Long-Range Conformational Changes in Monoclonal Antibodies Revealed Using FPOP-LC-MS/MS-Reference-Cited by-同舟云学术

Long-Range Conformational Changes in Monoclonal Antibodies Revealed Using FPOP-LC-MS/MS

Published:2019-11-05 Issue:23 Volume:91 Page:15163-15170
ISSN:0003-2700
Container-title:Analytical Chemistry
language:en
Short-container-title:Anal. Chem.

Author:

Cornwell Owen¹^ORCID,Bond Nicholas J.²,Radford Sheena E.¹^ORCID,Ashcroft Alison E.¹^ORCID

Affiliation:

1. Astbury Centre for Structural Molecular Biology and School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, U.K.

2. Analytical Sciences, BioPharmaceutical Development, BioPharmaceuticals R&D, AstraZeneca, Granta Park, Cambridge, CB21 6GH, U.K.

Funder

AstraZeneca

Biotechnology and Biological Sciences Research Council

Publisher

American Chemical Society (ACS)

Subject

Analytical Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acs.analchem.9b03958

Reference56 articles.

1. IgG cooperativity – Is there allostery? Implications for antibody functions and therapeutic antibody development

2. Revisiting the Immunoglobulin Intramolecular Signaling Hypothesis

3. Ig Constant Region Effects on Variable Region Structure and Function

4. Structural basis for binding of human IgG1 to its high-affinity human receptor FcγRI

5. Independence of the binding of domain-specific ligands to Fab and Fc suggests that antigen-induced effects in IgG antibodies are not allosteric

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