Human Cellular Retinol Binding Protein II Forms a Domain‐Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering-Reference-Cited by-同舟云学术

Human Cellular Retinol Binding Protein II Forms a Domain‐Swapped Trimer Representing a Novel Fold and a New Template for Protein Engineering

Published:2020-08-14 Issue:22 Volume:21 Page:3192-3196
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Ghanbarpour Alireza¹²,Santos Elizabeth M.¹³,Pinger Cody⁴,Assar Zahra⁵,Hossaini Nasr Seyedmehdi¹,Vasileiou Chrysoula¹,Spence Dana⁴,Borhan Babak¹,Geiger James H.¹^ORCID

Affiliation:

1. Department of Chemistry Michigan State University 578 S. Shaw Lane East Lansing MI 48824 USA

2. Yale University Medical School Department of Cell Biology 333 S. Cedar Street New Haven CT 06510 USA

3. Dow Performance Silicones 2200W Salzburg Road Midland MI 48686 USA

4. Department of Biomedical Engineering Michigan State University 775 Woodlot Drive East Lansing MI 48823 USA

5. Cayman Chemical 1180 East Ellsworth Road Ann Arbor MI 48108 USA

Funder

National Institutes of Health

U.S. Department of Energy

Michigan Economic Development Corporation

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.202000405

Reference51 articles.

1. Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states

2. Protein-protein interactions: A review of protein dimer structures

3. Protein oligomerization: How and why

4. A review on protein oligomerization process

5. Protein oligomerization as a metabolic control mechanism: Application to apoE

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