Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemia cells.
about
Inhalation exposure to carbon nanotubes (CNT) and carbon nanofibers (CNF): methodology and dosimetryHSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activatorInhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70Genomic organization and promoter analysis of the human heat shock factor 2 geneA heat shock-responsive domain of human HSF1 that regulates transcription activation domain functionActivation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1Regulation of protein phosphatase 2A activity by heat shock transcription factor 2Structural organization of the gene encoding the neuroendocrine chaperone 7B2The loop domain of heat shock transcription factor 1 dictates DNA-binding specificity and responses to heat stressFunction and regulation of heat shock factor 2 during mouse embryogenesisAnalysis of HSF4 binding regions reveals its necessity for gene regulation during development and heat shock response in mouse lensesEssential requirement for both hsf1 and hsf2 transcriptional activity in spermatogenesis and male fertilityActivation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stressTranscriptional regulation and binding of heat shock factor 1 and heat shock factor 2 to 32 human heat shock genes during thermal stress and differentiation.Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcriptionProteotoxic stress and inducible chaperone networks in neurodegenerative disease and agingDetermination of the consensus binding sequence for the purified embryonic heat shock factor 2.Structural organization and promoter analysis of murine heat shock transcription factor-1 gene.In silico analyses of proteomic data suggest a role for heat shock proteins in umbilical cord blood hematopoietic stem cells.On mechanisms that control heat shock transcription factor activity in metazoan cells.Heat shock element architecture is an important determinant in the temperature and transactivation domain requirements for heat shock transcription factor.Heat shock protein 70 is upregulated in the intestine of intrauterine growth retardation piglets.Multiple functions of Drosophila heat shock transcription factor in vivoConservation of a stress response: human heat shock transcription factors functionally substitute for yeast HSF.Novel isoforms of heat shock transcription factor 1, HSF1γα and HSF1γβ, regulate chaperone protein gene transcription.Disruption of heat shock factor 1 reveals an essential role in the ubiquitin proteolytic pathway.Pharmacological modulation of heat shock factor 1 by antiinflammatory drugs results in protection against stress-induced cellular damage.A murine world without HSFs: meeting reportClinical implications of the stress responseHeat shock transcription factor 2 is not essential for embryonic development, fertility, or adult cognitive and psychomotor function in mice.Unraveling complex interplay between heat shock factor 1 and 2 splicing isoforms.Role of heat-shock factor 2 in cerebral cortex formation and as a regulator of p35 expressionComplex expression of murine heat shock transcription factors.Molecular parameters of hyperthermia for radiosensitization.Dealing with misfolded proteins: examining the neuroprotective role of molecular chaperones in neurodegeneration.Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element.Promotion of heat shock factor Hsf1 degradation via adaptor protein filamin A-interacting protein 1-like (FILIP-1L).Deficient induction of human hsp70 heat shock gene transcription in Y79 retinoblastoma cells despite activation of heat shock factor 1.The outcome of poliovirus infections in K562 cells is cytolytic rather than persistent after hemin-induced differentiationHsp70 accumulation in chondrocytic cells exposed to high continuous hydrostatic pressure coincides with mRNA stabilization rather than transcriptional activation
P2860
Q23913295-35EF54CC-FC4B-4A94-980B-35BA1D57558BQ24308493-3D649396-FA7B-464A-9F4E-0D80141B4526Q24308507-DDDC44D2-66A8-4379-8D53-78E9531AD61CQ24563843-0E83981E-B20E-4054-8BAA-8D46A7AA62F1Q28116048-13ABAF12-C0B8-4511-B12F-A0EA4FE62F72Q28118171-CB4EED34-8DCB-4E81-A230-027B08396621Q28142799-4214767B-CE27-4ABE-8AE6-148AE7480D83Q28277075-7B16E0D0-6BE8-4E68-8458-81759A881EC7Q28346242-C77C81A8-3E5C-4618-84AE-CA53A1E405C8Q28506597-D0A2C50E-AA2B-46C8-ADFD-6BCE78822364Q28508550-33E2D807-4370-4C05-A9C0-00033B16FF0CQ28587569-24EE03C0-1A1B-48EA-B44D-0D7CAC10A5B3Q28609211-B42EB68E-2972-455A-AB66-3654C42B15C9Q28609627-389BBDB4-7ACA-449E-9947-8EB81ABF9B9DQ28609646-4E372583-7D38-4892-AF57-C9460B7501FDQ29614783-51391BDD-5180-4F5C-8532-920775628E3BQ31061523-88987FA2-762D-40B7-AB01-2BC5B9BF9CFEQ31965950-85AE1234-5076-437C-9615-66AC9BAB7F1EQ33653357-0155E14A-436F-41A2-99E0-869C7418363FQ33716872-1725E837-2ED8-4D3E-B9FB-B6D2DB4536D9Q33781387-08695CCA-B37A-4A07-9691-E31FA2A1D3F6Q33838953-89E17D8F-C63F-409C-A8D9-7D05A8625027Q33886554-160C5ABB-E090-4A8E-BBEE-EB0769A17C76Q33887676-A4F43EC1-C439-4890-AA9A-5FD0C031037FQ33931099-3279E642-4877-472A-8FB8-00BD7CBDF6DFQ33962741-B454C661-1094-42AF-813E-4617D6783455Q34036459-5E59A361-CE77-48F1-84C3-A0561638DF34Q34133502-EA6B787E-6978-474E-B8F9-916D6F64EB7EQ34192112-041B4278-FA1F-44BF-9166-EE1B6047BF79Q34303749-2712A799-833E-424D-B669-174218810D37Q34589825-8CCB1B13-3C9B-4800-9D3B-A4028CFF417DQ34649131-EB966631-0AA4-4711-99BB-BA86F8E5DF23Q34736948-649E80B2-9D5E-437B-A50E-B730BAB8F74DQ34990657-AF79C687-4C49-4A3A-A4E2-BA1DC238D2D8Q35096762-56A12D21-7F17-4D59-871F-1193ADA033EDQ35201814-6C17B5B0-E300-4910-BC96-5774FFED5205Q35213186-164C8CFC-EDEC-4F65-BCA9-6C883E786BCFQ35742134-9E5B7803-DAD3-4ED3-A0F1-854717C15CAAQ35866433-DCF10044-5832-4493-AB7B-625758D3A1B7Q35913988-8A07FAC4-56AF-4CC1-9D4D-1AF15A0073C2
P2860
Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemia cells.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
Activation of heat shock facto ...... f human erythroleukemia cells.
@ast
Activation of heat shock facto ...... f human erythroleukemia cells.
@en
type
label
Activation of heat shock facto ...... f human erythroleukemia cells.
@ast
Activation of heat shock facto ...... f human erythroleukemia cells.
@en
prefLabel
Activation of heat shock facto ...... f human erythroleukemia cells.
@ast
Activation of heat shock facto ...... f human erythroleukemia cells.
@en
P2093
P2860
P356
P1476
Activation of heat shock facto ...... f human erythroleukemia cells.
@en
P2093
Abravaya K
Morimoto RI
Phillips B
Sistonen L
P2860
P304
P356
10.1128/MCB.12.9.4104
P407
P577
1992-09-01T00:00:00Z