Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities - Wikidata - awgldk - TriplyDB

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

http://www.wikidata.org/entity/Q37170396

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Conformational changes within the HLA-A1:MAGE-A1 complex induced by binding of a recombinant antibody fragment with TCR-like specificity Germ Line-governed Recognition of a Cancer Epitope by an Immunodominant Human T-cell Receptor T Cell Receptor Cross-reactivity Directed by Antigen-Dependent Tuning of Peptide-MHC Molecular Flexibility Genetic and Structural Basis for Selection of a Ubiquitous T Cell Receptor Deployed in Epstein-Barr Virus Infection Minimal conformational plasticity enables TCR cross-reactivity to different MHC class II heterodimers Loss of T Cell Antigen Recognition Arising from Changes in Peptide and Major Histocompatibility Complex Protein Flexibility: IMPLICATIONS FOR VACCINE DESIGN Disparate Degrees of Hypervariable Loop Flexibility Control T-Cell Receptor Cross-Reactivity, Specificity, and Binding Mechanism T-cell Receptor Specificity Maintained by Altered Thermodynamics Increased peptide contacts govern high affinity binding of a modified TCR whilst maintaining a native pMHC docking mode Structure of a TCR-Mimic Antibody with Target Predicts Pharmacogenetics.Exploration of the Conformational Dynamics of Major Histocompatibility Complex Molecules.Understanding TR binding to pMHC complexes: how does a TR scan many pMHC complexes yet preferentially bind to one.Heterologous Immunity between Adenoviruses and Hepatitis C Virus: A New Paradigm in HCV Immunity and Vaccines.Differential temperature-dependent multimeric assemblies of replication and repair polymerases on DNA increase processivity.Cross-reactivity of T cells and its role in the immune system Differential utilization of binding loop flexibility in T cell receptor ligand selection and cross-reactivity.Methods for quantifying T cell receptor binding affinities and thermodynamics.Hotspot autoimmune T cell receptor binding underlies pathogen and insulin peptide cross-reactivity.Structure-Based, Rational Design of T Cell Receptors.Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes.T-cell receptor binding affinities and kinetics: impact on T-cell activity and specificity.The versatility of the αβ T-cell antigen receptor.TCR scanning of peptide/MHC through complementary matching of receptor and ligand molecular flexibility.Structural and biophysical determinants of αβ T-cell antigen recognition.Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism.A structural voyage toward an understanding of the MHC-I-restricted immune response: lessons learned and much to be learned.Phage Display Engineered T Cell Receptors as Tools for the Study of Tumor Peptide-MHC Interactions.Peptide and Peptide-Dependent Motions in MHC Proteins: Immunological Implications and Biophysical Underpinnings.Revealing the peptide presenting process of human leukocyte antigen through the analysis of fluctuation Combinations of affinity-enhancing mutations in a T cell receptor reveal highly nonadditive effects within and between complementarity determining regions and chains.A Molecular Switch Abrogates Glycoprotein 100 (gp100) T-cell Receptor (TCR) Targeting of a Human Melanoma Antigen.The contribution of major histocompatibility complex contacts to the affinity and kinetics of T cell receptor binding Structural basis for ineffective T-cell responses to MHC anchor residue-improved "heteroclitic" peptides.Proximity of TCR and its CD8 coreceptor controls sensitivity of T cells.Novel cellular microarray assay for profiling T-cell peptide antigen specificities.Insights into the structure of the LC13 TCR/HLA-B8-EBV peptide complex with molecular dynamics simulations.Absolute free energies of biomolecules from unperturbed ensembles.Unexpected T-cell recognition of an altered peptide ligand is driven by reversed thermodynamics.Microfluidic platform for characterizing TCR-pMHC interactions.A study of CDR3 loop dynamics reveals distinct mechanisms of peptide recognition by T-cell receptors exhibiting different levels of cross-reactivity.

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Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

http://www.wikidata.org/entity/Q37170396

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on July 2008

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

@en

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities.

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type

label

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

@en

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities.

@nl

prefLabel

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

@en

Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities.

@nl

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Journal of Molecular Recognition

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Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities

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P2093

Brian M Baker

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Francis K Insaidoo

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Kathryn M Armstrong

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P2860

Application of a Theory of Enzyme Specificity to Protein Synthesis

Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor

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

Poor binding of a HER-2/neu epitope (GP2) to HLA-A2.1 is due to a lack of interactions with the center of the peptide

Two different, highly exposed, bulged structures for an unusually long peptide bound to rat MHC class I RT1-Aa

Class I major histocompatibility complex anchor substitutions alter the conformation of T cell receptor contacts

High-resolution structure of HLA-A*0201 in complex with a tumour-specific antigenic peptide encoded by the MAGE-A4 gene

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

Structural Basis of Cytochrome c Presentation by IE k

CDR3 loop flexibility contributes to the degeneracy of TCR recognition

P304

275-287

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scholarly article

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10.1002/JMR.896

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4

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21

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2008-07-01T00:00:00Z

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5353056

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18496839

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3674762

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