Induced protein degradation: an emerging drug discovery paradigm
Small-molecule drug discovery has traditionally focused on occupancy of a binding site that
directly affects protein function, and this approach typically precludes targeting proteins that …
directly affects protein function, and this approach typically precludes targeting proteins that …
[HTML][HTML] The Hsp70/Hsp90 chaperone machinery in neurodegenerative diseases
RE Lackie, A Maciejewski, VG Ostapchenko… - Frontiers in …, 2017 - frontiersin.org
The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …
The impact of transposable elements in adaptive evolution
L Schrader, J Schmitz - Molecular Ecology, 2019 - Wiley Online Library
The growing knowledge about the influence of transposable elements (TE s) on (a) long‐
term genome and transcriptome evolution;(b) genomic, transcriptomic and epigenetic …
term genome and transcriptome evolution;(b) genomic, transcriptomic and epigenetic …
Molecular chaperones in protein folding and proteostasis
Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …
Molecular chaperone functions in protein folding and proteostasis
The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …
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 …
Targeting the dynamic HSP90 complex in cancer
J Trepel, M Mollapour, G Giaccone, L Neckers - Nature reviews cancer, 2010 - nature.com
The molecular chaperone heat shock protein 90 (HSP90) has been used by cancer cells to
facilitate the function of numerous oncoproteins, and it can be argued that cancer cells …
facilitate the function of numerous oncoproteins, and it can be argued that cancer cells …
[HTML][HTML] Roles of Hsp90 in Candida albicans morphogenesis and virulence
Highlights•Hsp90 is a molecular chaperone that modulates the function of many client
proteins.•Morphogenesis is an important Candida albicans virulence trait.•Hsp90 regulates …
proteins.•Morphogenesis is an important Candida albicans virulence trait.•Hsp90 regulates …
The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions
JA Kolhe, NL Babu, BC Freeman - Molecular cell, 2023 - cell.com
Molecular chaperones govern proteome health to support cell homeostasis. An essential
eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology …
eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology …
[PDF][PDF] Structure, function and regulation of the hsp90 machinery
Heat shock protein 90 (Hsp90), one of the most abundant and conserved molecular
chaperones, is essential in eukaryotic cells.[1, 2] Different from other well‑known mo‑lecular …
chaperones, is essential in eukaryotic cells.[1, 2] Different from other well‑known mo‑lecular …