Structure, function, and regulation of the Hsp90 machinery
MM Biebl, J Buchner - Cold Spring Harbor perspectives …, 2019 - cshperspectives.cshlp.org
Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …
HSP90AB1: Hel** the good and the bad
M Haase, G Fitze - Gene, 2016 - Elsevier
HSP90AB1 (heat shock protein 90 kDA alpha, class B, member 1), also known as
HSP90beta, is a member of the large family of HSPs which function as molecular …
HSP90beta, is a member of the large family of HSPs which function as molecular …
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 …
Hsp90 Co-chaperones form plastic genetic networks adapted to client maturation
MM Biebl, M Riedl, J Buchner - Cell reports, 2020 - cell.com
Summary Heat shock protein 90 (Hsp90) is a molecular chaperone regulating the activity of
diverse client proteins together with a plethora of different co-chaperones. Whether these …
diverse client proteins together with a plethora of different co-chaperones. Whether these …
Hsp90 and cochaperones have two genetically distinct roles in regulating eEF2 function
MD Fulton, DJ Yama, E Dahl, JL Johnson - PLoS genetics, 2024 - journals.plos.org
Protein homeostasis relies on the accurate translation and folding of newly synthesized
proteins. Eukaryotic elongation factor 2 (eEF2) promotes GTP-dependent translocation of …
proteins. Eukaryotic elongation factor 2 (eEF2) promotes GTP-dependent translocation of …
Hsp70-hsp90 chaperone networking in protein-misfolding disease
Molecular chaperones and their associated co-chaperones are essential in health and
disease as they are key facilitators of protein-folding, quality control and function. In …
disease as they are key facilitators of protein-folding, quality control and function. In …
The co-chaperone Cns1 and the recruiter protein Hgh1 link Hsp90 to translation elongation via chaperoning elongation factor 2
FH Schopf, EM Huber, C Dodt, A Lopez, MM Biebl… - Molecular cell, 2019 - cell.com
The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory
factors. Cns1 is one of the few essential co-chaperones in yeast, but its structure and …
factors. Cns1 is one of the few essential co-chaperones in yeast, but its structure and …
Hsp90-downregulation influences the heat-shock response, innate immune response and onset of oocyte development in nematodes
J Eckl, S Sima, K Marcus, C Lindemann, K Richter - PloS one, 2017 - journals.plos.org
Hsp90 is a molecular chaperone involved in the regulation and maturation of kinases and
transcription factors. In Caenorhabditis elegans, it contributes to the development of fertility …
transcription factors. In Caenorhabditis elegans, it contributes to the development of fertility …
Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects
The protein molecular chaperone Hsp90 (Heat shock protein, 90 kilodalton) plays multiple
roles in the biogenesis and regulation of client proteins impacting myriad aspects of cellular …
roles in the biogenesis and regulation of client proteins impacting myriad aspects of cellular …
Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation
Peptidyl prolyl isomerases (PPIases) accelerate the rate limiting step of protein folding by
catalyzing cis/trans isomerization of peptidyl prolyl bonds. The larger PPIases have been …
catalyzing cis/trans isomerization of peptidyl prolyl bonds. The larger PPIases have been …