Results 11 to 20 of about 9,646 (179)

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

open access: yesBiomedicines, 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   +3 more
doaj   +1 more source

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

open access: yesPathogens, 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   +4 more
doaj   +1 more source

The Role of Hsp27 in Chemotherapy Resistance

open access: yesBiomedicines, 2022
Heat shock protein (Hsp)-27 is a small-sized, ATP-independent, chaperone molecule that is overexpressed under conditions of cellular stress such as oxidative stress and heat shock, and protects proteins from unfolding, thus facilitating proteostasis and ...
Marios Lampros   +3 more
doaj   +1 more source

p53-dependent induction of heat shock protein 27 (HSP27) expression [PDF]

open access: yesInternational Journal of Cancer, 2000
Transcriptional activation of the p53 target genes plays a critical role in the cellular response to DNA damage, hypoxia, cellular stress and other signals regulating the cell cycle and apoptosis. The discovery of new p53 target genes continues to reveal novel mechanisms of action of this multifaceted protein.
C, Gao   +5 more
openaire   +2 more sources

Mechanistic insights into heat shock protein 27, a potential therapeutic target for cardiovascular diseases

open access: yesFrontiers in Cardiovascular Medicine, 2023
Heat shock protein 27 (HSP27) is a small chaperone protein that is overexpressed in a variety of cellular stress states. It is involved in regulating proteostasis and protecting cells from multiple sources of stress injury by stabilizing protein ...
Yifei Zou   +5 more
doaj   +1 more source

Heat shock proteins HSP27, HSP60, HSP70, and HSP90 [PDF]

open access: yesCancer, 2003
AbstractBACKGROUNDHeat shock proteins (HSPs) are synthesized by cells in response to various stress conditions, including carcinogenesis. The expression of HSPs in neoplasia has been implicated in the regulation of apoptosis, and HSPs also can act by increasing immunity. In the current study, the authors attempted to clarify the significance of HSPs in
Thierry, Lebret   +6 more
openaire   +2 more sources

Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target [PDF]

open access: yesFibrogenesis & Tissue Repair, 2012
Abstract Heat shock protein 27 (HSP27) is a multidimensional protein which acts as a protein chaperone and an antioxidant and plays a role in the inhibition of apoptosis and actin cytoskeletal remodeling. In each of these capacities, HSP27 has been implicated in different disease states playing both protective and counter-protective roles ...
Vidyasagar, Aparna   +2 more
openaire   +2 more sources

Knock down of heat shock protein 27 (HspB1) induces degradation of several putative client proteins. [PDF]

open access: yesPLoS ONE, 2012
Hsp27 belongs to the heat shock protein family and displays chaperone properties in stress conditions by holding unfolded polypeptides, hence avoiding their inclination to aggregate.
Benjamin Gibert   +10 more
doaj   +1 more source

Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular Inflammation

open access: yesFrontiers in Immunology, 2016
Heat shock protein 27 (HSP27) is traditionally viewed as an intra-cellular chaperone protein with anti-apoptotic properties. However, recent data indicate that a number of heat shock proteins, including HSP27, are also found in the extra-cellular space ...
Zarah Batulan   +7 more
doaj   +1 more source

Localization and expression of Hsp27 and αB-crystallin in rat primary myocardial cells during heat stress in vitro. [PDF]

open access: yesPLoS ONE, 2013
Neonatal rat primary myocardial cells were subjected to heat stress in vitro, as a model for investigating the distribution and expression of Hsp27 and αB-crystallin.
Shu Tang   +7 more
doaj   +1 more source

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