↓ Skip to main content

Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1

Overview of attention for article published in BMC Biology, May 2011
Altmetric Badge

Mentioned by

wikipedia
1 Wikipedia page

Citations

dimensions_citation
63 Dimensions

Readers on

mendeley
77 Mendeley
You are seeing a free-to-access but limited selection of the activity Altmetric has collected about this research output. Click here to find out more.
Title
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1
Published in
BMC Biology, May 2011
DOI 10.1186/1741-7007-9-33
Pubmed ID
Authors

Tara A Gomez, Natalie Kolawa, Marvin Gee, Michael J Sweredoski, Raymond J Deshaies

Abstract

The proteasome is a multi-subunit protein machine that is the final destination for cellular proteins that have been marked for degradation via an ubiquitin (Ub) chain appendage. These ubiquitylated proteins either bind directly to the intrinsic proteasome ubiqutin chain receptors Rpn10, Rpn13, or Rpt5, or are shuttled to the proteasome by Rad23, Dsk2, or Ddi1. The latter proteins share an Ub association domain (UBA) for binding poly-Ub chains and an Ub-like-domain (UBL) for binding to the proteasome. It has been proposed that shuttling receptors dock on the proteasome via Rpn1, but the precise nature of the docking site remains poorly defined.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 77 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 2 3%
Unknown 75 97%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 28 36%
Researcher 10 13%
Student > Master 10 13%
Student > Bachelor 7 9%
Student > Doctoral Student 6 8%
Other 9 12%
Unknown 7 9%
Readers by discipline Count As %
Agricultural and Biological Sciences 36 47%
Biochemistry, Genetics and Molecular Biology 21 27%
Chemistry 4 5%
Medicine and Dentistry 3 4%
Pharmacology, Toxicology and Pharmaceutical Science 1 1%
Other 5 6%
Unknown 7 9%