Crossref
journal-article
Elsevier BV
Structure (78)
References
54
Referenced
34
10.1038/nsb1002-716
/ Nat. Struct. Biol. / Where chaperones and nascent polypeptides meet by Albanese (2002)10.1016/S0079-6107(00)00005-5
/ Prog. Biophys. Mol. Biol. / A decade of progress in understanding the structural basis of protein synthesis by Al-Karadaghi (2000)10.1046/j.1432-1327.2000.01355.x
/ Eur. J. Biochem. / Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium by Bang (2000)10.1093/protein/6.1.37
/ Protein Eng. / Alscript by Barton (1993)10.1016/S1097-2765(03)00009-1
/ Mol. Cell / Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression by Bashan (2003)10.1093/emboj/19.1.134
/ EMBO J. / Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor by Beck (2000)10.1016/S0092-8674(01)00541-4
/ Cell / Architecture of the protein-conducting channel associated with the translating 80S ribosome by Beckmann (2001)10.1038/nsb915
/ Nat. Struct. Biol. / Structural insight into the role of the ribosomal tunnel in cellular regulation by Berisio (2003)10.1016/S0022-2836(02)01436-5
/ J. Mol. Biol. / Localization of the trigger factor binding site on the ribosomal 50S subunit by Blaha (2003)10.1006/jmbi.2001.5359
/ J. Mol. Biol. / Crystal structure of the 30 S ribosomal subunit from Thermus thermophilus by Brodersen (2002)10.1107/S0907444998003254
/ Acta Crystallogr. D / Crystallography & NMR system by Brunger (1998)10.1016/0014-5793(95)01109-R
/ FEBS Lett. / Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family by Callebaut (1995){'key': '10.1016/j.str.2003.11.003_BIB13', 'first-page': '760', 'article-title': 'The CCP4 (Collaborative Computational Project 4) suite', 'volume': '50', 'author': 'CCP4', 'year': '1994', 'journal-title': 'Acta Crystallogr. D'}
/ Acta Crystallogr. D / The CCP4 (Collaborative Computational Project 4) suite by CCP4 (1994)10.1093/emboj/17.16.4545
/ EMBO J. / The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface by Davies (1998){'key': '10.1016/j.str.2003.11.003_BIB15', 'series-title': 'The PyMOL Molecular Graphics System', 'author': 'DeLano', 'year': '2002'}
/ The PyMOL Molecular Graphics System by DeLano (2002)10.1046/j.1365-2958.2003.03370.x
/ Mol. Microbiol. / Trigger Factor and DnaK possess overlapping substrate pools and binding specificities by Deuerling (2003)10.1038/88549
/ Nat. Struct. Biol. / The structural basis of protein targeting and translocation in bacteria by Driessen (2001)10.1016/S0959-440X(99)00044-5
/ Curr. Opin. Struct. Biol. / Protein folding in vivo by Feldman (2000)10.1016/S0076-6879(97)76073-7
/ Methods in Enzymology / Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods by de La Fortelle (1997)10.1261/rna.2196403
/ RNA / The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome by Gu (2003)10.1074/jbc.272.35.21865
/ J. Biol. Chem. / The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes by Hesterkamp (1997)10.1006/jmbi.1993.1489
/ J. Mol. Biol. / Protein structure comparison by alignment of distance matrices by Holm (1993)10.1126/science.7761829
/ Science / Classical electrostatics in biology and chemistry by Honig (1995)10.1073/pnas.93.1.13
/ Proc. Natl. Acad. Sci. USA / Principles of protein-protein interactions by Jones (1996){'key': '10.1016/j.str.2003.11.003_BIB25', 'series-title': 'Crystallographic and Modeling Methods in Molecular Design', 'first-page': '189', 'article-title': 'O', 'author': 'Jones', 'year': '1990'}
/ Crystallographic and Modeling Methods in Molecular Design / O by Jones (1990)10.1074/jbc.274.53.37743
/ J. Biol. Chem. / Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL by Kandror (1999)10.1073/pnas.89.6.2195
/ Proc. Natl. Acad. Sci. USA / Molecular surface recognition by Katchalski-Katzir (1992)10.1038/87639
/ Nat. Struct. Biol. / Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity by Kim (2001)10.1107/S0907444995014983
/ Acta Crystallogr. D / xdlMAPMAN and xdlDATAMAN—programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets by Kleywegt (1996)10.1107/S0907444998007100
/ Acta Crystallogr. D / Databases in protein crystallography by Kleywegt (1998)10.1038/nature01047
/ Nature / L23 protein functions as a chaperone docking site on the ribosome by Kramer (2002)10.1107/S0021889891004399
/ J. Appl. Crystallogr. / Molscript by Kraulis (1991){'key': '10.1016/j.str.2003.11.003_BIB33', 'series-title': 'International Tables for Crystallography', 'first-page': '720', 'article-title': 'The ARP/wARP suite for automated construction and refinement of protein models', 'author': 'Lamzin', 'year': '2001'}
/ International Tables for Crystallography / The ARP/wARP suite for automated construction and refinement of protein models by Lamzin (2001)10.1107/S0021889892009944
/ J. Appl. Crystallogr. / Procheck by Laskowski (1993)10.1016/S0014-5793(01)02896-4
/ FEBS Lett. / The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli by Li (2001)10.1016/S0022-2836(02)01427-4
/ J. Mol. Biol. / Interaction of trigger factor with the ribosome by Maier (2003)10.1016/S0022-2836(02)01111-7
/ J. Mol. Biol. / Structure of the mammalian ribosome-channel complex at 17 Å resolution by Morgan (2002)10.1126/science.289.5481.920
/ Science / The structural basis of ribosome activity in peptide bond synthesis by Nissen (2000)10.1515/BC.2002.182
/ Biol. Chem. / Three-state equilibrium of Escherichia coli trigger factor by Patzelt (2002)10.1073/pnas.261432298
/ Proc. Natl. Acad. Sci. USA / Binding specificity of Escherichia coli trigger factor by Patzelt (2001)10.1126/science.1072366
/ Science / Distinct modes of signal recognition particle interaction with the ribosome by Pool (2002)10.1038/358768a0
/ Nature / The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA by Ramakrishnan (1992)10.1016/S0968-0004(98)01193-1
/ Trends Biochem. Sci. / The ins and outs of a molecular chaperone machine by Richardson (1998)10.1093/emboj/16.1.54
/ EMBO J. / Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding by Scholz (1997)10.1093/emboj/19.4.749
/ EMBO J. / Structure of Hsp15 reveals a novel RNA-binding motif by Staker (2000)10.1002/j.1460-2075.1995.tb00177.x
/ EMBO J. / A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor by Stoller (1995)10.1107/S0907444900005072
/ Acta Crystallogr. D / Maximum-likelihood density modification by Terwilliger (2000)10.1107/S0907444999000839
/ Acta Crystallogr. D / Automated MAD and MIR structure solution by Terwilliger (1999)10.1083/jcb.200302130
/ J. Cell Biol. / Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome by Ullers (2003)10.1006/jmbi.1993.1012
/ J. Mol. Biol. / Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin by Van Duyne (1993)10.1016/S0022-2836(02)00112-2
/ J. Mol. Biol. / NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein by Vogtherr (2002)10.1038/35030006
/ Nature / Structure of the 30S ribosomal subunit by Wimberly (2000)10.2174/1389203023380828
/ Curr. Protein Pept. Sci. / High-resolution structures of large ribosomal subunits from mesophilic eubacteria and halophilic archaea at various functional states by Yonath (2002)10.1126/science.1060089
/ Science / Crystal structure of the ribosome at 5.5 Å resolution by Yusupov (2001)
Dates
Type | When |
---|---|
Created | 21 years, 8 months ago (Dec. 6, 2003, 6:47 a.m.) |
Deposited | 5 years, 5 months ago (March 27, 2020, 3:20 p.m.) |
Indexed | 1 year, 6 months ago (Feb. 10, 2024, 12:23 p.m.) |
Issued | 21 years, 8 months ago (Dec. 1, 2003) |
Published | 21 years, 8 months ago (Dec. 1, 2003) |
Published Print | 21 years, 8 months ago (Dec. 1, 2003) |
@article{Kristensen_2003, title={Chaperone Binding at the Ribosomal Exit Tunnel}, volume={11}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/j.str.2003.11.003}, DOI={10.1016/j.str.2003.11.003}, number={12}, journal={Structure}, publisher={Elsevier BV}, author={Kristensen, Ole and Gajhede, Michael}, year={2003}, month=dec, pages={1547–1556} }