Small Molecule Inhibitors of the PCSK9·LDLR Interaction-Reference-Cited by-同舟云学术

Small Molecule Inhibitors of the PCSK9·LDLR Interaction

Published:2018-01-29 Issue:9 Volume:140 Page:3242-3249
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Taechalertpaisarn Jaru¹,Zhao Bosheng¹,Liang Xiaowen²,Burgess Kevin¹^ORCID

Affiliation:

1. Department of Chemistry, Texas A & M University, Box 30012, College Station, Texas 77842, United States

2. Center for Infectious and Inflammatory Diseases, Institute of Biosciences and Technology (IBT), Texas A&M Health Science Center, Houston, Texas 77030, United States

Funder

Welch Foundation

Congressionally Directed Medical Research Programs

Cancer Prevention and Research Institute of Texas

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.7b09360

Reference56 articles.

1. PCSK9 and LDL cholesterol: unravelling the target to design the bullet

2. Secreted PCSK9 promotes LDL receptor degradation independently of proteolytic activity

3. Catalytic Activity Is Not Required for Secreted PCSK9 to Reduce Low Density Lipoprotein Receptors in HepG2 Cells

4. Targeting PCSK9 for Hypercholesterolemia

5. Interaction between the ligand-binding domain of the LDL receptor and the C-terminal domain of PCSK9 is required for PCSK9 to remain bound to the LDL receptor during endosomal acidification

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