Intrinsic disorder-based protein interactions and their modulators

Current Pharmaceutical Design

Volumn 19, Issue 23, 2013, Pages 4191-4213

  Uversky, Vladimir N ^a,b  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

^b INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

Author keywords

Alternative splicing; Hub proteins; Intrinsically disordered protein; Posttranslational modification; Protein protein interaction; Structure function relationship

Indexed keywords

ALANINE; ARGININE; ASPARAGINE; ASPARTIC ACID; CYSTEINE; DNA; GLUTAMIC ACID; GLUTAMINE; GLYCINE; HISTIDINE; INTRINSICALLY DISORDERED PROTEIN; ISOLEUCINE; LEUCINE; LYSINE; METHIONINE; MONOMER; PHENYLALANINE; PROLINE; PROTEIN; RNA; SERINE; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

ACETYLATION; ALTERNATIVE RNA SPLICING; AMIDATION; AMINO ACID SEQUENCE; BINDING AFFINITY; BINDING SITE; CARBOXYLATION; DEAMINATION; DIHYDROXYLATION; DISULFIDE BOND; HYDROXYLATION; ISOMERIZATION; METHYLATION; MOLECULAR DYNAMICS; MOLECULAR MECHANICS; MOLECULAR RECOGNITION; NITROSYLATION; PALMITOYLATION; PATHOGENESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN METHYLATION; PROTEIN MOTIF; PROTEIN PRENYLATION; PROTEIN PROCESSING; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; STATIC ELECTRICITY; STEADY STATE; X RAY CRYSTALLOGRAPHY;

INTRINSICALLY DISORDERED PROTEINS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 84878627017     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/1381612811319230005     Document Type: Review

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