Results 51 to 60 of about 59,353 (250)
Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90)
Chromatin immunoprecipitation followed by sequencing (ChIP-seq) is a widely used technique for genome-wide mapping of protein-DNA interactions and epigenetic marks in vivo. Recent studies have suggested an important role of heat shock protein 90 (Hsp90) in chromatin. This molecular chaperone assists other proteins to acquire their mature and functional
openaire +2 more sources
This study delineates a novel HSP90AB1‐ITGBL1 signaling axis governing osteosarcoma. HSP90AB1 promotes K63‐linked ubiquitination and proteasomal degradation of ITGBL1. Restoring ITGBL1 induces reactive oxygen species‐dependent endoplasmic reticulum stress and pro‐death autophagy, suppressing tumor growth and metastasis.
Zhen Wang +17 more
wiley +1 more source
HSP90α is significantly upregulated in platelets from sepsis patients, with its origin from megakaryocyte‐derived trafficking. Furthermore, activated platelets secrete HSP90α into the extracellular space in both free and exosome‐associated forms. Finally, extracellular HSP90α directly engages TLR4 on neutrophils to induce autophagy, leading to NET ...
Chengbo Wang +17 more
wiley +1 more source
Aging cellular networks: chaperones as major participants
We increasingly rely on the network approach to understand the complexity of cellular functions. Chaperones (heat shock proteins) are key "networkers", which have among their functions to sequester and repair damaged protein. In order to link the network
Agoston +56 more
core +1 more source
Heat shock induces rapid resorption of primary cilia [PDF]
Primary cilia are involved in important developmental and disease pathways, such as the regulation of neurogenesis and tumorigenesis. They function as sensory antennae and are essential in the regulation of key extracellular signalling systems.
Anckar +32 more
core +1 more source
Heat shock protein hsp90 regulates dioxin receptor function in vivo. [PDF]
The dioxin (aryl hydrocarbon) receptor is a ligand-dependent basic helix-loop-helix (bHLH) factor that binds to xenobiotic response elements of target promoters upon heterodimerization with the bHLH partner factor Arnt. Here we have replaced the bHLH motif of the dioxin receptor with a heterologous DNA-binding domain to create fusion proteins that ...
M L, Whitelaw +4 more
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This study reveals that abnormal mechanical stress downregulates the expression of HSP70 and impairs proteasome function in osteoarthritic bone cells, leading to misfolded collagen I accumulation and ER stress. When intracellular proteostasis capacity is exceeded, USP19 mediates the secretion of misfolded proteins into the extracellular space ...
Hailun Xu +20 more
wiley +1 more source
The combined effect of drought stress and heat shock on the induction of boiling stable proteins viz: WGA, SOD, HSP90,Aquaporin, CyPs, APase and LEA proteins was studied in 3-days old seedlings of drought tolerant and drought susceptible cultivars of ...
Gurmeen Rakhra, Arun Dev Sharma
doaj +1 more source
Functions of J-domain proteins in mitochondrial protein biogenesis. [PDF]
Abstract Mitochondrial biogenesis and functions depend on the import and assembly of more than 1000 proteins that are made as precursors on cytosolic ribosomes. The majority of these precursor proteins are transported from the ribosome to the translocase of the outer membrane (TOM complex), which constitutes the main entry site for mitochondrial ...
Tiku V, Bossenz G, Kirstein J, Becker T.
europepmc +2 more sources
RET Is a Heat Shock Protein 90 (HSP90) Client Protein and Is Knocked Down upon HSP90 Pharmacological Block [PDF]
Mutations of the RET receptor tyrosine kinase are associated to multiple endocrine neoplasia type 2 (MEN2) and sporadic medullary thyroid carcinoma (MTC). The heat shock protein (HSP) 90 chaperone is required for folding and stability of several kinases.
Alfano L. +6 more
openaire +5 more sources

