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Items: 1 to 20 of 39

1.
ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle
Elliott Crooke, Brenda Guthrie, Stewart Lecker, Roland Lill, William Wickner
Cell. 1988 Sep 23; 54(7): 1003–1011. Published online 2004 May 7. doi: 10.1016/0092-8674(88)90115-8
PMCID:
PMC7133343
ArticlePDF–2.0M
2.
Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone
Soichiro Kawagoe, Hiroshi Nakagawa, Hiroyuki Kumeta, Koichiro Ishimori, Tomohide Saio
J Biol Chem. 2018 Sep 28; 293(39): 15095–15106. Published online 2018 Aug 9. doi: 10.1074/jbc.RA118.003579
PMCID:
PMC6166725
ArticlePDF–4.5M
3.
Structural Basis for Protein anti-Aggregation Activity of the Trigger Factor Chaperone*
Tomohide Saio, Xiao Guan, Paolo Rossi, Anastassios Economou, Charalampos G. Kalodimos
Science. Author manuscript; available in PMC 2014 Jun 25.
Published in final edited form as: Science. 2014 May 9; 344(6184): 1250494. doi: 10.1126/science.1250494
PMCID:
PMC4070327
ArticlePDF–2.0M
4.
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome
Frieder Merz, Daniel Boehringer, Christiane Schaffitzel, Steffen Preissler, Anja Hoffmann, Timm Maier, Anna Rutkowska, Jasmin Lozza, Nenad Ban, Bernd Bukau, Elke Deuerling
EMBO J. 2008 Jun 4; 27(11): 1622–1632. Published online 2008 May 22. doi: 10.1038/emboj.2008.89
PMCID:
PMC2426727
ArticlePDF–910K
5.
Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor
Yi Shi, Dong-Jie Fan, Shu-Xin Li, Hong-Jie Zhang, Sarah Perrett, Jun-Mei Zhou
Protein Sci. 2007 Jun; 16(6): 1165–1175. doi: 10.1110/ps.062623707
PMCID:
PMC2206664
ArticlePDF–699K
6.
Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding.
C Scholz, G Stoller, T Zarnt, G Fischer, F X Schmid
EMBO J. 1997 Jan 2; 16(1): 54–58. doi: 10.1093/emboj/16.1.54
PMCID:
PMC1169613
SummaryPDF–191K
7.
A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.
G Stoller, K P Rücknagel, K H Nierhaus, F X Schmid, G Fischer, J U Rahfeld
EMBO J. 1995 Oct 16; 14(20): 4939–4948. doi: 10.1002/j.1460-2075.1995.tb00177.x
PMCID:
PMC394597
ArticlePDF–2.1M
8.
Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form.
E Crooke, W Wickner
Proc Natl Acad Sci U S A. 1987 Aug; 84(15): 5216–5220. doi: 10.1073/pnas.84.15.5216
PMCID:
PMC298825
ArticlePDF–1.4M
9.
Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli
Kazuyo Nishihara, Masaaki Kanemori, Hideki Yanagi, Takashi Yura
Appl Environ Microbiol. 2000 Mar; 66(3): 884–889. doi: 10.1128/aem.66.3.884-889.2000
PMCID:
PMC91917
ArticlePDF–743K
10.
Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
T Hesterkamp, S Hauser, H Lütcke, B Bukau
Proc Natl Acad Sci U S A. 1996 Apr 30; 93(9): 4437–4441. doi: 10.1073/pnas.93.9.4437
PMCID:
PMC39556
ArticlePDF–1.3M
11.
Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures
Olga Kandror, Alfred L. Goldberg
Proc Natl Acad Sci U S A. 1997 May 13; 94(10): 4978–4981. doi: 10.1073/pnas.94.10.4978
PMCID:
PMC24616
ArticlePDF–250K
12.
Copper Induces Protein Aggregation, a Toxic Process Compensated by Molecular Chaperones
Lisa Zuily, Nora Lahrach, Rosi Fassler, Olivier Genest, Peter Faller, Olivier Sénèque, Yann Denis, Marie-Pierre Castanié-Cornet, Pierre Genevaux, Ursula Jakob, Dana Reichmann, Marie-Thérèse Giudici-Orticoni, Marianne Ilbert
mBio. 2022 Mar-Apr; 13(2): e03251-21. Published online 2022 Mar 15. doi: 10.1128/mbio.03251-21
PMCID:
PMC9040851
ArticlePDF–3.3M
13.
Expression and purification of the functional ectodomain of human anthrax toxin receptor 2 in E. coli Origami B cells with assistance of bacterial Trigger Factor
Pedro Jacquez, Ningjing Lei, David Weigt, Chuan Xiao, Jianjun Sun
Protein Expr Purif. Author manuscript; available in PMC 2015 Mar 1.
Published in final edited form as: Protein Expr Purif. 2014 Mar; 95: 149–155. Published online 2013 Dec 28. doi: 10.1016/j.pep.2013.12.010
PMCID:
PMC4222247
ArticlePDF–713K
14.
Chaperone domains convert prolyl isomerases into generic catalysts of protein folding
Roman P. Jakob, Gabriel Zoldák, Tobias Aumüller, Franz X. Schmid
Proc Natl Acad Sci U S A. 2009 Dec 1; 106(48): 20282–20287. Published online 2009 Nov 17. doi: 10.1073/pnas.0909544106
PMCID:
PMC2787138
ArticlePDF–1.2M
15.
Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.
G. C. Huang, Z. Y. Li, J. M. Zhou, G. Fischer
Protein Sci. 2000 Jun; 9(6): 1254–1261. doi: 10.1110/ps.9.6.1254
PMCID:
PMC2144665
SummaryPDF–218K
16.
In vivo analysis of the overlapping functions of DnaK and trigger factor
Pierre Genevaux, France Keppel, Françoise Schwager, Petra S Langendijk-Genevaux, F Ulrich Hartl, Costa Georgopoulos
EMBO Rep. 2004 Feb; 5(2): 195–200. Published online 2004 Jan 9. doi: 10.1038/sj.embor.7400067
PMCID:
PMC1298978
ArticlePDF–187K
17.
Trigger factor depletion or overproduction causes defective cell division but does not block protein export.
B Guthrie, W Wickner
J Bacteriol. 1990 Oct; 172(10): 5555–5562. doi: 10.1128/jb.172.10.5555-5562.1990
PMCID:
PMC526866
ArticlePDF–2.3M
18.
Trigger factor binds to ribosome–signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor
Iwona Buskiewicz, Elke Deuerling, Shan-Qing Gu, Johannes Jöckel, Marina V. Rodnina, Bernd Bukau, Wolfgang Wintermeyer
Proc Natl Acad Sci U S A. 2004 May 25; 101(21): 7902–7906. Published online 2004 May 17. doi: 10.1073/pnas.0402231101
PMCID:
PMC419529
ArticlePDF–370K
19.
Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.
S Lecker, R Lill, T Ziegelhoffer, C Georgopoulos, P J Bassford, Jr, C A Kumamoto, W Wickner
EMBO J. 1989 Sep; 8(9): 2703–2709. doi: 10.1002/j.1460-2075.1989.tb08411.x
PMCID:
PMC401277
ArticlePDF–1.6M
20.
Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins.
O Kandror, M Sherman, M Rhode, A L Goldberg
EMBO J. 1995 Dec 1; 14(23): 6021–6027. doi: 10.1002/j.1460-2075.1995.tb00290.x
PMCID:
PMC394722
ArticlePDF–1.4M

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