Literature DB >> 22157013

Analysis and functional prediction of reactive cysteine residues.

Stefano M Marino1, Vadim N Gladyshev.   

Abstract

Cys is much different from other common amino acids in proteins. Being one of the least abundant residues, Cys is often observed in functional sites in proteins. This residue is reactive, polarizable, and redox-active; has high affinity for metals; and is particularly responsive to the local environment. A better understanding of the basic properties of Cys is essential for interpretation of high-throughput data sets and for prediction and classification of functional Cys residues. We provide an overview of approaches used to study Cys residues, from methods for investigation of their basic properties, such as exposure and pK(a), to algorithms for functional prediction of different types of Cys in proteins.

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Year:  2011        PMID: 22157013      PMCID: PMC3281665          DOI: 10.1074/jbc.R111.275578

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  71 in total

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  76 in total

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Review 3.  Redox Systems Biology: Harnessing the Sentinels of the Cysteine Redoxome.

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Review 4.  Thiol-Based Redox Modulation of Soluble Guanylyl Cyclase, the Nitric Oxide Receptor.

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5.  Sulfhydration of p66Shc at cysteine59 mediates the antioxidant effect of hydrogen sulfide.

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Review 7.  Reactive nitrogen species and hydrogen sulfide as regulators of protein tyrosine phosphatase activity.

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Review 8.  Cysteine oxidative posttranslational modifications: emerging regulation in the cardiovascular system.

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9.  Protein flexibility and cysteine reactivity: influence of mobility on the H-bond network and effects on pKa prediction.

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Journal:  Protein J       Date:  2014-08       Impact factor: 2.371

10.  Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair.

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