Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
March 1, 1996Journal of Biological ChemistryOpen Access

Mycobacterium tuberculosis 16-kDa Antigen (Hsp16.3) Functions as an Oligomeric Structure in Vitro to Suppress Thermal Aggregation

View Full Paper
Ask AI
Bookmark
Share

Authors

ZCZengyi ChangPeking UniversityTPTodd P. PrimmSam Houston State UniversityJJJoanita JakanaBaylor College of Medicine

Discussion

Loading...

Member takes

Overview

Key Points

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

Cite This Study

Chang et al. (1996) studied this question.

synapsesocial.com/papers/6a6fefeea7fbea1e4407e51ehttps://doi.org/10.1074/jbc.271.12.7218
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Alpha-crystallin can function as a molecular chaperone.1992 · 1,847 citations
  2. 2Supramolecular structure of the recombinant murine small heat shock protein hsp251991 · 73 citations
  3. 3Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp271994 · 247 citations
  4. 4Structure and in Vitro Molecular Chaperone Activity of Cytosolic Small Heat Shock Proteins from Pea1995 · 320 citations