Effects of Desialylation on Human α1-Acid Glycoprotein–Ligand Interactions-Reference-Cited by-同舟云学术

Effects of Desialylation on Human α1-Acid Glycoprotein–Ligand Interactions

Published:2013-09-27 Issue:40 Volume:52 Page:7127-7136
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Huang Richard Y.-C.¹²,Hudgens Jeffrey W.¹²

Affiliation:

1. Bioprocess Measurements Group, Biomolecular Measurement Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899, United States

2. Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi4011094

Reference40 articles.

1. The 1.8-Å Crystal Structure of α1-Acid Glycoprotein (Orosomucoid) Solved by UV RIP Reveals the Broad Drug-Binding Activity of This Human Plasma Lipocalin

2. Disulfide bonds of α1-acid glycoprotein

3. Structure of human α1-acid glycoprotein and its high-affinity binding site

4. HUMAN ALPHA-1-GLYCOPROTEIN AND ITS INTERACTIONS WITH DRUGS†,‡

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