Comparison of llama VH sequences from conventional and heavy chain antibodies (Q57985853)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9566760%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

title

Comparison of llama VH sequences from conventional and heavy chain antibodies (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9566760%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

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K B Vu

1

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11 November 2019

M A Ghahroudi

series ordinal

2

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11 November 2019

publication date

1 November 1997

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11 November 2019

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11 November 2019

volume

34

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11 November 2019

issue

16-17

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11 November 2019

page(s)

1121-1131

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Molecular analysis of spontaneous somatic mutants

11 November 2019

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Somatic diversification of immunoglobulin heavy chain VDJ genes: evidence for somatic gene conversion in rabbits

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Use of antibody fragments in immunoaffinity chromatography. Comparison of FV fragments, VH fragments and paralog peptides

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Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

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Kinetic analysis of recombinant antibody-antigen interactions: relation between structural domains and antigen binding

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The outline structure of the T-cell alpha beta receptor.

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Structural repertoire of the human VH segments

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Antibody VH domains as small recognition units

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Single antibody domains as small recognition units: design and in vitro antigen selection of camelized, human VH domains with improved protein stability

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Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme

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Selection and identification of single domain antibody fragments from camel heavy-chain antibodies

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Naturally occurring antibodies devoid of light chains

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BiP binding sequences in antibodies.

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Organization and evolution of variable region genes of the human immunoglobulin heavy chain

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Elbow motion in the immunoglobulins involves a molecular ball-and-socket joint

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Murine heavy chain disease

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Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains

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Anatomy of the antibody molecule

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Identification of specificity-determining residues in antibodies

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Somatic hyperconversion diversifies the single Vh gene of the chicken with a high incidence in the D region

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Rearrangement of the former VL interface in the solution structure of a camelised, single antibody VH domain

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Structural patterns at residue positions 9, 18, 67 and 82 in the VH framework regions of human and murine immunoglobulins

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7 January 2021

Structural implications of VH sequence patterns

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7 January 2021

Dynamic aspects of antibody structure

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7 January 2021

Structure and evolution of mammalian VH families

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Redefining the minimal antigen-binding fragment

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7 January 2021

The crystal structure of a llama heavy chain variable domain

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7 January 2021

The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops

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7 January 2021

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

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Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli

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Rearrangement/hypermutation/gene conversion: when, where and why?

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Length distribution of CDRH3 in antibodies

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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:9566760%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

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