Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
January 23, 1996Proceedings of the National Academy of SciencesOpen Access

Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting.

View Full Paper
Ask AI
Bookmark
Share

Authors

RBR. W. BealManchester Metropolitan UniversityQDQuinn L. DeverauxInhibrx (United States)GXGui‐Yang XiaBeijing University of Chinese Medicine

Discussion

Loading...

Member takes

Overview

Key Points

Key points are not available for this paper at this time.

Cite This Study

Beal et al. (1996) studied this question.

synapsesocial.com/papers/6a0ba0efe08198424b95d2b2https://doi.org/10.1073/pnas.93.2.861
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains. Role in protein degradation.1992 · 167 citations
  2. 2Synthesis and characterization of ubiquitin ethyl ester, a new substrate for ubiquitin carboxyl-terminal hydrolase1986 · 60 citations
  3. 3A Hot Spot of Binding Energy in a Hormone-Receptor Interface1995 · 2,022 citations
  4. 4Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain.1994 · 235 citations
  5. 5A multicomponent system that degrades proteins conjugated to ubiquitin. Resolution of factors and evidence for ATP-dependent complex formation.1988 · 161 citations