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The product of HSF1 is a heat-shock transcription factor. Additionally we are shipping HSF1 Antibodies (494) and HSF1 Kits (56) and many more products for this protein.
Showing 10 out of 14 products:
These functions of HPK-1 (show MAP4K1 Proteins)/HSF-1 undergo rapid down-regulation once animals reach reproductive maturity. We show that HPK-1 (show MAP4K1 Proteins) fortifies proteostasis and extends longevity by an additional independent mechanism: induction of autophagy.
Diminution in phenotypic variation for both gene expression and life span at 25 degrees C may be a consequence of low level hsf-1-dependent expression of HSP-16.2 and other chaperones at the higher temperature.
We demonstrate that while DAF-16/FOXO is dispensable, the age-dependent suppression of cilia phenotypes in IFT mutants requires cell-autonomous functions of the HSF1 heat shock factor and the Hsp90 chaperone
HSF-1 is a codeterminant of both alcohol and nicotine sensitivity in C. elegans and that this phenotype requires the small HSP, HSP-16.48. HSP-16.48 function in drug sensitivity is unrelated to a chaperone action during the heat shock stress response.
Heat-stress-enhanced ascaroside production appears to be mediated at least in part by HSF-1, which seems to be important in adaptation strategies for coping with heat stress in this nematode.
FUdR treatment can modulate the HSR and proteostasis, and should be used with caution when used to inhibit reproduction.
Excitation of the AFD thermosensory neurons is sufficient to activate HSF1 in another cell, even in the absence of temperature increase. Excitation of the AFD thermosensory neurons enhances serotonin release.
hsf-1 RNAi suppressed the restoration of thrashing reduced by heat stress. In contrast, hsf-1 knockdown cancelled prevention of movement reduction in a daf-2 mutant, but didn't suppress thrashing restoration in daf-2 mutant.
we engaged C. elegans mutants and identified that the p38 MAPK (show MAPK14 Proteins) signaling, insulin (show INS Proteins)/IGF-1 (show IGF1 Proteins) signaling (IIS), and HSF-1 play pivotal roles in the WCESP-mediated host immune response
HSF-1 has a prominent role in cytoskeletal integrity, ensuring cellular function during stress and aging. Overexpression of pat-10 increased actin filament stability, thermotolerance, and longevity, indicating that in addition to chaperone regulation, HSF-1 has a prominent role in cytoskeletal integrity, ensuring cellular function during stress and aging.
the expression level of NFATc2 (show NFAT1 Proteins), miR (show MLXIP Proteins)-208b and miR (show MLXIP Proteins)-499 suggested that these responses were suppressed in HSF1-null mice
identify 4 huntingtin (show HTT Proteins)-targeting miRNAs viz. miR (show MLXIP Proteins)-125b, miR (show MLXIP Proteins)-146a, miR (show MLXIP Proteins)-150 and miR (show MLXIP Proteins)-214 as candidate miRNAs responsible for observed inhibitory effect of HSF1 on huntingtin (show HTT Proteins) expression.
HSF1 plays an important role in the occurrence of UVR-B-induced cataracts, possibly via regulation of HSPs such as HSP25 (show HSPB1 Proteins).
Targeted deletion of HSF1 results in changes of locomotor function associated with changes in cerebellar calbindin (show CALB1 Proteins) protein levels. These findings suggest a role of HSF1 in regular Purkinje cell calcium homeostasis.
this study shows that HSF1 overexpression protects against TDP-43 (show TARDBP Proteins) pathology by upregulation of chaperones, especially HSP70 (show HSP70 Proteins), rather than enhancing autophagy
Acetylation of the protein triggers TDP-43 (show TARDBP Proteins) pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein.
These findings provide insight into the role of HSF1 in Leydig cell steroidogenesis, suggesting that it maintains cholesterol transport by recovering StAR under chronic heat stress.
In mammalian cell lines, only heat shock-induced but not basal expression of chaperones is dependent on the mammalian Hsf1 homolog.
Upregulating HSF1 relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (show DDIT3 Proteins) and increasing HSP70 (show HSP70 Proteins) a5 (BiP/GRP78 (show HSPA5 Proteins)). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 being one likely key player in both systems.
HSF1 translationally augments the proteotoxic stress response.
MD simulation of high-resolution X-ray structures reveals post-translational modification dependent conformational changes in HSF-DNA interaction.
We found that HSF1 activation mediated by 1,4-NQ upregulated downstream genes, such as HSPA6 (show HSPA6 Proteins). The results suggest that activation of the HSP90 (show HSP90 Proteins)-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.
casein kinase 1 (show CSNK1A1 Proteins) phosphorylates the SQSTM1 (show SQSTM1 Proteins) S349 residue when harmful proteins accumulate under HSF1 stress
Evidence for the essential function of HSF1 in the transcriptional activation of TERRA (show DMRT2 Proteins) and in telomere protection upon stress.
Low glucose culture hampered typical epithelial-mesenchymal transition-like morphological change, "cadherin switching," and cell migration of hepatocellular carcinoma cells through inducing persistent down-regulation of HSF1, resulting in direct inhibition of snail1 (show SNAI1 Proteins) expression.
piR (show PIR Proteins)-823 increased the transcriptional activity of HSF1, the common transcription factor of HSPs, by binding to HSF1 and promoting its phosphorylation at Ser326.
Reporter assay showed that HSF1 increased the transcriptional activity of ATG4B (show ATG4B Proteins) gene promoter, and chromatin immunoprecipitation assay verified that HSF1 bound to the site (-1429 to -1417) in ATG4B (show ATG4B Proteins) gene promoter region.
Knockdown of HSF1 reduced the proliferation, migration and invasion of osteosarcoma cells, while overexpression of HSF1 promoted the proliferation, migration and invasion of osteosarcoma cells.
Data suggest that hnRNPK plays role in heat shock response of cells by regulating HSF1; hnRNPK inhibits HSF1 activity, resulting in reduced expression of HSP27 and HSP70 mRNAs; hnRNPK also down-regulates binding of HSF1 to heat shock response element. (hnRNPK = heterogeneous-nuclear ribonucleoprotein K; HSF1 = heat shock transcription factor 1; HSP = heat-shock protein)
As the 4693-T mutation caused the disruption of microRNA target binding (resulting in the relief of the transcriptional repression), the HSF1 gene is useful in dairy cattle thermal tolerant breeding.
HSF1 is a key trans-acting factor for counteracting transgene promoter silencing in Chlamydomonas.
Data show that activated HSF1 and CRR1 transcription factors mediate the acetylation of histones H3/4, nucleosome eviction, remodeling of the H3K4 mono- and dimethylation marks, and transcription initiation/elongation.
data suggest that HSF1 is a key regulator of the stress response in Chlamydomonas
Data suggest that myocardial HSF1 and HSP70 (show HSP70 Proteins) (70 kDa heat-shock protein (show HSPA9 Proteins)) can be up-regulated by dietary factors (here, antioxidant taurine as a dietary supplement administered to counteract effects of atherogenic diet).
The results indicate that Heat shock protein 70 (Hsp70) mediates distinct stress-related functions in different tissues during transportation. Heat shock factor-1 (HSF-1) levels were reduced at 1 and 4 h only in the hearts of transported pigs.
The transcriptional up-regulation of unc45b, hsp90aa1.1 and smyd1b is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models
data suggest that HSF1 is involved in regulating constitutive lens specific expression of hsp70 (show HSPA1A Proteins) in the embryonic zebrafish
The product of this gene is a heat-shock transcription factor. Transcription of heat-shock genes is rapidly induced after temperature stress. Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of this gene.
heat shock factor protein
, heat shock transcription factor
, Heat Shock Factor family member (hsf-1)
, HSF 1
, HSTF 1
, heat shock factor protein 1
, heat shock transcription factor 1