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Hsp70 transiently interacts with mutant SOD1 aggregates (in differentiated PC12 cells). Matsumoto G,/ et. al/._ J Cell Biol._ 2005 Oct 10;171(1):75-85.


Poly Q size-dependent aggregation in/ C. elegans/ primary neurons: Q19, Q40, Q82 (Heather Brignull)


Chaperone networks: Regulation of protein conformation


Genetic screen for genes that regulate protein misfolding


PolyQ length and age-dependent aggregation and toxicity in C. elegans


PolyQ-GFP proteins: Probes of the folding environment in C. elegans



Molecular chaperone Hsp70 interacts transiently with the surface of polyQ aggregates

Transcriptional regulation of heat shock response
Roles of Molecular Chaperones in Protein Folding, Trafficking, and Stress Sensors in Cell Growth and Death
All Chaperome Project
Misfolded and aggregation prone proteins in neu
C elegans as a model system for analysis of stress response and diseases of protein misfolding
Small molecule screen for the stress response
Systems Approach to Stress Biology