DisCons: A novel tool to quantify and classify evolutionary conservation of intrinsic protein disorder

BMC Bioinformatics

Volumn 16, Issue 1, 2015, Pages

  Varadi, Mihaly ^a,b   Guharoy, Mainak ^a,b   Zsolyomi, Fruzsina ^b   Tompa, Peter ^a,b,c  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^c INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

Author keywords

Intrinsic protein disorder; Large scale sequence analysis; Molecular recognition features (MoRFs); Short linear motifs (SLiMs)

Indexed keywords

AMINO ACIDS; MOLECULAR BIOLOGY;

CONFORMATIONAL FLEXIBILITY; EVOLUTIONARY CONSERVATIONS; EVOLUTIONARY HISTORY; INDIVIDUAL PROTEINS; INTRINSIC PROTEIN DISORDER; INTRINSICALLY DISORDERED PROTEINS; LARGE-SCALE SEQUENCES; SHORT LINEAR MOTIFS (SLIMS);

PROTEINS;

PROTEIN P53; TP53 PROTEIN, HUMAN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHEMICAL STRUCTURE; CHEMISTRY; CONSERVED SEQUENCE; HUMAN; MOLECULAR EVOLUTION; MOLECULAR GENETICS; PROCEDURES; PROTEIN CONFORMATION; SEQUENCE ANALYSIS; SOFTWARE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CONSERVED SEQUENCE; EVOLUTION, MOLECULAR; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ANALYSIS, PROTEIN; SOFTWARE; TUMOR SUPPRESSOR PROTEIN P53;

EID: 84929179017     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/s12859-015-0592-2     Document Type: Article

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