1996
Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (∗)
Mandiyan V, O'Brien R, Zhou M, Margolis B, Lemmon M, Sturtevant J, Schlessinger J. Thermodynamic Studies of SHC Phosphotyrosine Interaction Domain Recognition of the NPXpY Motif (∗). Journal Of Biological Chemistry 1996, 271: 4770-4775. PMID: 8617744, DOI: 10.1074/jbc.271.9.4770.Peer-Reviewed Original ResearchAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceBinding SitesCalorimetryErbB ReceptorsGlutathione TransferaseMolecular Sequence DataMutagenesis, Site-DirectedPeptide FragmentsPhosphotyrosinePoint MutationProtein BiosynthesisProteinsRecombinant Fusion ProteinsShc Signaling Adaptor ProteinsSrc Homology DomainsThermodynamics
1994
Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck.
Lemmon MA, Ladbury JE. Thermodynamic studies of tyrosyl-phosphopeptide binding to the SH2 domain of p56lck. Biochemistry 1994, 33: 5070-6. PMID: 7513553, DOI: 10.1021/bi00183a010.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBinding SitesCalorimetryCloning, MolecularConserved SequenceErbB ReceptorsEscherichia coliLymphocyte Specific Protein Tyrosine Kinase p56(lck)LymphocytesMolecular Sequence DataPeptide FragmentsPhosphopeptidesPhosphotyrosineProtein-Tyrosine KinasesRecombinant ProteinsSequence Homology, Amino AcidTyrosine