Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies-Reference-Cited by-同舟云学术

Using homology modeling to interrogate binding affinity in neutralization of ricin toxin by a family of single domain antibodies

Published:2017-08-04 Issue:11 Volume:85 Page:1994-2008
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Bazzoli Andrea¹²,Vance David J.³^ORCID,Rudolph Michael J.⁴,Rong Yinghui³,Angalakurthi Siva Krishna⁵,Toth Ronald T.⁵,Middaugh C. Russell⁵,Volkin David B.⁵,Weis David D.⁶^ORCID,Karanicolas John¹⁷⁸,Mantis Nicholas J.³^ORCID

Affiliation:

1. Center for Computational Biology; University of Kansas; Lawrence Kansas 66045

2. Computational Chemical Biology Core; University of Kansas; Lawrence Kansas 66047

3. New York State Department of Health; Division of Infectious Diseases, Wadsworth Center; Albany New York 12208

4. New York Structural Biology Center; New York New York 10027

5. Department of Pharmaceutical Chemistry; Macromolecule and Vaccine Stabilization Center, University of Kansas; Lawrence Kansas 66045

6. Department of Chemistry; University of Kansas; Lawrence Kansas 66045

7. Department of Molecular Biosciences; University of Kansas; Lawrence Kansas 66045

8. Program in Molecular Therapeutics, Fox Chase Cancer Center; Philadelphia Pennsylvania 19111

Funder

National Institutes of Allergy and Infectious Diseases

National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.25353/fullpdf

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4. Retrograde transport of protein toxins through the Golgi apparatus;Sandvig;Histochem Cell Biol.,2013

5. Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum;Spooner;Biochem J.,2004

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