A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF

TNF can be inhibited by small molecules that stabilize the TNF trimer in an asymmetric conformation. Here, the authors develop a monoclonal antibody that selectively binds this inactive form of TNF, enabling both target engagement assessment and structural characterization of TNF binding to TNF rece...

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Autores principales:	Daniel J. Lightwood, Rebecca J. Munro, John Porter, David McMillan, Bruce Carrington, Alison Turner, Anthony Scott-Tucker, Elizabeth S. Hickford, Antje Schmidt, David Fox, Alison Maloney, Tom Ceska, Tim Bourne, James O’Connell, Alastair D. G. Lawson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a700e6f6d0e341fa8bbbdf0203d53866
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spelling	oai:doaj.org-article:a700e6f6d0e341fa8bbbdf0203d538662021-12-02T13:57:54ZA conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF10.1038/s41467-020-20825-62041-1723https://doaj.org/article/a700e6f6d0e341fa8bbbdf0203d538662021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20825-6https://doaj.org/toc/2041-1723TNF can be inhibited by small molecules that stabilize the TNF trimer in an asymmetric conformation. Here, the authors develop a monoclonal antibody that selectively binds this inactive form of TNF, enabling both target engagement assessment and structural characterization of TNF binding to TNF receptor 1.Daniel J. LightwoodRebecca J. MunroJohn PorterDavid McMillanBruce CarringtonAlison TurnerAnthony Scott-TuckerElizabeth S. HickfordAntje SchmidtDavid FoxAlison MaloneyTom CeskaTim BourneJames O’ConnellAlastair D. G. LawsonNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Daniel J. Lightwood Rebecca J. Munro John Porter David McMillan Bruce Carrington Alison Turner Anthony Scott-Tucker Elizabeth S. Hickford Antje Schmidt David Fox Alison Maloney Tom Ceska Tim Bourne James O’Connell Alastair D. G. Lawson A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF
description	TNF can be inhibited by small molecules that stabilize the TNF trimer in an asymmetric conformation. Here, the authors develop a monoclonal antibody that selectively binds this inactive form of TNF, enabling both target engagement assessment and structural characterization of TNF binding to TNF receptor 1.
format	article
author	Daniel J. Lightwood Rebecca J. Munro John Porter David McMillan Bruce Carrington Alison Turner Anthony Scott-Tucker Elizabeth S. Hickford Antje Schmidt David Fox Alison Maloney Tom Ceska Tim Bourne James O’Connell Alastair D. G. Lawson
author_facet	Daniel J. Lightwood Rebecca J. Munro John Porter David McMillan Bruce Carrington Alison Turner Anthony Scott-Tucker Elizabeth S. Hickford Antje Schmidt David Fox Alison Maloney Tom Ceska Tim Bourne James O’Connell Alastair D. G. Lawson
author_sort	Daniel J. Lightwood
title	A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF
title_short	A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF
title_full	A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF
title_fullStr	A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF
title_full_unstemmed	A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF
title_sort	conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of tnf
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a700e6f6d0e341fa8bbbdf0203d53866
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A conformation-selective monoclonal antibody against a small molecule-stabilised signalling-deficient form of TNF

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