GroES

Revision as of 17:56, 4 September 2012 by WikiBot (talk | contribs) (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search


Heat shock 10kDa protein 1 (chaperonin 10)
Identifiers
Symbols HSPE1 ; CPN10; GROES; HSP10
External IDs Template:OMIM5 Template:MGI HomoloGene: 20500
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Heat shock 10kDa protein 1 (chaperonin 10), also known as HSPE1 or GroES, is a chaperonin which usually works in conjunction with GroEL.[1] In eukaryotes, it is very similar to Heat Shock Protein 10 or Hsp10.

References

  1. ↑ "Entrez Gene: HSPE1 heat shock 10kDa protein 1 (chaperonin 10)".

Further reading

  • Czarnecka AM, Campanella C, Zummo G, Cappello F (2007). "Heat shock protein 10 and signal transduction: a "capsula eburnea" of carcinogenesis?". Cell Stress Chaperones. 11 (4): 287–94. PMID 17278877.
  • Legname G, Fossati G, Gromo G; et al. (1995). "Expression in Escherichia coli, purification and functional activity of recombinant human chaperonin 10". FEBS Lett. 361 (2–3): 211–4. PMID 7698325.
  • Cavanagh AC, Morton H (1994). "The purification of early-pregnancy factor to homogeneity from human platelets and identification as chaperonin 10". Eur. J. Biochem. 222 (2): 551–60. PMID 7912672.
  • Monzini N, Legname G, Marcucci F; et al. (1994). "Identification and cloning of human chaperonin 10 homologue". Biochim. Biophys. Acta. 1218 (3): 478–80. PMID 7914093.
  • Chen JJ, McNealy DJ, Dalal S, Androphy EJ (1994). "Isolation, sequence analysis and characterization of a cDNA encoding human chaperonin 10". Biochim. Biophys. Acta. 1219 (1): 189–90. PMID 7916212.
  • Samali A, Cai J, Zhivotovsky B; et al. (1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMID 10205158.
  • Summers KM, Fletcher BH, Macaranas DD; et al. (2000). "Mapping and characterization of the eukaryotic early pregnancy factor/chaperonin 10 gene family". Somat. Cell Mol. Genet. 24 (6): 315–26. PMID 10763410.
  • Richardson A, Schwager F, Landry SJ, Georgopoulos C (2001). "The importance of a mobile loop in regulating chaperonin/ co-chaperonin interaction: humans versus Escherichia coli". J. Biol. Chem. 276 (7): 4981–7. doi:10.1074/jbc.M008628200. PMID 11050098.
  • Fletcher BH, Cassady AI, Summers KM, Cavanagh AC (2001). "The murine chaperonin 10 gene family contains an intronless, putative gene for early pregnancy factor, Cpn10-rs1". Mamm. Genome. 12 (2): 133–40. PMID 11210183.
  • Parissi V, Calmels C, De Soultrait VR; et al. (2001). "Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60". J. Virol. 75 (23): 11344–53. doi:10.1128/JVI.75.23.11344-11353.2001. PMID 11689615.
  • Hansen JJ, Dürr A, Cournu-Rebeix I; et al. (2002). "Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60". Am. J. Hum. Genet. 70 (5): 1328–32. PMID 11898127.
  • Guidry JJ, Wittung-Stafshede P (2002). "Low stability for monomeric human chaperonin protein 10: interprotein interactions contribute majority of oligomer stability". Arch. Biochem. Biophys. 405 (2): 280–2. PMID 12220543.
  • Lee KH, Kim HS, Jeong HS, Lee YS (2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". Biochem. Biophys. Res. Commun. 298 (2): 216–24. PMID 12387818.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Hansen JJ, Bross P, Westergaard M; et al. (2003). "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter". Hum. Genet. 112 (1): 71–7. doi:10.1007/s00439-002-0837-9. PMID 12483302.
  • Mansell JP, Yarram SJ, Brown NL, Sandy JR (2004). "Type I collagen synthesis by human osteoblasts in response to placental lactogen and chaperonin 10, a homolog of early-pregnancy factor". In Vitro Cell. Dev. Biol. Anim. 38 (9): 518–22. PMID 12703979.
  • Cappello F, Bellafiore M, David S; et al. (2003). "Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix". Cancer Lett. 196 (1): 35–41. PMID 12860287.
  • Shan YX, Liu TJ, Su HF; et al. (2004). "Hsp10 and Hsp60 modulate Bcl-2 family and mitochondria apoptosis signaling induced by doxorubicin in cardiac muscle cells". J. Mol. Cell. Cardiol. 35 (9): 1135–43. PMID 12967636.
  • Shan YX, Yang TL, Mestril R, Wang PH (2003). "Hsp10 and Hsp60 suppress ubiquitination of insulin-like growth factor-1 receptor and augment insulin-like growth factor-1 receptor signaling in cardiac muscle: implications on decreased myocardial protection in diabetic cardiomyopathy". J. Biol. Chem. 278 (46): 45492–8. doi:10.1074/jbc.M304498200. PMID 12970367.
  • Guidry JJ, Shewmaker F, Maskos K; et al. (2004). "Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identified". BMC Biochem. 4: 14. doi:10.1186/1471-2091-4-14. PMID 14525625.

External links

Template:WikiDoc Sources

Retrieved from "https://www.wikidoc.org/index.php?title=GroES&oldid=715914"