Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal. - Test2 - elhamkhani - TriplyDB

Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

http://www.wikidata.org/entity/Q37208000

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Epitopes rationally selected through computational analyses induce T-cell proliferation in mice and are recognized by serum from individuals infected with Schistosoma mansoni.

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

http://www.wikidata.org/entity/Q37208000

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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 October 2013

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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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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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FIMMU.2013.00308

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Frontiers in Immunology

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Thermodynamics of Peptide-MHC Class II Interactions: Not all Complexes are Created Equal.

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Andrea Ferrante

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HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive mechanism

Crystal Structure of the HLA-DM–HLA-DR1 Complex Defines Mechanisms for Rapid Peptide Selection

Conformational lability in the class II MHC 310 helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange

The mechanism of action of tapasin in the peptide exchange on MHC class I molecules determined from kinetics simulation studies

Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM

SYFPEITHI: database for MHC ligands and peptide motifs

Enthalpy-entropy compensation and cooperativity as thermodynamic epiphenomena of structural flexibility in ligand-receptor interactions

Identification of destabilizing residues in HLA class II-selected bacteriophage display libraries edited by HLA-DM.

Improving MHC binding peptide prediction by incorporating binding data of auxiliary MHC molecules.

Cooperativity, partially bound states, and enthalpy-entropy compensation.

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scholarly article

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10.3389/FIMMU.2013.00308

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2013-10-01T00:00:00Z

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