Rational Design of High Affinity Interaction Between CC Chemokine Binding Protein vCCI and CCL17/TARC-Reference-Cited by-同舟云学术

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Rational Design of High Affinity Interaction Between CC Chemokine Binding Protein vCCI and CCL17/TARC

Published:2024-08-28 Issue: Volume: Page:
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Guan Wenyan¹,Stark Lauren E.¹,Zhang Ning¹^ORCID,Bains Arjan¹,Martinez Airam¹,Dupureur Cynthia M.²,Colvin Michael E.¹,LiWang Patricia J.¹³^ORCID

Affiliation:

1. School of Natural Sciences, University of California Merced, 5200 North Lake Rd., Merced, California 95343, United States

2. Department of Chemistry and Biochemistry, University of Missouri-St. Louis, St. Louis, Missouri 63043, United States

3. Health Sciences Research Institute, University of California, Merced, Merced, California 95343, United States

Funder

Army Research Office

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.4c00298

Reference12 articles.

1. Deriving Immune Modulating Drugs from Viruses—A New Class of Biologics

2. Comprehensive Mapping of Poxvirus vCCI Chemokine-binding Protein

3. Efficient production of fluorophore‐labeled CC chemokines for biophysical studies using recombinant enterokinase and recombinant sortase

4. Structural Insights into the Interaction between a Potent Anti-inflammatory Protein, Viral CC Chemokine Inhibitor (vCCI), and the Human CC Chemokine, Eotaxin-1

5. Solution structure of the complex between poxvirus-encoded CC chemokine inhibitor vCCI and human MIP-1beta

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