Results 1 to 10 of about 3,351,166 (211)

Ac-SDKP modulates apoptosis via HSP27 and the FAS/FASL and mitochondrial axes. [PDF]

Animal Model Exp Med
Schematic diagram of Ac‐SDKP regulating the FAS/FASL and mitochondrial apoptosis pathways via HSP27. Ac‐SDKP inhibits HSP27 expression, activates the FAS/FASL pathway and Caspase‐3 signaling, increases Caspase‐8 and Caspase‐3 expression, and induces cell apoptosis.
Guo W, Yan J, Li W, Wang J, Liu L, Zhang C, Cao W, Yao S, Gong H, He Y, Zhou Z, Chen S, Feng L, Deng H.   +13 more
europepmc   +2 more sources

Heat Shock Proteins in Cancer: Mechanisms and Therapeutic Targeting. [PDF]

MedComm (2020)
This review illustrates heat shock proteins (HSPs) as central regulators of cancer metabolic reprogramming. By stabilizing key metabolic enzymes and coordinating glycolysis, oxidative phosphorylation, redox homeostasis, and stress adaptation, HSPs support tumor growth, metastasis, and therapeutic resistance. Targeting HSP networks may therefore provide
Ma S, Liu CQ, Ma SY, Wang SG, Xia QD, Xu MY.   +5 more
europepmc   +2 more sources

Function within disorder: Small heat shock proteins use different functional regions to chaperone tau aggregation. [PDF]

Protein Sci
Abstract In numerous neurodegenerative diseases known collectively as tauopathies, the microtubule‐associated protein tau forms fibrillar aggregates that are hallmarks of disease pathology. Tauopathies represent a substantial fraction of diseases associated with protein misfolding.
Cervantes M, Janowska MK, Tuttle LM, Guttman M, Nath A, Klevit RE.   +5 more
europepmc   +2 more sources

Therapeutic targets in diabetic peripheral neuropathy: heat shock proteins [PDF]

Frontiers in Endocrinology
Diabetic peripheral neuropathy (DPN), a debilitating diabetic complication, has a complex pathological mechanism involving oxidative stress, mitochondrial dysfunction, and endoplasmic reticulum stress, and there are no effective disease-mitigating ...
Chengzhi Yin, Jiao Lv, Shujia Huang, Chenyu Lang, Yunyun Zhao, Guoqiang Wang, Junming Kan, Xiuge Wang   +7 more
doaj   +2 more sources

Monitoring the Effect of Tributyltin Salicylate and Propionate, Retinoid X Receptor Ligands, on Heat Shock Protein Expression in MDA-MB-231 Cells by MALDI MS/MS. [PDF]

J Mass Spectrom
ABSTRACT Organotin (IV) compounds are known to induce apoptosis via the intrinsic mitochondrial pathway, which is a key mechanism of effective anticancer therapy. Their ability to selectively promote apoptotic cell death highlights their potential as chemotherapeutic agents. In this study, the in vitro effects of two triorganotin compounds, tributyltin
Strouhalova D, Macejova D, Brtko J, Bobalova J.   +3 more
europepmc   +2 more sources

Comment on: Low expression of HSP27 and HSP70 predicts poor prognosis in laryngeal squamous cell carcinoma [PDF]

Journal of Cancer Research and Clinical Oncology
Borowczak et al. recently explored the prognostic role of heat shock proteins HSP27 and HSP70 in laryngeal squamous cell carcinoma (LSCC). Their study demonstrated that lower expression levels of these proteins were linked to significantly reduced ...
Doga Topkan, Efsun Somay, Erkan Topkan, Ugur Selek   +3 more
doaj   +2 more sources

HSP27 Protein Dampens Encephalomyocarditis Virus Replication by Stabilizing Melanoma Differentiation-Associated Gene 5

Frontiers in Microbiology, 2021
Heat shock proteins (HSPs) are a protein family that respond to physiological stress, such as heat, starvation, and infection. As cellular protein chaperones, they play an important role in protein folding, assembly, and degradation.
Xiangrong Li, Ruixian Ma, Bei Wu, Yuhui Niu, Hongshan Li, Dianyu Li, Jingying Xie, Adi Idris, Ruofei Feng   +8 more
doaj   +1 more source

The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells. [PDF]

PLoS ONE, 2013
The heat shock response (HSR) is a highly conserved molecular response to various types of stresses, including heat shock, during which heat-shock proteins (Hsps) are produced to prevent and repair damages in labile proteins and membranes.
Zohar Bromberg, Pierre Goloubinoff, Younousse Saidi, Yoram George Weiss   +3 more
doaj   +1 more source

HSP27 Interacts with Nonstructural Proteins of Porcine Reproductive and Respiratory Syndrome Virus and Promotes Viral Replication

Pathogens, 2023
Heat shock protein 27 (HSP27) is a multifunctional protein and belongs to the small HSP family. It has been shown that HSP27 is involved in viral replication as a cellular chaperone, but the function of HSP27 during porcine reproductive and respiratory ...
Chunhui Song, Hanze Liu, Zhi Cao, Hu Shan, Qiaoya Zhang   +4 more
doaj   +1 more source

Heat Shock Protein 27 Affects Myeloid Cell Activation and Interaction with Prostate Cancer Cells

Biomedicines, 2022
Heat shock proteins are cytoprotective molecules induced by environmental stresses. The small heat shock protein 27 (Hsp27) is highly expressed under oxidative stress conditions, mediating anti-oxidative effects and blocking apoptosis.
Debora Singer, Verena Ressel, Matthias B. Stope, Sander Bekeschus   +3 more
doaj   +1 more source