CDR3 loop flexibility contributes to the degeneracy of TCR recognition - sprookjes - yvandenbroek - TriplyDB

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

http://www.wikidata.org/entity/Q27640417

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Redundancy in antigen-presenting function of the HLA-DR and -DQ molecules in the multiple sclerosis-associated HLA-DR2 haplotype Quantitative challenges in understanding ligand discrimination by alphabeta T cells Evolving models of the immunopathogenesis of T cell-mediated drug allergy: The role of host, pathogens, and drug response.Adoptive T-cell therapy for Leukemia Beyond model antigens: high-dimensional methods for the analysis of antigen-specific T cells Surface-anchored monomeric agonist pMHCs alone trigger TCR with high sensitivity A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?Structures of MART-126/27–35 Peptide/HLA-A2 Complexes Reveal a Remarkable Disconnect between Antigen Structural Homology and T Cell Recognition Single MHC Mutation Eliminates Enthalpy Associated with T Cell Receptor Binding A New Twist in TCR Diversity Revealed by a Forbidden αβ TCR Crossreactive T Cells Spotlight the Germline Rules for αβ T Cell-Receptor Interactions with MHC Molecules Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation Different Thermodynamic Binding Mechanisms and Peptide Fine Specificities Associated with a Panel of Structurally Similar High-Affinity T Cell Receptors † ‡Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity T Cell Receptor Cross-reactivity Directed by Antigen-Dependent Tuning of Peptide-MHC Molecular Flexibility Hard wiring of T cell receptor specificity for the major histocompatibility complex is underpinned by TCR adaptability Structural Basis of Specificity and Cross-Reactivity in T Cell Receptors Specific for Cytochrome c-I-E A Single T Cell Receptor Bound to Major Histocompatibility Complex Class I and Class II Glycoproteins Reveals Switchable TCR Conformers Disparate Degrees of Hypervariable Loop Flexibility Control T-Cell Receptor Cross-Reactivity, Specificity, and Binding Mechanism T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex Crossreactivity of a human autoimmune TCR is dominated by a single TCR loop Effect of CDR3 Sequences and Distal V Gene Residues in Regulating TCR-MHC Contacts and Ligand Specificity Deconstructing the Peptide-MHC Specificity of T Cell Recognition High-Throughput Sequencing-Based Immune Repertoire Study during Infectious Disease What Is Direct Allorecognition?The CD8 T-cell response during tolerance induction in liver transplantation The molecular basis of TCR germline bias for MHC is surprisingly simple Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interaction Structure of a TCR-Mimic Antibody with Target Predicts Pharmacogenetics.DynaDom: structure-based prediction of T cell receptor inter-domain and T cell receptor-peptide-MHC (class I) association angles.Directed evolution of human T cell receptor CDR2 residues by phage display dramatically enhances affinity for cognate peptide-MHC without increasing apparent cross-reactivity.The effect of mutations on the alloreactive T cell receptor/peptide-MHC interface structure: a molecular dynamics study.Estimating the diversity, completeness, and cross-reactivity of the T cell repertoire.Structural biology of the T-cell receptor: insights into receptor assembly, ligand recognition, and initiation of signaling.TCRep 3D: an automated in silico approach to study the structural properties of TCR repertoires.Evolving concepts of specificity in immune reactions Vgamma2Vdelta2 T Cell Receptor recognition of prenyl pyrophosphates is dependent on all CDRs T cell receptor recognition of self and foreign antigens in the induction of autoimmunity.T cell receptor-ligand interactions: a conformational preequilibrium or an induced fit.

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P2860

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

http://www.wikidata.org/entity/Q27640417

description

2003 nî lūn-bûn

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2003 թուականի Մարտին հրատարակուած գիտական յօդուած

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2003 թվականի մարտին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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type

label

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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CDR3 loop flexibility contributes to the degeneracy of TCR recognition

@en

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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prefLabel

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

@ast

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

@en

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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Nature Immunology

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CDR3 loop flexibility contributes to the degeneracy of TCR recognition

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P2093

Alice Kearney

http://www.w3.org/2001/XMLSchema#string

Claude Grégoire

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Claudine Darnault

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Dominique Housset

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Gilbert Mazza

http://www.w3.org/2001/XMLSchema#string

Jean-Baptiste Reiser

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Juan Carlos Fontecilla-Camps

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Thomas Mosser

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241-7

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scholarly article

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1618307

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10.1038/NI891

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3

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4

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Bernard Malissen

Philip Anton van der Merwe

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2003-03-01T00:00:00Z

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10921354

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12563259

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