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Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.

Lenarčič Živković M, Zaręba-Kozioł M, Zhukova L, Poznański J, Zhukov I, Wysłouch-Cieszyńska A
J Biol Chem 287 40457-70 (2012)
Cited: 15 times
EuropePMC logo PMID: 22989881

Abstract

Background

S100A1 protein is a proposed target of molecule-guided therapy for heart failure.

Results

S-Nitrosylation of S100A1 is present in cells, increases Ca(2+) binding, and tunes the overall protein conformation.

Articles - 2llt mentioned but not cited (5)

  1. dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation. Chen YJ, Lu CT, Su MG, Huang KY, Ching WC, Yang HH, Liao YC, Chen YJ, Lee TY. Nucleic Acids Res 43 D503-11 (2015)
  2. Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein. Lenarčič Živković M, Zaręba-Kozioł M, Zhukova L, Poznański J, Zhukov I, Wysłouch-Cieszyńska A. J Biol Chem 287 40457-40470 (2012)
  3. Conservation of Specificity in Two Low-Specificity Proteins. Wheeler LC, Anderson JA, Morrison AJ, Wong CE, Harms MJ. Biochemistry 57 684-695 (2018)
  4. Molecular Basis of S100A1 Activation and Target Regulation Within Physiological Cytosolic Ca2+ Levels. Sun B, Kekenes-Huskey PM. Front Mol Biosci 7 77 (2020)
  5. PTM-Psi: A python package to facilitate the computational investigation of post-translational modification on protein structures and their impacts on dynamics and functions. Mejia-Rodriguez D, Kim H, Sadler N, Li X, Bohutskyi P, Valiev M, Qian WJ, Cheung MS. Protein Sci 32 e4822 (2023)


Reviews citing this publication (4)

  1. Protein post-translational modifications: In silico prediction tools and molecular modeling. Audagnotto M, Dal Peraro M. Comput Struct Biotechnol J 15 307-319 (2017)
  2. S100 proteins as therapeutic targets. Bresnick AR. Biophys Rev 10 1617-1629 (2018)
  3. Computational Structural Biology of S-nitrosylation of Cancer Targets. Bignon E, Allega MF, Lucchetta M, Tiberti M, Papaleo E. Front Oncol 8 272 (2018)
  4. Cardiomyocytes, endothelial cells and cardiac fibroblasts: S100A1's triple action in cardiovascular pathophysiology. Rohde D, Busch M, Volkert A, Ritterhoff J, Katus HA, Peppel K, Most P. Future Cardiol 11 309-321 (2015)

Articles citing this publication (6)

  1. The Ca2+ sensor S100A1 modulates neuroinflammation, histopathology and Akt activity in the PSAPP Alzheimer's disease mouse model. Afanador L, Roltsch EA, Holcomb L, Campbell KS, Keeling DA, Zhang Y, Zimmer DB. Cell Calcium 56 68-80 (2014)
  2. An Interplay of S-Nitrosylation and Metal Ion Binding for Astrocytic S100B Protein. Bajor M, Zaręba-Kozioł M, Zhukova L, Goryca K, Poznański J, Wysłouch-Cieszyńska A. PLoS One 11 e0154822 (2016)
  3. Molecular Basis of S100A1 Activation at Saturating and Subsaturating Calcium Concentrations. Scott CE, Kekenes-Huskey PM. Biophys J 110 1052-1063 (2016)
  4. Understanding Calcium-Dependent Conformational Changes in S100A1 Protein: A Combination of Molecular Dynamics and Gene Expression Study in Skeletal Muscle. Chaturvedi N, Ahmad K, Yadav BS, Lee EJ, Sonkar SC, Marina N, Choi I. Cells 9 E181 (2020)
  5. Identification of 2-oxohistidine Interacting Proteins Using E. coli Proteome Chips. Lin JM, Tsai YT, Liu YH, Lin Y, Tai HC, Chen CS. Mol Cell Proteomics 15 3581-3593 (2016)
  6. Intracellular Protein S-Nitrosylation-A Cells Response to Extracellular S100B and RAGE Receptor. Zaręba-Kozioł M, Burdukiewicz M, Wysłouch-Cieszyńska A. Biomolecules 12 613 (2022)


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