Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains (Q34214306)

31 July 2017

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title

Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains (English)

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31 July 2017

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Muyldermans S

1

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31 July 2017

Cambillau C

series ordinal

2

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31 July 2017

Wyns L

series ordinal

3

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31 July 2017

language of work or name

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1 April 2001

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31 July 2017

number of pages

6

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Trends in Biochemical Sciences

inferred from page(s)

published in

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31 July 2017

volume

26

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31 July 2017

issue

4

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31 July 2017

page(s)

230-235

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Anatomy of the antibody molecule

31 July 2017

cites work

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X-ray crystallography of antibodies.

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Length distribution of CDRH3 in antibodies

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

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Canonical structures for the hypervariable regions of immunoglobulins

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Structural conservation of hypervariable regions in immunoglobulins evolution

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Standard conformations for the canonical structures of immunoglobulins

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Conformations of immunoglobulin hypervariable regions

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Structural families in loops of homologous proteins: automatic classification, modelling and application to antibodies

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Conformations of the third hypervariable region in the VH domain of immunoglobulins

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H3-rules: identification of CDR-H3 structures in antibodies

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Naturally occurring antibodies devoid of light chains

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Induction of immune responses and molecular cloning of the heavy chain antibody repertoire of Lama glama

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Comparison of llama VH sequences from conventional and heavy chain antibodies

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

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Structural determinants in the sequences of immunoglobulin variable domain 1 1Edited by A. R. Fersht

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Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire

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The human immunoglobulin VH repertoire

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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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Natural and designer binding sites made by phage display technology

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Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae

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A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops

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

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The crystal structure of a llama heavy chain variable domain

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Camelid heavy-chain variable domains provide efficient combining sites to haptens

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

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'Camelising' human antibody fragments: NMR studies on VH domains.

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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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Both DNA strands of antibody genes are hypermutation targets

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7 January 2021

Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?

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Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate

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The atomic structure of protein-protein recognition sites

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Potent enzyme inhibitors derived from dromedary heavy-chain antibodies

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Redefining the minimal antigen-binding fragment

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Scaffolds for engineering novel binding sites in proteins

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Recombinant antibody fragments

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Identifiers

DOI

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31 July 2017

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