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- Publications
- Influence
Mixed-linkage ubiquitin chains send mixed messages.
- Mark A. Nakasone, N. Livnat-Levanon, M. Glickman, R. Cohen, D. Fushman
- Chemistry, Medicine
- Structure
- 7 May 2013
Research on ubiquitin (Ub) signaling has focused primarily on homogeneously linked polyUb. Although polyUb containing different linkages within the same chain exist, their structures and signaling… Expand
Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains.
- C. Castañeda, T. Kashyap, Mark A. Nakasone, S. Krueger, D. Fushman
- Chemistry, Medicine
- Structure
- 2 July 2013
K11-linked polyubiquitin chains play important signaling and regulatory roles in both degradative and nonproteolytic pathways in eukaryotes. To understand the structural basis of how these chains are… Expand
Disassembly of Lys11 and Mixed Linkage Polyubiquitin Conjugates Provides Insights into Function of Proteasomal Deubiquitinases Rpn11 and Ubp6*
- W. Mansour, Mark A. Nakasone, +7 authors M. Glickman
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 11 November 2014
Background: Deconjugation of polyubiquitin is an essential step in preparing substrates for proteolysis by the 26S proteasome. Results: Proteasome-associated DUBs, Rpn11 and Ubp6, process long Lys11-… Expand
Extended ubiquitin species are protein-based DUB inhibitors
- Daria Krutauz, N. Reis, +7 authors M. Glickman
- Biology, Medicine
- Nature chemical biology
- 6 July 2014
A frame-shift mutation in the transcript of the ubiquitin-B gene leads to a C-terminally extended ubiquitin, UBB+1. UBB+1 has been considered to inhibit proteasomes, and as such to be the underlying… Expand
Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins.
- C. Castañeda, Emma K. Dixon, +7 authors D. Fushman
- Chemistry, Medicine
- Structure
- 1 March 2016
Polyubiquitination, a critical protein post-translational modification, signals for a diverse set of cellular events via the different isopeptide linkages formed between the C terminus of one… Expand
Chemical synthesis of phosphorylated ubiquitin and diubiquitin exposes positional sensitivities of e1-e2 enzymes and deubiquitinases.
- S. Bondalapati, Wissam Mansour, Mark A. Nakasone, S. Maity, M. Glickman, A. Brik
- Chemistry, Medicine
- Chemistry
- 11 May 2015
Modification of ubiquitin by phosphorylation extends the signaling possibilities of this dynamic signal, as it could affect the activity of ligases and the processing of ubiquitin chains by… Expand
Base-CP proteasome can serve as a platform for stepwise lid formation
- Z. Yu, N. Livnat-Levanon, +8 authors M. Glickman
- Chemistry, Medicine
- Bioscience reports
- 27 January 2015
26S proteasome, a major regulatory protease in eukaryotes, consists of a 20S proteolytic core particle (CP) capped by a 19S regulatory particle (RP). The 19S RP is divisible into base and lid… Expand
Proteomic identification and analysis of K63-linked ubiquitin conjugates.
- Joe R. Cannon, Mark A. Nakasone, D. Fushman, C. Fenselau
- Chemistry, Medicine
- Analytical chemistry
- 20 November 2012
Post-translational modification of proteins by covalent attachment of ubiquitin or a polyubiquitin chain is involved in myriad of processes in eukaryotic cells. The particular outcome of… Expand
Characterizing polyubiquitinated forms of the neurodegenerative ubiquitin mutant UBB+1
- M. Chojnacki, D. Zhang, +4 authors Mark A. Nakasone
- Chemistry, Medicine
- FEBS letters
- 1 December 2016
The ubiquitin mutant UBB+1 has been identified as a hallmark of neurodegenerative diseases. In this study, we characterize polyubiquitinated forms of UBB+1 in vitro and from patient samples. The… Expand
Structural Basis for the Inhibitory Effects of Ubistatins in the Ubiquitin-Proteasome Pathway.
- Mark A. Nakasone, T. A. Lewis, +16 authors D. Fushman
- Biology, Medicine
- Structure
- 5 December 2017
The discovery of ubistatins, small molecules that impair proteasomal degradation of proteins by directly binding to polyubiquitin, makes ubiquitin itself a potential therapeutic target. Although… Expand