Results 81 to 90 of about 6,022 (190)
Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90
The molecular chaperones Hsc70 and Hsp90 are required for proteostasis control and specific folding of client proteins in eukaryotic and prokaryotic organisms.
Lukas Schmauder +5 more
doaj +1 more source
Bioengineered Extracellular Vesicles in Emerging Cancer Vaccine Platforms
This review highlights recent advances in engineering extracellular vesicles (EVs) as next‐generation cancer vaccines. It outlines their biological roles and antigen‐presenting capacity, explores key strategies for antigen loading and delivery optimization, and summarizes preclinical and clinical applications using EVs from diverse immune and tumor ...
Wonkyung Ahn +4 more
wiley +1 more source
A Novel Therapeutic Strategy for the Treatment of Glioma, Combining Chemical and Molecular Targeting of Hsp90a [PDF]
Hsp90α's vital role in tumour survival and progression, together with its highly inducible expression profile in gliomas and its absence in normal tissue and cell lines validates it as a therapeutic target for glioma.
Adi Mehta +55 more
core +2 more sources
Gasdermins: multifunctional effectors of membrane permeabilization across cellular compartments
Gasdermins (GSDMs) are pore‐forming proteins best known for driving pyroptosis through plasma membrane (PM) permeabilization. Beyond triggering inflammatory cell death, GSDMs can also associate with organelle membranes, including mitochondria, lysosomes, ER, and nucleus, where they modulate membrane integrity and cellular signaling.
Eleonora Margheritis +2 more
wiley +1 more source
Receptor-interacting serine/threonine-protein kinase 3 (RIPK3) normally signals to necroptosis by phosphorylating MLKL. We report here that when the cellular RIPK3 chaperone Hsp90/CDC37 level is low, RIPK3 also signals to apoptosis.
Dianrong Li +10 more
doaj +1 more source
The Human Cdc37·Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy [PDF]
The cell division cycle protein 37 (Cdc37) and the 90-kDa heat shock protein (Hsp90) are molecular chaperones, which are crucial elements in the protein signaling pathway. The largest class of client proteins for Cdc37 and Hsp90 are protein kinases. The catalytic domains of these kinases are stabilized by Cdc37, and their proper folding and functioning
Sreeramulu, Sridhar +5 more
openaire +4 more sources
The Hsp90β Isoform: An Attractive Target for Drug Development
ABSTRACT The beta isoform of 90 kDa heat shock protein (Hsp90β) plays a critical role in maintaining cellular proteostasis by assisting in the folding and refolding of proteins, which is essential for both normal cellular function and stress response.
Subhabrata Chaudhury +2 more
wiley +1 more source
Background Multiple myeloma (MM) is a B-cell malignancy that is largely incurable and is characterized by the accumulation of malignant plasma cells in the bone marrow.
Xu Yuan-Ji +6 more
doaj +1 more source
Using celastrol as a case study, this review summarizes various target discovery strategies for natural products, including chemical proteomics, protein microarray, degradation‐based protein profiling, proteome‐wide label‐free approaches, network pharmacology, target‐based drug screening, and indirect strategies.
Yanbei Tu +5 more
wiley +1 more source
Exploring Long Noncoding RNAs as Regulators of Tumor Ferroptosis: Advances and Challenges
Long noncoding RNAs (lncRNAs) play pivotal roles in regulating gene expression and are closely associated with cancer progression, prognosis, and therapeutic resistance. This review highlights recent advancements in understanding how lncRNAs modulate ferroptosis, a regulated form of cell death characterized by iron‐dependent lipid peroxidation ...
Gang Li +3 more
wiley +1 more source

