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Nitric Oxide Signaling and Sensing in Age-Related Diseases

Mazuryk, O., Gurgul, I., Oszajca, M., Polaczek, J., Kieca, K., Bieszczad-Żak, E., Martyka, T., & Stochel, G. (2024) · Antioxidants · doi:10.3390/antiox13101213 · Cited by 28 · 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

Medical and Veterinary Importance of the Moonlighting Functions of Triosephosphate Isomerase

Rodríguez-Bolaños, M., & Pérez‐Montfort, R. (2018) · Current Protein and Peptide Science · doi:10.2174/1389203719666181026170751 · Cited by 24 · see citing works

Protein Oxidative Modifications in Neurodegenerative Diseases: From Advances in Detection and Modelling to Their Use as Disease Biomarkers

Anjo, S. I., He, Z., Hussain, Z., Farooq, A., McIntyre, A., Laughton, C. A., Carvalho, A. N., & Finelli, M. J. (2024) · Antioxidants · doi:10.3390/antiox13060681 · Cited by 23 · see citing works

Modification of Glyceraldehyde-3-Phosphate Dehydrogenase with Nitric Oxide: Role in Signal Transduction and Development of Apoptosis

Muronetz, V. I., Medvedeva, M. V., Sevostyanova, I. A., & Schmalhausen, E. V. (2021) · Biomolecules · doi:10.3390/biom11111656 · Cited by 22 · see citing works

The Altered Hepatic Tubulin Code in Alcoholic Liver Disease

Groebner, J. L., & Tuma, P. L. (2015) · Biomolecules · doi:10.3390/biom5032140 · Cited by 22 · see citing works

Quantitative 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

Integrated Proteomics and Lipidomics Investigation of the Mechanism Underlying the Neuroprotective Effect of N-benzylhexadecanamide

Zhou, Y., Wang, H., Guo, F., Si, N., Brantner, A. H., Yang, J. T., Han, L., Wei, X., Zhao, H., & Bian, B. (2018) · Molecules · doi:10.3390/molecules23112929 · Cited by 20 · see citing works

A simple isotopic labeling method to study cysteine oxidation in Alzheimer’s disease: oxidized cysteine-selective dimethylation (OxcysDML)

Gu, L., & Robinson, R. A. S. (2016) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-016-9307-4 · Cited by 18 · see citing works

A systems biology-led insight into the role of the proteome in neurodegenerative diseases

Fasano, M., Monti, C., & Alberio, T. (2016) · Expert Review of Proteomics · doi:10.1080/14789450.2016.1219254 · Cited by 17 · see citing works

Insight into the cellular effects of nitrated phospholipids: Evidence for pleiotropic mechanisms of action

Duarte, S., Melo, T., Domingues, R., Ramírez, J. D. D. A., & Pérez‐Sala, D. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.06.003 · Cited by 16 · see citing works

Glyceraldehyde-3-phosphate dehydrogenase is involved in the pathogenesis of Alzheimer's disease

Schmalhausen, E. V., Medvedeva, M. V., & Muronetz, V. I. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110065 · Cited by 15 · see citing works

Quantitative Proteomics Reveals the Mechanism of Oxygen Treatment on Lenses of Alzheimer’s Disease Model Mice

Wang, H., Wang, Y., Hong, X., Li, S., & Wang, Y. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160263 · Cited by 15 · see citing works

Identification of Blood-Based Glycolysis Gene Associated with Alzheimer’s Disease by Integrated Bioinformatics Analysis

Wang, F., Xu, C., Chen, W., Duan, S., Xu, S., Dai, J., & Wang, Q. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210540 · Cited by 13 · see citing works

Increased Neuronal Nitric Oxide Synthase in Alzheimer's Disease Mediates Spontaneous Calcium Signaling and Divergent Glutamatergic Calcium Responses

Balez, R., Stevens, C. H., Lenk, K., Maksour, S., Sidhu, K., Sutherland, G. T., & Ooi, L. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0395 · Cited by 12 · see citing works

Proteomic Investigation of Murine Neuronal α7-Nicotinic Acetylcholine Receptor Interacting Proteins

Mulcahy, M. J., Paulo, J. A., & Hawrot, E. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00618 · Cited by 12 · see citing works

Unraveling the genetic architecture of blood unfolded p-53 among non-demented elderlies: novel candidate genes for early Alzheimer's disease

Yaghoobi, A., & Malekpour, S. A. (2024) · BMC Genomics · doi:10.1186/s12864-024-10363-6 · Cited by 10 · see citing works

Proteomics and lipidomics in the human brain

Ferrer, I. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-63639-3.00020-7 · Cited by 10 · see citing works

Updates on Versatile Role of Putative Gasotransmitter Nitric Oxide: Culprit in Neurodegenerative Disease Pathology

Singh, S. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00230 · Cited by 10 · see citing works

Identification of novel risk genes for Alzheimer’s disease by integrating genetics from hippocampus

Li, J., Li, L., Cai, S., Song, K., & Hu, S. (2024) · Scientific Reports · doi:10.1038/s41598-024-78181-0 · Cited by 9 · see citing works

Intracellular Accumulation of α-Synuclein Aggregates Promotes S-Nitrosylation of MAP1A Leading to Decreased NMDAR-Evoked Calcium Influx and Loss of Mature Synaptic Spines

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

Mass spectrometry analysis of S-nitrosylation of proteins and its role in cancer, cardiovascular and neurodegenerative diseases

Wang, X., Zhou, W., Gao, Z., & Lv, X. (2022) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2022.116625 · Cited by 9 · see citing works

Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD +

González, M. C., Romero, J. M., Ingaramo, M., Sosa, C. J. M., Curtino, J. A., & Carrizo, M. E. (2016) · FEBS Letters · doi:10.1002/1873-3468.12242 · Cited by 8 · see citing works

Nitric Oxide Mediated Degradation of CYP2A6 via the Ubiquitin-Proteasome Pathway in Human Hepatoma Cells

Cerrone, J., Lee, C., Tian, M., & Morgan, E. T. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.119.089961 · Cited by 8 · see citing works

Global Proteome-Wide Analysis of Cysteine S-Nitrosylation in Toxoplasma gondii

Wang, Z.-X., Li, J., Yang, Q., & Sun, X.-L. (2023) · Molecules · doi:10.3390/molecules28217329 · Cited by 7 · see citing works

Computational Prediction and Analysis of Associations between Small Molecules and Binding-Associated S-Nitrosylation Sites

Huang, G., Li, J., & Zhao, C. (2018) · Molecules · doi:10.3390/molecules23040954 · Cited by 7 · see citing works

A novel insight into differential expression profiles of sporadic cerebral cavernous malformation patients with different symptoms

Gozel, H. E., Kök, K., Özlen, F., İşler, C., & Pençe, S. (2021) · Scientific Reports · doi:10.1038/s41598-021-98647-9 · Cited by 7 · see citing works

The Role of Protein S-Nitrosylation in Mitochondrial Quality Control in Central Nervous System Diseases

Qiu, F., Liu, Y., & Liu, Z. (2024) · Aging and Disease · doi:10.14336/ad.2024.0099 · Cited by 6 · see citing works

S-nitrosoglutathione alleviates hyperglycemia-induced neurobehavioral deficits involving nitro-oxidative stress and aberrant monaminergic system

Aggarwal, A., Yadav, A., Saini, N., & Sandhir, R. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.03.001 · Cited by 5 · 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

Molecular etiopathogenesis of neurodegenerative diseases

Divya, D., Thekkekkara, D., Sai, T. E., Ramakrishna, D., Manjula, S. N., & Goswami, S. K. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-28822-7.00002-7 · Cited by 2 · see citing works

Clinical proteomics of enervated neurons

Sengupta, M. B., Chakrabarti, A., Saha, S. G., & Mukhopadhyay, D. (2016) · Clinical Proteomics · doi:10.1186/s12014-016-9112-2 · Cited by 2 · see citing works

Molecular and structural basis for nitrosoglutathione-dependent redox regulation of triosephosphate isomerase from Chlamydomonas reinhardtii

Meloni, M., Mattioli, E. J., Fanti, S., Peppi, G. M. E., Bin, T., Gabellini, G., Tedesco, D., Henri, J., Trost, P., Lemaire, S. D., et al. (2025) · Plant Science · doi:10.1016/j.plantsci.2025.112768 · Cited by 1 · see citing works

The Role of Protein S-Nitrosylationin Alzheimer’s Disease and its Treatment

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mTOR S-nitrosylation inhibits autophagy and lysosomal proteolysisPreprint

Tan, B. W. Q., Tan, S., Tan, B. W. L., Navakkode, S., Ng, C. Y., Yuan, S., Liang, M. C., Liu, C., Shi, Y. P., Chai, C., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.11.292607 · Cited by 1 · see citing works

A Glycolysis Gene Methylation Prediction Model Based on Explainable Machine Learning for Alzheimer's DiseasePreprint

Wang, F., Xu, C., Chen, W.-H., Duan, S., Xu, S., Dai, J., & Wang, Q. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3797592 · Cited by 1 · see citing works

S-nitrosylation in brain of mice exposed to low or high doses of gamma rays

Nicolas, F. (2018) · doi:10.7282/t3q52sz5

Characterization of high-density prion protein oligomers in rapid progressive and sporadic Alzheimer’s disease

Shafiq, M. (2019) · doi:10.53846/goediss-7266

Oxidative modification of vesicular transporters in an animal model of Alzheimer’s disease

Wang, Y. (2015) · Mspace (University of Manitoba)

Cysteine in Alzheimer's Disease

Ingale, S. P., Patil, R., & Upaganlawar, A. (2020) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-7998-1317-0.ch013

Reversing increased neuronal nitric oxide synthase in Alzheimer’s disease prevents aberrant glutamatergic calcium responsesPreprint

Balez, R., Stevens, C. H., Lenk, K., Maksour, S., Sidhu, K., Sutherland, G. T., & Ooi, L. (2022) · Research Square · doi:10.21203/rs.3.rs-2257266/v1

The Low Expression Of ALDOB Is Associated With Poor Prognosis In Renal Clear Cell CarcinomaPreprint

Cai, Z., Bai, P., Huang, H., Chen, B., Zhang, W., Luo, Y., Miao, C., Hong, Y., Lai, L., Zhu, K., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-2254556/v1

The biochemical pathways of Alzheimer's disease

El-Gammal, M. A., & Kodous, F. E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15702-8.00001-4

Additional file 1 of Unraveling the genetic architecture of blood unfolded p-53 among non-demented elderlies: novel candidate genes for early Alzheimer's disease

Yaghoobi, A., & Malekpour, S. A. (2024) · Figshare · doi:10.6084/m9.figshare.26715724

Acute low-dose benzo[a]pyrene exposure induces neurodegenerative syndrome in cyp1a low-expression zebrafish: A novel living Bioindicator for dioxin-like environmental pollutants

Li, M., Huang, X., Wang, D., Chen, Z., Wang, S., Qing, X., & Xie, S. (2026) · Aquatic Toxicology · doi:10.1016/j.aquatox.2026.107743

S-Nitrosylation in Alzheimer's disease

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Quantitative proteome analysis of S-nitrosylation on synaptosomal proteins in Alzheimer's disease

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Quantitative 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

Global analysis of S-nitrosylation sites in the wild type (APP) transgenic mouse brain: Clues for synaptic pathology

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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