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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: 18 times
EuropePMC logo PMID: 22989881

Abstract

Background
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 (6)

  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)
  5. Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery. Young BD, Cook ME, Costabile BK, Samanta R, Zhuang X, Sevdalis SE, Varney KM, Mancia F, Matysiak S, Lattman E, Weber DJ. J Mol Biol 434 167872 (2022)
  6. Protein S-Nitrosylation: A Chemical Modification with Ubiquitous Biological Activities. Aboalroub AA, Al Azzam KM. Protein J 43 639-655 (2024)

Articles citing this publication (7)



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