Modular binding domains in signal transduction proteins

Identifieur interne : 004079 ( Main/Exploration ); précédent : 004078; suivant : 004080

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Modular binding domains in signal transduction proteins

Auteurs : George B. Cohen [États-Unis] ; Ruibao Ren [États-Unis] ; David Baltimore [États-Unis]

Source :

• Cell [ 0092-8674 ] ; 1995.

RBID : ISTEX:FDF1DE80E78F088E956FA8F82BCB4744EF55C02F

English descriptors

• Teeft :
  • Adaptor molecule, Affinity, Affinity ligands, Amino acids, Authorsand publisher, Backbone bonds, Bind, Binding domains, Binding pocket, Binding site, Binding sites, Binding specificity, Biol, Biological relevance, Carboxyl tail, Catalytic, Catalytic activity, Catalytic domain, Conformational change, Critical pros, Crystal structure, Crystal structures, Domain, Domain specificity, Domains bind, Dynamin, Embo, Enzymatic activities, Family tyrosine kinases, Globular proteins, Grb2, Growth factor receptor, Growth factors, Helix, High affinity, High affinity ligands, High affinity phosphotyrosyl peptide, Homology, Hydrogen bonds, Hydrophobic, Hydrophobic residues, Important role, Insulin receptor, Insulin receptor kinase, Kinase, Ligand, Ligand binding, Ligated, Ligated peptides, Local concentration, Localization, Many investigators, Many proteins, Modular binding domains, Musacchio, Mutation, Mutational analysis, Nature struct, Nonlinear sequences, Nonreceptor tyrosine kinases, Other domains, Other molecules, Other proteins, Oxidase, Pathway, Pawson, Pdgf receptor, Pdgfr, Peptide, Peptide backbone, Peptide chain, Phagocyte nadph oxidase, Phagocyte nadph oxidase system, Phenol ring, Phosphatase, Phosphatidylinositol, Phosphopeptides, Phosphoprotein, Phosphorylated, Phosphorylation, Phosphorylation sites, Pi3k, Plasma membrane, Pleckstrin, Pleckstrin homology domain, Ppii, Ppii helices, Ppii helix, Protein, Protein complexes, Ptyr, Pxxp motif, Quiescent cells, Receptor, Residue, Schlessinger, Selectivity, Sh2s, Shoelson, Side chain, Side chains, Signal transducers, Signal transduction, Signal transduction pathways, Signal transduction proteins, Single residue, Solution structure, Songyang, Structural basis, Structural evidence, Structural studies, Subcellular localization, Transcription factors, Transduction, Trends biochem, Trends cell biol, Trigonal prism, Tyrosine, Tyrosine kinase, Tyrosine kinases, Variable loops, Waksman, Wide variety.

Url:

• https://api.istex.fr/ark:/67375/6H6-W721DZ1B-5/fulltext.pdf

DOI: 10.1016/0092-8674(95)90406-9

Affiliations:

• États-Unis

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