The conservation pattern of short linear motifs is highly correlated with the function of interacting protein domains

BMC Genomics

Volumn 9, Issue , 2008, Pages

  Ren, Siyuan ^a,c   Yang, Guang ^a   He, Youyu ^b   Wang, Yiguo ^a   Li, Yixue ^b   Chen, Zhengjun ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b Chinese Academy of Sciences   (China)

^c TEMPLE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CYTOSKELETON PROTEIN; MEMBRANE PROTEIN; PDZ PROTEIN; PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN SH2; PROTEIN SH3; PROTEIN TYROSINE KINASE;

ARTICLE; BIOINFORMATICS; CELL CYCLE REGULATION; CONTROLLED STUDY; CYTOPLASM; CYTOSKELETON; ENZYME PHOSPHORYLATION; EXTRACELLULAR SPACE; GENETIC CONSERVATION; GENETIC TRANSCRIPTION; HUMAN; NONHUMAN; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEOMICS; SCORING SYSTEM; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; GENETICS; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PDZ DOMAIN; PROTEIN DATABASE; SEQUENCE ALIGNMENT; SRC HOMOLOGY DOMAIN;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CONSERVED SEQUENCE; DATABASES, PROTEIN; HUMANS; MOLECULAR SEQUENCE DATA; PDZ DOMAINS; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN-TYROSINE KINASES; SEQUENCE ALIGNMENT; SRC HOMOLOGY DOMAINS;

EID: 55249126397     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-9-452     Document Type: Article

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