Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge
About this item
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Author / Creator
Maun, Henry R. , Vij, Rajesh , Walters, Benjamin T. , Morando, Ashley , Jackman, Janet K. , Wu, Ping , Estevez, Alberto , Chen, Xiaocheng , Franke, Yvonne , Lipari, Michael T. , Dennis, Mark S. , Kirchhofer, Daniel , Ciferri, Claudio , Loyet, Kelly M. , Yi, Tangsheng , Eigenbrot, Charles , Lazarus, Robert A. , Koerber, James T. and Stanford Univ., CA (United States)
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
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Publication information
Publisher
London: Nature Publishing Group UK
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Scope and Contents
Contents
Human β-tryptase, a tetrameric trypsin-like serine protease, is an important mediator of allergic inflammatory responses in asthma. Antibodies generally inhibit proteases by blocking substrate access by binding to active sites or exosites or by allosteric modulation. The bivalency of IgG antibodies can increase potency via avidity, but has never be...
Alternative Titles
Full title
Bivalent antibody pliers inhibit β-tryptase by an allosteric mechanism dependent on the IgG hinge
Authors, Artists and Contributors
Author / Creator
Vij, Rajesh
Walters, Benjamin T.
Morando, Ashley
Jackman, Janet K.
Wu, Ping
Estevez, Alberto
Chen, Xiaocheng
Franke, Yvonne
Lipari, Michael T.
Dennis, Mark S.
Kirchhofer, Daniel
Ciferri, Claudio
Loyet, Kelly M.
Yi, Tangsheng
Eigenbrot, Charles
Lazarus, Robert A.
Koerber, James T.
Stanford Univ., CA (United States)
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_731be2a1b0e94f0d9e6e6bb1c65b39da
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_731be2a1b0e94f0d9e6e6bb1c65b39da
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-020-20143-x
