2024.100683 · Cited by 9 · see citing works
Hallam, R. D., Buchner-Duby, B., Stykel, M. G., Coackley, C. L., & Ryan, S. D. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0074-22.2022 · Cited by 9 · see citing works
Network analysis of S-nitrosylated synaptic proteins demonstrates unique roles in health and disease
Stykel, M. G., & Ryan, S. D. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119720 · Cited by 9 · see citing works
Roles of Ion Fluxes, Metabolism, and Redox Balance in Cancer Therapy
Lai, H., Fan, X., Li, R., Wang, Y., Zhang, J., Liu, L., Neher, E., Yao, X., & Leung, E. L. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8125 · Cited by 9 · see citing works
Gaudet, I. D., Xu, H., Gordon, E., Cannestro, G. A., Lu, M. L., & Wei, J. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03038-2 · Cited by 7 · see citing works
Proteome profiling of s-nitrosylated synaptosomal proteins by isobaric mass tags
Wijasa, T. S., Sylvester, M., Brocke‐Ahmadinejad, N., Kummer, M. P., Brosseron, F., Gieselmann, V., & Heneka, M. T. (2017) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2017.08.005 · Cited by 6 · see citing works
S-Nitrosylation in Alzheimer’s Disease Using Oxidized Cysteine-Selective cPILOT
Dyer, R. R., Gu, L., & Robinson, R. A. S. (2017) · Neuromethods · doi:10.1007/978-1-4939-7119-0_14 · Cited by 4 · see citing works
Zaręba-Kozioł, M., Lalowski, M. M., & Wysłouch‐Cieszyńska, A. (2016) · Neuromethods · doi:10.1007/7657_2016_102 · Cited by 1 · see citing works
The Role of Protein S-Nitrosylationin Alzheimer’s Disease and its Treatment
Wang, J. (2015) · Journal of Pharmaceutics & Pharmacology · doi:10.13188/2327-204x.1000014 · Cited by 1 · see citing works
The molecular fingerprint of stress resiliencePreprint
Włodarczyk, J., Bączyńska, E., Zaręba-Kozioł, M., Ruszczycki, B., Krzystyniak, A., Wójtowicz, T., Bijata, K., Pochwat, B., Magnowska, M., Roszkowska, M., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1780322/v1 · Cited by 1 · see citing works
Oxidative modification of vesicular transporters in an animal model of Alzheimer’s disease
Wang, Y. (2015) · Mspace (University of Manitoba)
Gaudet, I. D., Xu, H., Gordon, E., Cannestro, G. A., Lu, M. L., & Wei, J. (2024) · Figshare · doi:10.6084/m9.figshare.26686506
- Authors
- Zaręba-Kozioł, M., Szwajda, A., Dadlez, M., Wysłouch-Cieszyńska, A., & Lalowski, M.
- Affiliations
- Institute of Biochemistry and Biophysics, Polish Academy of Sciences (PL)
- Institute for Molecular Medicine Finland (FI)
- University of Helsinki (FI)
- Corresponding author
- Lalowski, Maciej
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2014-09
- Volume
- 13
- Issue
- 9
- Pages
- 2288-2305
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC4159650
- OpenAlex
- W2140005295
- Cited by
- 39
- References
- 145
- Citations by year
- 2024: 4 · 2023: 1 · 2022: 5 · 2021: 2 · 2020: 5 · 2019: 4 · 2018: 1 · 2017: 3 · 2016: 6 · 2015: 5 · 2014: 3
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Helsingin Yliopisto
- Fundacja na rzecz Nauki Polskiej (TEAM/2011-7/1, POIG.02.02.00-14-024/08-00)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- S-nitrosylation, Alzheimer's disease, amyloid precursor protein, APP transgenic mice, synaptosomal proteins, synaptic proteins, post-translational modification, synaptic regulation, membrane-associated guanylate kinase, CaMKII, synaptotagmin, glycolysis, calcium homeostasis, vesicle trafficking, axon guidance
- MeSH terms
- Animals, Brain, Female, Mice, Transgenic, Nerve Tissue Proteins, Protein Processing, Post-Translational, Synapses, Synaptosomes, S-Nitrosothiols, Nitric Oxide Synthase Type II, Nitric Oxide Synthase Type I
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