A new family of receptor tyrosine kinases with a venus flytrap binding domain in insects and other invertebrates activated by aminoacids

PLoS ONE

Volumn 4, Issue 5, 2009, Pages

  Ahier, Arnaud ^a   Rondard, Philippe ^b   Gouignard, Nadège ^a   Khayath, Naji ^a   Huang, Siluo ^b   Trolet, Jacques ^a   Donoghue, Daniel J ^d   Gauthier, Monique ^c   Pin, Jean Philippe ^b   Dissous, Colette ^a  

^a INSERM   (France)

^b UNIV MONTPELLIER   (France)

^c Université Paul Sabatier   (France)

^d UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; ALPHA AMINO ACID; ARGININE; INSULIN RECEPTOR; PROTEIN TYROSINE KINASE; TYROSINE; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG; VENUS KINASE RECEPTOR; AMINO ACID;

ANIMAL TISSUE; ARTICLE; AUTOPHOSPHORYLATION; BINDING SITE; CONTROLLED STUDY; DEVELOPMENTAL STAGE; ENZYME ACTIVATION; FEMALE; GONAD FUNCTION; HUMAN; HUMAN CELL; INSECT; INVERTEBRATE; LARVAL DEVELOPMENT; LARVAL STAGE; MOLECULAR PHYLOGENY; MONOPHYLY; NONHUMAN; NUCLEOTIDE SEQUENCE; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; RESIDUE ANALYSIS; SEQUENCE HOMOLOGY; STRUCTURAL HOMOLOGY; AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; GONAD; LARVA; METABOLISM; MOLECULAR GENETICS; MULTIGENE FAMILY; PHYLOGENY; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

DIONAEA; HEXAPODA; INVERTEBRATA; PLATYHELMINTHES; SCHISTOSOMA MANSONI;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CELL LINE; CONSERVED SEQUENCE; ENZYME ACTIVATION; GONADS; HUMANS; INSECTS; INVERTEBRATES; LARVA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PHYLOGENY; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTOR PROTEIN-TYROSINE KINASES; SEQUENCE ALIGNMENT;

EID: 66249089158     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005651     Document Type: Article

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