HSPA4

From Wikipedia, the free encyclopedia

Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Heat shock 70 kDa protein 4 is a protein that in humans is encoded by the HSPA4 gene.[1][2]

The protein encoded by this gene was originally suggested to be a member of the heat shock protein 70 family.[1] However it is now known that human HSPA4 is an equivalent to mouse the Apg-2 protein and is a member of the Hsp110 family.[3]

Interactions

HSPA4 has been shown to interact with:

Page Template:Div col/styles.css has no content.

References

Page Template:Reflist/styles.css has no content.

  1. ^ a b Page Module:Citation/CS1/styles.css has no content.Fathallah DM, Cherif D, Dellagi K, Arnaout MA (Jul 1993). "Molecular cloning of a novel human hsp70 from a B cell line and its assignment to chromosome 5". Journal of Immunology. 151 (2): 810–3. doi:10.4049/jimmunol.151.2.810. PMID 8335910.
  2. ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: HSPA4 heat shock 70kDa protein 4".
  3. ^ Page Module:Citation/CS1/styles.css has no content.Kaneko Y, Kimura T, Kishishita M, Noda Y, Fujita J (Apr 1997). "Cloning of apg-2 encoding a novel member of heat shock protein 110 family". Gene. 189 (1): 19–24. doi:10.1016/S0378-1119(96)00807-4. PMID 9161406.
  4. ^ Page Module:Citation/CS1/styles.css has no content.Saleh A, Srinivasula SM, Balkir L, Robbins PD, Alnemri ES (Aug 2000). "Negative regulation of the Apaf-1 apoptosome by Hsp70". Nature Cell Biology. 2 (8): 476–83. doi:10.1038/35019510. PMID 10934467. S2CID 20374981.
  5. ^ a b c Page Module:Citation/CS1/styles.css has no content.Oh WK, Song J (Aug 2003). "Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation". Molecules and Cells. 16 (1): 84–91. doi:10.1016/S1016-8478(23)13770-8. PMID 14503850.
  6. ^ a b Page Module:Citation/CS1/styles.css has no content.Johnson CA, White DA, Lavender JS, O'Neill LP, Turner BM (Mar 2002). "Human class I histone deacetylase complexes show enhanced catalytic activity in the presence of ATP and co-immunoprecipitate with the ATP-dependent chaperone protein Hsp70". The Journal of Biological Chemistry. 277 (11): 9590–7. doi:10.1074/jbc.M107942200. PMID 11777905.
  7. ^ Page Module:Citation/CS1/styles.css has no content.Nair SC, Toran EJ, Rimerman RA, Hjermstad S, Smithgall TE, Smith DF (Dec 1996). "A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1, and the aryl hydrocarbon receptor". Cell Stress & Chaperones. 1 (4): 237–50. doi:10.1379/1466-1268(1996)001<0237:apomci>2.3.co;2 (inactive 12 July 2025). PMC 376461. PMID 9222609.{{cite journal}}: CS1 maint: DOI inactive as of July 2025 (link)
  8. ^ Page Module:Citation/CS1/styles.css has no content.Abravaya K, Myers MP, Murphy SP, Morimoto RI (Jul 1992). "The human heat shock protein hsp70 interacts with HSF, the transcription factor that regulates heat shock gene expression". Genes & Development. 6 (7): 1153–64. doi:10.1101/gad.6.7.1153. PMID 1628823.
  9. ^ Page Module:Citation/CS1/styles.css has no content.Anwar A, Siegel D, Kepa JK, Ross D (Apr 2002). "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1". The Journal of Biological Chemistry. 277 (16): 14060–7. doi:10.1074/jbc.M111576200. PMID 11821413.
  10. ^ Page Module:Citation/CS1/styles.css has no content.Ballinger CA, Connell P, Wu Y, Hu Z, Thompson LJ, Yin LY, Patterson C (Jun 1999). "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions". Molecular and Cellular Biology. 19 (6): 4535–45. doi:10.1128/mcb.19.6.4535. PMC 104411. PMID 10330192.

Further reading

Page Template:Refbegin/styles.css has no content.

Lua error in package.lua at line 80: module 'Module:Navbox/configuration' not found.