Conformational Changes Associated with Post-Translational Modifications of Pro143 in Skp1 of Dictyostelium—A Dipeptide Model System-Reference-Cited by-同舟云学术

Conformational Changes Associated with Post-Translational Modifications of Pro143 in Skp1 of Dictyostelium—A Dipeptide Model System

Published:2014-10-16 Issue:43 Volume:136 Page:15170-15175
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Karunaratne Chamini V.¹,Weldeghiorghis Thomas K.¹,West Christopher M.²,Taylor Carol M.¹

Affiliation:

1. Department of Chemistry, Louisiana State University, Baton Rouge, Louisiana 70803, United States

2. Department of Biochemistry & Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja5033277

Reference66 articles.

1. RING Domain E3 Ubiquitin Ligases

2. The Skp1 Prolyl Hydroxylase from Dictyostelium Is Related to the Hypoxia-inducible Factor-α Class of Animal Prolyl 4-Hydroxylases

3. Requirements for Skp1 Processing by Cytosolic Prolyl 4(trans)-Hydroxylase and α-N-Acetylglucosaminyltransferase Enzymes Involved in O2Signaling inDictyostelium

4. Prolyl 4-hydroxylase-1 mediates O2 signaling during development ofDictyostelium

5. Prolyl hydroxylation- and glycosylation-dependent functions of Skp1 in O2-regulated development of Dictyostelium

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