301 related articles for article (PubMed ID: 8095403)
1. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.
Jackson GS; Staniforth RA; Halsall DJ; Atkinson T; Holbrook JJ; Clarke AR; Burston SG
Biochemistry; 1993 Mar; 32(10):2554-63. PubMed ID: 8095403
[TBL] [Abstract][Full Text] [Related]
2. The origins and consequences of asymmetry in the chaperonin reaction cycle.
Burston SG; Ranson NA; Clarke AR
J Mol Biol; 1995 May; 249(1):138-52. PubMed ID: 7776368
[TBL] [Abstract][Full Text] [Related]
3. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10.
Staniforth RA; Burston SG; Atkinson T; Clarke AR
Biochem J; 1994 Jun; 300 ( Pt 3)(Pt 3):651-8. PubMed ID: 7912068
[TBL] [Abstract][Full Text] [Related]
4. The chaperonin cycle and protein folding.
Lund P
Bioessays; 1994 Apr; 16(4):229-31. PubMed ID: 7913317
[TBL] [Abstract][Full Text] [Related]
5. Differential effects of co-chaperonin homologs on cpn60 oligomers.
Bonshtien AL; Parnas A; Sharkia R; Niv A; Mizrahi I; Azem A; Weiss C
Cell Stress Chaperones; 2009 Sep; 14(5):509-19. PubMed ID: 19224397
[TBL] [Abstract][Full Text] [Related]
6. The formation of symmetrical GroEL-GroES complexes in the presence of ATP.
Llorca O; Marco S; Carrascosa JL; Valpuesta JM
FEBS Lett; 1994 May; 345(2-3):181-6. PubMed ID: 7911087
[TBL] [Abstract][Full Text] [Related]
7. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action.
Mendoza JA; Demeler B; Horowitz PM
J Biol Chem; 1994 Jan; 269(4):2447-51. PubMed ID: 7905478
[TBL] [Abstract][Full Text] [Related]
8. Intermediates in the chaperonin-assisted refolding of rhodanese are trapped at low temperature and show a small stoichiometry.
Mendoza JA; Lorimer GH; Horowitz PM
J Biol Chem; 1991 Sep; 266(26):16973-6. PubMed ID: 1680127
[TBL] [Abstract][Full Text] [Related]
9. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding.
Martin J; Mayhew M; Langer T; Hartl FU
Nature; 1993 Nov; 366(6452):228-33. PubMed ID: 7901770
[TBL] [Abstract][Full Text] [Related]
10. Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase.
Miller AD; Maghlaoui K; Albanese G; Kleinjan DA; Smith C
Biochem J; 1993 Apr; 291 ( Pt 1)(Pt 1):139-44. PubMed ID: 8097086
[TBL] [Abstract][Full Text] [Related]
11. Identification and functional analysis of chaperonin 10, the groES homolog from yeast mitochondria.
Rospert S; Glick BS; Jenö P; Schatz G; Todd MJ; Lorimer GH; Viitanen PV
Proc Natl Acad Sci U S A; 1993 Dec; 90(23):10967-71. PubMed ID: 7902576
[TBL] [Abstract][Full Text] [Related]
12. Hydrolysis of adenosine 5'-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion.
Todd MJ; Viitanen PV; Lorimer GH
Biochemistry; 1993 Aug; 32(33):8560-7. PubMed ID: 8102879
[TBL] [Abstract][Full Text] [Related]
13. Purification and characterization of chaperonins 60 and 10 from Methylobacillus glycogenes.
Kawata Y; Doi K; Omoto H; Mizobata T; Nagai J
Cell Stress Chaperones; 1998 Sep; 3(3):200-7. PubMed ID: 9764760
[TBL] [Abstract][Full Text] [Related]
14. Binding of a chaperonin to the folding intermediates of lactate dehydrogenase.
Badcoe IG; Smith CJ; Wood S; Halsall DJ; Holbrook JJ; Lund P; Clarke AR
Biochemistry; 1991 Sep; 30(38):9195-200. PubMed ID: 1680001
[TBL] [Abstract][Full Text] [Related]
15. Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures.
Mendoza JA; Lorimer GH; Horowitz PM
J Biol Chem; 1992 Sep; 267(25):17631-4. PubMed ID: 1355476
[TBL] [Abstract][Full Text] [Related]
16. Symmetric complexes of GroE chaperonins as part of the functional cycle.
Schmidt M; Rutkat K; Rachel R; Pfeifer G; Jaenicke R; Viitanen P; Lorimer G; Buchner J
Science; 1994 Jul; 265(5172):656-9. PubMed ID: 7913554
[TBL] [Abstract][Full Text] [Related]
17. Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.
Lubben TH; Gatenby AA; Donaldson GK; Lorimer GH; Viitanen PV
Proc Natl Acad Sci U S A; 1990 Oct; 87(19):7683-7. PubMed ID: 1977163
[TBL] [Abstract][Full Text] [Related]
18. Sulfhydryl modification of E. coli Cpn60 leads to loss of its ability to support refolding of rhodanese but not to form a binary complex.
Mendoza JA; Horowitz PM
J Protein Chem; 1992 Dec; 11(6):589-94. PubMed ID: 1361328
[TBL] [Abstract][Full Text] [Related]
19. Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange.
Sadis S; Hightower LE
Biochemistry; 1992 Oct; 31(39):9406-12. PubMed ID: 1356434
[TBL] [Abstract][Full Text] [Related]
20. Identification of nucleotide-binding regions in the chaperonin proteins GroEL and GroES.
Martin J; Geromanos S; Tempst P; Hartl FU
Nature; 1993 Nov; 366(6452):279-82. PubMed ID: 7901771
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]