How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides? - sprookjes - yvandenbroek - TriplyDB

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'Structures of MART-126/27–35 Peptide/HLA-A2 Complexes Reveal a Remarkable Disconnect between Antigen Structural Homology and T Cell Recognition How a T Cell Receptor-like Antibody Recognizes Major Histocompatibility Complex-bound Peptide 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 † ‡T Cell Receptor Cross-reactivity Directed by Antigen-Dependent Tuning of Peptide-MHC Molecular Flexibility Conformational Melding Permits a Conserved Binding Geometry in TCR Recognition of Foreign and Self Molecular Mimics 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 Disparate Epitopes Mediating Protective Heterologous Immunity to Unrelated Viruses Share Peptide-MHC Structural Features Recognized by Cross-Reactive T Cells 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 What Is Direct Allorecognition?Structural insights into the editing of germ-line-encoded interactions between T-cell receptor and MHC class II by Vα CDR3 The molecular basis of TCR germline bias for MHC is surprisingly simple T cell receptor bias for MHC: co-evolution or co-receptors?Peptide modulation of class I major histocompatibility complex protein molecular flexibility and the implications for immune recognition.Force measurements of TCR/pMHC recognition at T cell surface DynaDom: structure-based prediction of T cell receptor inter-domain and T cell receptor-peptide-MHC (class I) association angles.High-affinity T cell receptor differentiates cognate peptide-MHC and altered peptide ligands with distinct kinetics and thermodynamics.Understanding TR binding to pMHC complexes: how does a TR scan many pMHC complexes yet preferentially bind to one.T-cell receptors binding orientation over peptide/MHC class I is driven by long-range interactions Structural and dynamical insights on HLA-DR2 complexes that confer susceptibility to multiple sclerosis in Sardinia: a molecular dynamics simulation study Vgamma2Vdelta2 T Cell Receptor recognition of prenyl pyrophosphates is dependent on all CDRs Generation of MHC class II-peptide ligands for CD4 T-cell allorecognition of MHC class II molecules.The Dynamics of the Human Leukocyte Antigen Head Domain Modulates Its Recognition by the T-Cell Receptor.Generation of CD20-specific TCRs for TCR gene therapy of CD20low B-cell malignancies insusceptible to CD20-targeting antibodies.Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity.Epitope-specificity of recombinant antibodies reveals promiscuous peptide-binding properties.A long journey coming to fruition: In sight of the preselection T-cell repertoire Differential utilization of binding loop flexibility in T cell receptor ligand selection and cross-reactivity.Recognition of self-peptide-MHC complexes by autoimmune T-cell receptors.Evolutionarily conserved amino acids that control TCR-MHC interaction.Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes.Alloreactive cytotoxic T cells provide means to decipher the immunopeptidome and reveal a plethora of tumor-associated self-epitopes.The structural bases of direct T-cell allorecognition: implications for T-cell-mediated transplant rejection.Mechanisms controlling granule-mediated cytolytic activity of cytotoxic T lymphocytes.

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

http://www.wikidata.org/entity/Q27644089

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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2007年の論文

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2007年論文

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2007年論文

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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label

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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prefLabel

How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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SJ.EMBOJ.7601605

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The EMBO Journal

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How much can a T-cell antigen receptor adapt to structurally distinct antigenic peptides?

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Alain Roussel

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Alice Kearney

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Catherine Mazza

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Christine Kellenberger

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Claude Gregoire

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P2860

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical

Crystal structure of a T cell receptor bound to an allogeneic MHC molecule

Structural and functional consequences of altering a peptide MHC anchor residue

A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex

A structural basis for the selection of dominant alphabeta T cell receptors in antiviral immunity

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

Crystal structure of the major histocompatibility complex class I H-2Kb molecule containing a single viral peptide: implications for peptide binding and T-cell receptor recognition

Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen

Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids

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1972-83

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2020860

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10.1038/SJ.EMBOJ.7601605

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7

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Bernard Malissen

Anne-Marie Schmitt-Verhulst

Nathalie Auphan-Anezin

Philip Anton van der Merwe

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2007-04-04T00:00:00Z

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6443131

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17363906

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1847653

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