Category:Complex:GroEL-GroES Chaperonin-CPLX: Difference between revisions

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==About==
'''Description''' (originally from EcoCyc<ref name='LIB:EcoCyc11.1'/>) GroEL-GroES Chaperonin-CPLX
 
'''Comments''' (originally from EcoCyc<ref name='LIB:EcoCyc11.1'/>) The <I>Escherichia coli</I> chaperone protein GroEL (Hsp60) and its regulator
GroES are necessary for the proper folding of certain proteins <ref name='PMID:2573517'/><ref name='PMID:8104102'/><ref name='PMID:7935790'/><ref name='PMID:9285585'/><ref name='PMID:15802642'/><ref name='PMID:9285585'/><ref name='PMID:16051146'/><ref name='PMID:15832945'/><ref name='PMID:2563997'/><ref name='PMID:8104102'/><ref name='PMID:1359538'/><ref name='PMID:7715448'/><ref name='PMID:15944406'/>
 
 
 
==References==
<references/>

Revision as of 12:37, 20 July 2007

About

Description (originally from EcoCyc[1]) GroEL-GroES Chaperonin-CPLX

Comments (originally from EcoCyc[1]) The Escherichia coli chaperone protein GroEL (Hsp60) and its regulator GroES are necessary for the proper folding of certain proteins [2][3][4][5][6][5][7][8][9][3][10][11][12]


References

  1. ↑ 1.0 1.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. ↑ Kusukawa, N et al. (1989) Effects of mutations in heat-shock genes groES and groEL on protein export in Escherichia coli. EMBO J. 8 3517-21 PubMed
  3. ↑ 3.0 3.1 Horwich, AL et al. (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74 909-17 PubMed
  4. ↑ Braig, K et al. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371 578-86 PubMed
  5. ↑ 5.0 5.1 Xu, Z et al. (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388 741-50 PubMed
  6. ↑ Donald, LJ et al. (2005) Multiple equilibria of the Escherichia coli chaperonin GroES revealed by mass spectrometry. Protein Sci 14 1375-9 PubMed
  7. ↑ Kerner, MJ et al. (2005) Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122 209-20 PubMed
  8. ↑ Chaudhuri, TK & Gupta, P (2005) Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach. Cell Stress Chaperones 10 24-36 PubMed
  9. ↑ Fayet, O et al. (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171 1379-85 PubMed
  10. ↑ Gragerov, A et al. (1992) Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 89 10341-4 PubMed
  11. ↑ Gaitanaris, GA et al. (1994) Successive action of Escherichia coli chaperones in vivo. Mol Microbiol 14 861-9 PubMed
  12. ↑ Taguchi, H (2005) Chaperonin GroEL meets the substrate protein as a "load" of the rings. J Biochem 137 543-9 PubMed

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