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3. Cloning and nucleotide sequence comparison of the groE operon of Pseudomonas aeruginosa and Burkholderia cepacia. Jensen P; Fomsgaard A; Høiby N; Hindersson P APMIS; 1995 Feb; 103(2):113-23. PubMed ID: 7538307 [TBL] [Abstract][Full Text] [Related]
4. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. van der Vies SM; Gatenby AA; Georgopoulos C Nature; 1994 Apr; 368(6472):654-6. PubMed ID: 7908418 [TBL] [Abstract][Full Text] [Related]
5. The Escherichia coli groE chaperonins. Georgopoulos C; Ang D Semin Cell Biol; 1990 Feb; 1(1):19-25. PubMed ID: 1983267 [TBL] [Abstract][Full Text] [Related]
6. The chaperonins of Synechocystis PCC 6803 differ in heat inducibility and chaperone activity. Kovács E; van der Vies SM; Glatz A; Török Z; Varvasovszki V; Horváth I; Vígh L Biochem Biophys Res Commun; 2001 Dec; 289(4):908-15. PubMed ID: 11735133 [TBL] [Abstract][Full Text] [Related]
8. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Trent JD; Nimmesgern E; Wall JS; Hartl FU; Horwich AL Nature; 1991 Dec; 354(6353):490-3. PubMed ID: 1836250 [TBL] [Abstract][Full Text] [Related]
9. Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen. Jindal S; Dudani AK; Singh B; Harley CB; Gupta RS Mol Cell Biol; 1989 May; 9(5):2279-83. PubMed ID: 2568584 [TBL] [Abstract][Full Text] [Related]
10. Demonstration by genetic suppression of interaction of GroE products with many proteins. Van Dyk TK; Gatenby AA; LaRossa RA Nature; 1989 Nov; 342(6248):451-3. PubMed ID: 2573840 [TBL] [Abstract][Full Text] [Related]
11. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Goloubinoff P; Christeller JT; Gatenby AA; Lorimer GH Nature; 1989 Dec 21-28; 342(6252):884-9. PubMed ID: 10532860 [TBL] [Abstract][Full Text] [Related]
12. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. Mogk A; Homuth G; Scholz C; Kim L; Schmid FX; Schumann W EMBO J; 1997 Aug; 16(15):4579-90. PubMed ID: 9303302 [TBL] [Abstract][Full Text] [Related]
13. Sequence and structural homology between a mouse T-complex protein TCP-1 and the 'chaperonin' family of bacterial (GroEL, 60-65 kDa heat shock antigen) and eukaryotic proteins. Gupta RS Biochem Int; 1990; 20(4):833-41. PubMed ID: 1972327 [TBL] [Abstract][Full Text] [Related]
14. Isolation and sequence analysis of rpoH genes encoding sigma 32 homologs from gram negative bacteria: conserved mRNA and protein segments for heat shock regulation. Nakahigashi K; Yanagi H; Yura T Nucleic Acids Res; 1995 Nov; 23(21):4383-90. PubMed ID: 7501460 [TBL] [Abstract][Full Text] [Related]
15. Molecular characterization of the gene operon of heat shock proteins HSP60 and HSP10 in methicillin-resistant Staphylococcus aureus. Ohta T; Honda K; Kuroda M; Saito K; Hayashi H Biochem Biophys Res Commun; 1993 Jun; 193(2):730-7. PubMed ID: 7916607 [TBL] [Abstract][Full Text] [Related]
16. Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli (groEL) and chloroplasts (Rubisco-binding protein). Waldinger D; Eckerskorn C; Lottspeich F; Cleve H Biol Chem Hoppe Seyler; 1988 Oct; 369(10):1185-9. PubMed ID: 2907406 [TBL] [Abstract][Full Text] [Related]