The plasticity of the Hsp90 co-chaperone system
P Sahasrabudhe, J Rohrberg, MM Biebl, DA Rutz… - Molecular cell, 2017 - cell.com
The Hsp90 system in the eukaryotic cytosol is characterized by a cohort of co-chaperones
that bind to Hsp90 and affect its function. Although progress has been made regarding the …
that bind to Hsp90 and affect its function. Although progress has been made regarding the …
Contributions of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity
A Walton-Diaz, S Khan, D Bourboulia… - Future medicinal …, 2013 - Taylor & Francis
Hsp90 is a molecular chaperone and important driver of stabilization and activation of
several oncogenic proteins that are involved in the malignant transformation of tumor cells …
several oncogenic proteins that are involved in the malignant transformation of tumor cells …
p23 and Aha1
AB Rehn, J Buchner - The Networking of Chaperones by Co-chaperones …, 2015 - Springer
Hsp90 is a conserved molecular chaperone and is responsible for the folding and activation
of several hundred client proteins, involved in various cellular processes. The large number …
of several hundred client proteins, involved in various cellular processes. The large number …
The mechanism of Hsp90 ATPase stimulation by Aha1
Hsp90 is a dimeric molecular chaperone responsible for the folding, maturation, and
activation of hundreds of substrate proteins called 'clients'. Numerous co-chaperone proteins …
activation of hundreds of substrate proteins called 'clients'. Numerous co-chaperone proteins …
Hsp90 mutants with distinct defects provide novel insights into cochaperone regulation of the folding cycle
R Mercier, D Yama, P LaPointe, JL Johnson - PLoS Genetics, 2023 - journals.plos.org
Molecular chaperones play a key role in maintaining proteostasis and cellular health. The
abundant, essential, cytosolic Hsp90 (Heat shock protein, 90 kDa) facilitates the folding and …
abundant, essential, cytosolic Hsp90 (Heat shock protein, 90 kDa) facilitates the folding and …
Exploring the Trypanosoma brucei Hsp83 Potential as a Target for Structure Guided Drug Design
JC Pizarro, T Hills, G Senisterra… - PLoS neglected …, 2013 - journals.plos.org
Human African trypanosomiasis is a neglected parasitic disease that is fatal if untreated. The
current drugs available to eliminate the causative agent Trypanosoma brucei have multiple …
current drugs available to eliminate the causative agent Trypanosoma brucei have multiple …
Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation
Hsp90 is a molecular chaperone that acts on its clients through an ATP-dependent and
conformationally dynamic functional cycle. The cochaperone Accelerator of Hsp90 ATPase …
conformationally dynamic functional cycle. The cochaperone Accelerator of Hsp90 ATPase …
An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
AD Zuehlke, M Reidy, C Lin, P LaPointe… - Nature …, 2017 - nature.com
Abstract Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone. To
properly chaperone its clientele, Hsp90 proceeds through an ATP-dependent …
properly chaperone its clientele, Hsp90 proceeds through an ATP-dependent …
p53 protein regulates Hsp90 ATPase activity and thereby Wnt signaling by modulating Aha1 expression
The p53 tumor suppressor gene encodes a homotetrameric transcription factor which is
activated in response to a variety of cellular stressors, including DNA damage and …
activated in response to a variety of cellular stressors, including DNA damage and …
AHSA1 regulates proliferation, apoptosis, migration, and invasion of osteosarcoma
J Shao, L Wang, C Zhong, R Qi, Y Li - Biomedicine & Pharmacotherapy, 2016 - Elsevier
Activator of 90 kDa heat shock protein ATPase homolog 1 (AHSA1) is a chaperone of heat
shock 90 kDa (HSP90) and stimulates ATPase activity of HSP90. The function of AHSA1 in …
shock 90 kDa (HSP90) and stimulates ATPase activity of HSP90. The function of AHSA1 in …