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Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding.
van der Vies SM, Gatenby AA, Georgopoulos C. van der Vies SM, et al. Among authors: gatenby aa. Nature. 1994 Apr 14;368(6472):654-6. doi: 10.1038/368654a0. Nature. 1994. PMID: 7908418
A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form.
Mummert E, Grimm R, Speth V, Eckerskorn C, Schiltz E, Gatenby AA, Schäfer E. Mummert E, et al. Among authors: gatenby aa. Nature. 1993 Jun 17;363(6430):644-8. doi: 10.1038/363644a0. Nature. 1993. PMID: 8099715
Chaperonin-mediated reconstitution of the phytochrome photoreceptor.
Grimm R, Donaldson GK, van der Vies SM, Schäfer E, Gatenby AA. Grimm R, et al. Among authors: gatenby aa. J Biol Chem. 1993 Mar 5;268(7):5220-6. J Biol Chem. 1993. PMID: 8095267
Demonstration by genetic suppression of interaction of GroE products with many proteins.
Van Dyk TK, Gatenby AA, LaRossa RA. Van Dyk TK, et al. Among authors: gatenby aa. Nature. 1989 Nov 23;342(6248):451-3. doi: 10.1038/342451a0. Nature. 1989. PMID: 2573840
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.
Goloubinoff P, Gatenby AA, Lorimer GH. Goloubinoff P, et al. Among authors: gatenby aa. Nature. 1989 Jan 5;337(6202):44-7. doi: 10.1038/337044a0. Nature. 1989. PMID: 2562907
Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.
Lubben TH, Gatenby AA, Donaldson GK, Lorimer GH, Viitanen PV. Lubben TH, et al. Among authors: gatenby aa. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7683-7. doi: 10.1073/pnas.87.19.7683. Proc Natl Acad Sci U S A. 1990. PMID: 1977163 Free PMC article.
Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria.
Gatenby AA, Viitanen PV, Lorimer GH. Gatenby AA, et al. Trends Biotechnol. 1990 Dec;8(12):354-8. doi: 10.1016/0167-7799(90)90224-l. Trends Biotechnol. 1990. PMID: 1369447 Review.
Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins.
Viitanen PV, Gatenby AA, Lorimer GH. Viitanen PV, et al. Among authors: gatenby aa. Protein Sci. 1992 Mar;1(3):363-9. doi: 10.1002/pro.5560010308. Protein Sci. 1992. PMID: 1363913 Free PMC article.
A mutation in GroEL interferes with protein folding by reducing the rate of discharge of sequestered polypeptides.
Baneyx F, Gatenby AA. Baneyx F, et al. Among authors: gatenby aa. J Biol Chem. 1992 Jun 5;267(16):11637-44. J Biol Chem. 1992. PMID: 1350786
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. Goloubinoff P, et al. Among authors: gatenby aa. Nature. 1989 Dec 21-28;342(6252):884-9. doi: 10.1038/342884a0. Nature. 1989. PMID: 10532860
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