Role of HSP90 in Cancer
B Birbo, EE Madu, CO Madu, A Jain, Y Lu - International journal of …, 2021 - mdpi.com
HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein,
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …
it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits …
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …
[HTML][HTML] Tau interactome maps synaptic and mitochondrial processes associated with neurodegeneration
Tau (MAPT) drives neuronal dysfunction in Alzheimer disease (AD) and other tauopathies.
To dissect the underlying mechanisms, we combined an engineered ascorbic acid …
To dissect the underlying mechanisms, we combined an engineered ascorbic acid …
[HTML][HTML] The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones
Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of
numerous client proteins many of which are involved in essential cellular processes like …
numerous client proteins many of which are involved in essential cellular processes like …
Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
WB Pratt, DO Toft - Experimental biology and medicine, 2003 - journals.sagepub.com
Nearly 100 proteins are known to be regulated by hsp90. Most of these substrates or “client
proteins” are involved in signal transduction, and they are brought into complex with hsp90 …
proteins” are involved in signal transduction, and they are brought into complex with hsp90 …
The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review
P Csermely, T Schnaider, C So, Z Prohászka… - Pharmacology & …, 1998 - Elsevier
The 90-kDa molecular chaperone family (which comprises, among other proteins, the 90-
kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major …
kDa heat-shock protein, hsp90 and the 94-kDa glucose-regulated protein, grp94, major …
Structure and mechanism of the Hsp90 molecular chaperone machinery
LH Pearl, C Prodromou - Annu. Rev. Biochem., 2006 - annualreviews.org
Abstract Heat shock protein 90 (Hsp90) is a molecular chaperone essential for activating
many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 …
many signaling proteins in the eukaryotic cell. Biochemical and structural analysis of Hsp90 …
The interplay between the glucocorticoid receptor and nuclear factor-κB or activator protein-1: molecular mechanisms for gene repression
K De Bosscher, W Vanden Berghe… - Endocrine …, 2003 - academic.oup.com
The inflammatory response is a highly regulated physiological process that is critically
important for homeostasis. A precise physiological control of inflammation allows a timely …
important for homeostasis. A precise physiological control of inflammation allows a timely …
The structure and mechanism of protein phosphatases: insights into catalysis and regulation
▪ Abstract Eukaryotic protein phosphatases are structurally and functionally diverse enzymes
that are represented by three distinct gene families. Two of these, the PPP and PPM families …
that are represented by three distinct gene families. Two of these, the PPP and PPM families …
[HTML][HTML] The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR‐mediated protein–protein interactions
The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence identified in a
wide variety of proteins, present in tandem arrays of 3–16 motifs, which form scaffolds to …
wide variety of proteins, present in tandem arrays of 3–16 motifs, which form scaffolds to …