about
A "three-pronged" binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndromeSide-chain dynamics of the SAP SH2 domain correlate with a binding hot spot and a region with conformational plasticityStructure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptideCorrelation between dynamics and high affinity binding in an SH2 domain interactionIdentification and characterization of human genes encoding Hprp3p and Hprp4p, interacting components of the spliceosomeInteractions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitinationNMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domainAutoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domainpE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteinsPolyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivityMultiple modes of peptide recognition by the PTB domain of the cell fate determinant NumbSolution structure of a Nedd4 WW domain-ENaC peptide complexSolution structure and dynamics of the outer membrane enzyme PagP by NMR.Structural, Functional, and Bioinformatic Studies Demonstrate the Crucial Role of an Extended Peptide Binding Site for the SH3 Domain of Yeast Abp1pStructural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arraysCoupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificityComposite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligaseFolding of an intrinsically disordered protein by phosphorylation as a regulatory switchStructure of a Numb PTB domain-peptide complex suggests a basis for diverse binding specificityBackbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxationAn expanded WW domain recognition motif revealed by the interaction between Smad7 and the E3 ubiquitin ligase Smurf2High populations of non-native structures in the denatured state are compatible with the formation of the native folded stateDifferential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysisAllosteric coupling between the intracellular coupling helix 4 and regulatory sites of the first nucleotide-binding domain of CFTRNMR studies of tandem WW domains of Nedd4 in complex with a PY motif-containing region of the epithelial sodium channelAn allosteric conduit facilitates dynamic multisite substrate recognition by the SCF(Cdc4) ubiquitin ligaseBackbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniquesConformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer ModelEnsemble modeling of protein disordered states: experimental restraint contributions and validation.15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3.Megakaryocyte and platelet abnormalities in a patient with a W33C mutation in the conserved SH3-like domain of myosin heavy chain IIA.Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints.Improved structural characterizations of the drkN SH3 domain unfolded state suggest a compact ensemble with native-like and non-native structure.Oxygen as a paramagnetic probe of clustering and solvent exposure in folded and unfolded states of an SH3 domain.19F NMR studies of solvent exposure and peptide binding to an SH3 domain.Tryptophan solvent exposure in folded and unfolded states of an SH3 domain by 19F and 1H NMR.Characterization of the hydrodynamic properties of the folding transition state of an SH3 domain by magnetization transfer NMR spectroscopy.Hydration and packing along the folding pathway of SH3 domains by pressure-dependent NMR.Structural comparison of the unstable drkN SH3 domain and a stable mutant.
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description
hulumtuese
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researcher
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հետազոտող
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name
Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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Julie D Forman-Kay
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P106
P21
P31
P496
0000-0001-8265-972X