K
Kylie J. Walters
Researcher at National Institutes of Health
Publications - 84
Citations - 5406
Kylie J. Walters is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Ubiquitin & Proteasome. The author has an hindex of 35, co-authored 71 publications receiving 4725 citations. Previous affiliations of Kylie J. Walters include Harvard University & University of Minnesota.
Papers
More filters
Journal ArticleDOI
Ubiquitin-binding domains — from structures to functions
TL;DR: New structure-based insights provide strategies for controlling cellular processes by targeting ubiquitin–UBD interfaces with implications for drug design and cell reprograming.
Journal ArticleDOI
Proteasome subunit Rpn13 is a novel ubiquitin receptor
Koraljka Husnjak,Suzanne Elsasser,Naixia Zhang,Xiang Chen,Leah Randles,Yuan Shi,Kay Hofmann,Kylie J. Walters,Daniel Finley,Ivan Dikic,Ivan Dikic +10 more
TL;DR: The identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome, is reported, suggesting a coupling of chain recognition and disassembly at the prote asome.
Journal ArticleDOI
Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction
Patrick Schreiner,Xiang Chen,Koraljka Husnjak,Leah Randles,Naixia Zhang,Suzanne Elsasser,Daniel Finley,Ivan Dikic,Ivan Dikic,Kylie J. Walters,Michael Groll,Michael Groll +11 more
TL;DR: It is reported that Rpn13, a component of the nine-subunit proteasome base, functions as a ubiquitin receptor, complementing its known role in docking de-ubiquitinating enzyme Uch37/UCHL5 to the proteasomes, and a novel ubiquitIn-binding mode in which loops rather than secondary structural elements are used to capture ubiqu itin.
Journal ArticleDOI
Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome
Yuan Shi,Xiang Chen,Suzanne Elsasser,Bradley B. Stocks,Geng Tian,Byung-Hoon Lee,Yanhong Shi,Naixia Zhang,Stefanie A. H. de Poot,Fabian Tuebing,Shuangwu Sun,Jacob Vannoy,Sergey G. Tarasov,John R. Engen,Daniel Finley,Kylie J. Walters +15 more
TL;DR: The results indicate that proteasome subunit Rpn1 can recognize both ubiquitin and UBL domains of substrate shuttling factors that themselves bind ubiquit in and function as reversibly associated proteasomal Ubiquitin receptors.
Journal ArticleDOI
Gates, Channels, and Switches: Elements of the Proteasome Machine
TL;DR: Cryoelectron microscopy studies are brought together with molecular analyses to describe the principles of proteasome activity and regulation.