B-box1 Domain of MID1 Interacts with the Ube2D1 E2 Enzyme Differently Than RING E3 Ligases
Author:
Affiliation:
1. Department of Chemistry, George Washington University, 800 22nd St NW, Washington, D.C. 20052, United States
Funder
Division of Chemistry
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.2c00693
Reference94 articles.
1. X-linked Opitz syndrome: Novel mutations in theMID1gene and redefinition of the clinical spectrum
2. MID1 Catalyzes the Ubiquitination of Protein Phosphatase 2A and Mutations within Its Bbox1 Domain Disrupt Polyubiquitination of Alpha4 but Not of PP2Ac
3. Subclassification of the RBCC/TRIM Superfamily Reveals a Novel Motif Necessary for Microtubule Binding
4. Detection and Characterization of the In Vitro E3 Ligase Activity of the Human MID1 Protein
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1. Absence of the RING domain inMID1results in patterning defects in the developing human brain;Life Science Alliance;2024-01-18
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