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Xue B, Uversky VN. Structural characterizations of phosphorylatable residues in transmembrane proteins from . Intrinsically Disord Proteins. 2013;1(1):e25713doi: 10.4161/idp.25713.
Xue, B., & Uversky, V. N. (2013). Structural characterizations of phosphorylatable residues in transmembrane proteins from . Intrinsically disordered proteins, 1(1), e25713. https://doi.org/10.4161/idp.25713
Xue, Bin, and Uversky, Vladimir N. "Structural characterizations of phosphorylatable residues in transmembrane proteins from ." Intrinsically disordered proteins vol. 1,1 (2013): e25713. doi: https://doi.org/10.4161/idp.25713
Xue B, Uversky VN. Structural characterizations of phosphorylatable residues in transmembrane proteins from . Intrinsically Disord Proteins. 2013 Apr 01;1(1):e25713. doi: 10.4161/idp.25713. eCollection 2013. PMID: 28516016; PMCID: PMC5424800.
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Intrinsically Disord Proteins. 2013 Apr 01;1(1):e25713. doi: 10.4161/idp.25713. eCollection 2013.

Structural characterizations of phosphorylatable residues in transmembrane proteins from .

Intrinsically disordered proteins

Bin Xue, Vladimir N Uversky

Affiliations

  1. Department of Molecular Medicine; Morsani College of Medicine; University of South Florida; Tampa, FL USA.
  2. USF Health Byrd Alzheimer's Research Institute; Morsani College of Medicine; University of South Florida; Tampa, FL USA.
  3. Institute for Biological Instrumentation; Russian Academy of Sciences; Moscow Region, Russia.

PMID: 28516016 PMCID: PMC5424800 DOI: 10.4161/idp.25713

Abstract

Phosphorylation is a common post-translational modification that plays important roles in a wide range of biochemical and cellular processes. Many enzymes and receptors can be switched "on" or "off" by conformational changes induced by phosphorylation. The phosphorylation process is mediated by a family of enzymes called kinase. Currently, more than 1,000 different kinases have been identified in

Keywords: intrinsic disorder; phosphorylation; relative surface accessibility; structural flexibility

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