BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

251 related articles for article (PubMed ID: 8096339)

  • 1. Substoichiometric amounts of the molecular chaperones GroEL and GroES prevent thermal denaturation and aggregation of mammalian mitochondrial malate dehydrogenase in vitro.
    Hartman DJ; Surin BP; Dixon NE; Hoogenraad NJ; Høj PB
    Proc Natl Acad Sci U S A; 1993 Mar; 90(6):2276-80. PubMed ID: 8096339
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES.
    Peralta D; Hartman DJ; Hoogenraad NJ; Høj PB
    FEBS Lett; 1994 Feb; 339(1-2):45-9. PubMed ID: 7906229
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Refolding and recognition of mitochondrial malate dehydrogenase by Escherichia coli chaperonins cpn 60 (groEL) and cpn10 (groES).
    Hutchinson JP; el-Thaher TS; Miller AD
    Biochem J; 1994 Sep; 302 ( Pt 2)(Pt 2):405-10. PubMed ID: 7916564
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Minimal and optimal mechanisms for GroE-mediated protein folding.
    Ben-Zvi AP; Chatellier J; Fersht AR; Goloubinoff P
    Proc Natl Acad Sci U S A; 1998 Dec; 95(26):15275-80. PubMed ID: 9860959
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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]  

  • 6. Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation.
    Kawata Y; Nosaka K; Hongo K; Mizobata T; Nagai J
    FEBS Lett; 1994 May; 345(2-3):229-32. PubMed ID: 7911090
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Assay of malate dehydrogenase. A substrate for the E. coli chaperonins GroEL and GroES.
    Hayer-Hartl M
    Methods Mol Biol; 2000; 140():127-32. PubMed ID: 11484479
    [No Abstract]   [Full Text] [Related]  

  • 8. Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system.
    Illingworth M; Salisbury J; Li W; Lin D; Chen L
    Biochem Biophys Res Commun; 2015 Oct; 466(1):15-20. PubMed ID: 26271593
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Folding of malate dehydrogenase inside the GroEL-GroES cavity.
    Chen J; Walter S; Horwich AL; Smith DL
    Nat Struct Biol; 2001 Aug; 8(8):721-8. PubMed ID: 11473265
    [TBL] [Abstract][Full Text] [Related]  

  • 10. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
    Chatellier J; Hill F; Fersht AR
    J Mol Biol; 2000 Dec; 304(5):883-96. PubMed ID: 11124034
    [TBL] [Abstract][Full Text] [Related]  

  • 11. GroEL of the nitrogen-fixing cyanobacterium Anabaena sp. strain L-31 exhibits GroES and ATP-independent refolding activity.
    Potnis AA; Rajaram H; Apte SK
    J Biochem; 2016 Mar; 159(3):295-304. PubMed ID: 26449235
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Plant glyoxysomal but not mitochondrial malate dehydrogenase can fold without chaperone assistance.
    Gietl C; Seidel C; Svendsen I
    Biochim Biophys Acta; 1996 May; 1274(1-2):48-58. PubMed ID: 8645694
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Purification and characterization of chaperonin 60 and chaperonin 10 from the anaerobic thermophile Thermoanaerobacter brockii.
    Truscott KN; Høj PB; Scopes RK
    Eur J Biochem; 1994 Jun; 222(2):277-84. PubMed ID: 7912671
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
    Gupta P; Aggarwal N; Batra P; Mishra S; Chaudhuri TK
    Int J Biochem Cell Biol; 2006; 38(11):1975-85. PubMed ID: 16822698
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy.
    Chen S; Roseman AM; Hunter AS; Wood SP; Burston SG; Ranson NA; Clarke AR; Saibil HR
    Nature; 1994 Sep; 371(6494):261-4. PubMed ID: 7915827
    [TBL] [Abstract][Full Text] [Related]  

  • 16. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
    Chatellier J; Hill F; Foster NW; Goloubinoff P; Fersht AR
    J Mol Biol; 2000 Dec; 304(5):897-910. PubMed ID: 11124035
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.
    Illingworth M; Ramsey A; Zheng Z; Chen L
    J Biol Chem; 2011 Sep; 286(35):30401-30408. PubMed ID: 21757689
    [TBL] [Abstract][Full Text] [Related]  

  • 18. A comparison of the GroE chaperonin requirements for sequentially and structurally homologous malate dehydrogenases: the importance of folding kinetics and solution environment.
    Tieman BC; Johnston MF; Fisher MT
    J Biol Chem; 2001 Nov; 276(48):44541-50. PubMed ID: 11551947
    [TBL] [Abstract][Full Text] [Related]  

  • 19. On the role of groES in the chaperonin-assisted folding reaction. Three case studies.
    Schmidt M; Buchner J; Todd MJ; Lorimer GH; Viitanen PV
    J Biol Chem; 1994 Apr; 269(14):10304-11. PubMed ID: 7908292
    [TBL] [Abstract][Full Text] [Related]  

  • 20. On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding.
    Hayer-Hartl MK; Ewalt KL; Hartl FU
    Biol Chem; 1999 May; 380(5):531-40. PubMed ID: 10384959
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 13.