Maturation of an antibody response is governed by modulations in flexibility of the antigen-combining site (Q73291744)

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2 November 2019

title

Maturation of an antibody response is governed by modulations in flexibility of the antigen-combining site (English)

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2 November 2019

author name string

V Manivel

1

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2 November 2019

N C Sahoo

2

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2 November 2019

D M Salunke

3

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2 November 2019

K V Rao

4

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2 November 2019

publication date

1 November 2000

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2 November 2019

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2 November 2019

volume

13

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2 November 2019

issue

5

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2 November 2019

page(s)

611-620

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Structural analysis of antibody specificity. Detailed comparison of five Fab'-steroid complexes

2 November 2019

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Crystal Structure of the Complex of the Variable Domain of Antibody D1.3 and Turkey Egg White Lysozyme: A Novel Conformational Change in Antibody CDR-L3 Selects for Antigen

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The structural basis of repertoire shift in an immune response to phosphocholine

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Molecular dynamics and free-energy calculations applied to affinity maturation in antibody 48G7.

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Kinetic and affinity limits on antibodies produced during immune responses

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Junctional amino acids determine the maturation pathway of an antibody.

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

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Principles of protein-protein recognition from structure to thermodynamics

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A very high level of crossreactivity is an essential feature of the T-cell receptor

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B cell responses to a peptide epitope. X. Epitope selection in a primary response is thermodynamically regulated

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Selection in a T-dependent primary humoral response: new insights from polypeptide models.

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Structural evidence for induced fit as a mechanism for antibody-antigen recognition

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Early high-affinity neutralizing anti-viral IgG responses without further overall improvements of affinity

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Protein−Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis

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The Imprint of Somatic Hypermutation on the Repertoire of Human Germline V Genes

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The affinity maturation of anti-4-hydroxy-3-nitrophenylacetyl mouse monoclonal antibody. A calorimetric study of the antigen-antibody interaction

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Role of salt bridge formation in antigen-antibody interaction. Entropic contribution to the complex between hen egg white lysozyme and its monoclonal antibody HyHEL10

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Altering the antibody repertoire via transgene homologous recombination: evidence for global and clone-autonomous regulation of antigen-driven B cell differentiation

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Structural insights into the evolution of an antibody combining site

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TCR binding to peptide-MHC stabilizes a flexible recognition interface

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Antibody-antigen interactions: new structures and new conformational changes

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Evolution of shape complementarity and catalytic efficiency from a primordial antibody template

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Mutational analysis of the affinity maturation of antibody 48G7.

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7 January 2021

Imperfect interfaces.

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7 January 2021

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Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11114374%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

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