Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
54
Referenced
112
{'year': '2004', 'series-title': 'Structural Aspects of Protein Synthesis', 'author': 'Liljas', 'key': '10.1016/j.jmb.2006.10.025_bib1'}
/ Structural Aspects of Protein Synthesis by Liljas (2004)10.1126/science.289.5481.905
/ Science / The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution by Ban (2000)10.1038/35030006
/ Nature / Structure of the 30S ribosomal subunit by Wimberly (2000)10.1016/S0092-8674(00)00084-2
/ Cell / Structure of functionally activated small ribosomal subunit at 3.3 angstroms resolution by Schluenzen (2000)10.1016/S0092-8674(00)80690-X
/ Cell / Solution structure of the E. coli 70S ribosome at 11.5 Å resolution by Gabashvili (2000)10.1126/science.1060089
/ Science / Crystal structure of the ribosome at 5.5 Å resolution by Yusupov (2001)10.1126/science.1117230
/ Science / Structures of the bacterial ribosome at 3.5 Å resolution by Schuwirth (2005)10.1016/j.cell.2005.09.039
/ Cell / Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon by Petry (2005)10.1016/j.cell.2005.03.023
/ Cell / The cryo-EM structure of a translation initiation complex from Escherichia coli by Allen (2005)10.1016/S0092-8674(03)00476-8
/ Cell / Locking and unlocking of ribosomal motions by Valle (2003)10.1038/sj.emboj.7600102
/ EMBO J. / Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation by Spahn (2004)10.1016/S0092-8674(00)80927-7
/ Cell / Molecular movement inside the translational engine by Wilson (1998)10.1016/S0968-0004(03)00066-5
/ Trends Biochem. Sci. / Insights into the decoding mechanism from recent ribosome structures by Ogle (2003)10.1016/S0959-440X(00)00143-3
/ Curr. Opin. Struct. Biol. / The end of the beginning: structural studies of ribosomal proteins by Sanyal (2000)10.1021/bi026301y
/ Biochemistry / GTPase activation of elongation factors Tu and G on the ribosome by Mohr (2002)10.1016/j.cell.2005.04.015
/ Cell / Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation by Diaconu (2005)10.1038/sj.emboj.7600884
/ EMBO J. / Control of phosphate release from elongation factor G by ribosomal protein L7/12 by Savelsbergh (2005)10.2174/1389203023380756
/ Curr. Protein Pept. Sci. / Structure and function of the acidic ribosomal stalk proteins by Wahl (2002)10.1016/j.bbagen.2005.03.009
/ Biochim. Biophys. Acta / Acquisition of a stable structure by yeast ribosomal PO protein requires binding of P1A-P2B complex: in vitro formation of the stalk structure by Krokowski (2005)10.1139/o95-103
/ Biochem. Cell Biol. / Proteins P1, P2, and P0, components of the eukaryotic ribosome stalk. New structural and functional aspects by Remacha (1995)10.1074/jbc.M313384200
/ J. Biol. Chem. / From structure and dynamics of protein L7/L12 to molecular switching in ribosome by Bocharov (2004)10.1021/bi0495331
/ Biochemistry / Conformation and dynamics of ribosomal stalk protein L12 in solution and on the ribosome by Mulder (2004)10.1073/pnas.0400928101
/ Proc. Natl Acad. Sci. USA / Heteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomes by Christodoulou (2004)10.1016/0022-2836(87)90183-5
/ J. Mol. Biol. / Structure of the C-terminal domain of the ribosomal protein-L7 protein-L12 from Escherichia coli at 1.7 Å by Leijonmarck (1987)10.1016/S0092-8674(01)00546-3
/ Cell / High resolution structure of the large ribosomal subunit from a mesophilic eubacterium by Harms (2001)10.1016/0014-5793(82)80448-1
/ FEBS Letters / Proton nuclear magnetic resonance study of the ribosomal protein L7/L12 in situ by Gudkov (1982)10.1016/S0021-9258(17)42543-9
/ J. Biol. Chem. / Mobile domains in ribosomes revealed by proton nuclear magnetic resonance by Cowgill (1984)10.1021/bi9615001
/ Biochemistry / Rotational and conformational dynamics of Escherichia coli ribosomal protein L7/L12 by Hamman (1996)10.1016/0014-5793(84)80906-0
/ FEBS Letters / The L7/L12 proteins change their conformation upon interaction of EF-G with ribosomes by Gudkov (1984)10.1038/10695
/ Nature Struct. Biol. / EF-G dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome by Agrawal (1999)10.1038/38770
/ Nature / Visualization of elongation factor Tu on the Escherichia coli ribosome by Stark (1997)10.1038/nsb1003
/ Nature Struct. Biol. / Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy by Valle (2003){'key': '10.1016/j.jmb.2006.10.025_bib33', 'series-title': 'The Translational Apparatus: Structure, Function, Evolution', 'first-page': '521', 'article-title': 'Structure and function of Escherichia coli ribosomal protein L7/L12: effect of cross-links and deletions', 'author': 'Traut', 'year': '1993'}
/ The Translational Apparatus: Structure, Function, Evolution / Structure and function of Escherichia coli ribosomal protein L7/L12: effect of cross-links and deletions by Traut (1993)10.1016/S0021-9258(19)62705-5
/ J. Biol. Chem. / Localization of two epitopes of protein L7/L12 to both the body and stalk of the large ribosomal subunit. Immune electron microscopy using monoclonal antibodies by Olson (1986)10.1074/jbc.273.3.1670
/ J. Biol. Chem. / Cross-linking of selected residues in the N- and C-terminal domains of Escherichia coli protein L7/L12 to other ribosomal proteins and the effect of elongation factor Tu by Dey (1998)10.1074/jbc.275.2.890
/ J. Biol. Chem. / Stimulation of GTPase activity of translation elongation factor G by ribosomal protein L7/L12 by Savelsbergh (2000)10.1016/j.molcel.2005.10.028
/ Mol. Cell / Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM by Datta (2005)10.1016/j.jmb.2003.12.080
/ J. Mol. Biol. / Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome by Kothe (2004)10.1038/379511a0
/ Nature / The structure of the Escherichia coli EF-Tu center dot EF-Ts complex at 2.5 angstrom resolution by Kawashima (1996)10.1073/pnas.95.11.6134
/ Proc. Natl Acad. Sci. USA / Visualization of elongation factor G on the Escherichia coli 70S ribosome: the mechanism of translocation by Agrawal (1998)10.1016/S0092-8674(00)80666-2
/ Cell / Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation by Stark (2000)10.1038/nature02332
/ Nature / Visualization of release factor 3 on the ribosome during termination of protein synthesis by Klaholz (2004)10.1073/pnas.92.11.4748
/ Proc. Natl Acad. Sci. USA / The effect of protein concentration on ion binding by Linse (1995)10.1021/bi034536j
/ Biochemistry / NMR analysis of methyl groups at 100-500 kDa: model systems and Arp2/3 complex by Kreishman-Deitrick (2003)10.1073/pnas.76.7.3174
/ Proc. Natl Acad. Sci. USA / Nucleoside triphosphate regeneration decreases the frequency of translation errors by Jelenc (1979)10.1021/bi00039a007
/ Biochemistry / Interaction of guanosine nucleotides and their analogs with elongation-factor Tu from Thermus thermophilus by Wagner (1995)10.1016/S0092-8674(01)00508-6
/ Cell / A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3 by Zavialov (2001)10.1016/j.ab.2004.06.028
/ Anal. Biochem. / Pure translation display by Forster (2001)10.1111/j.1432-1033.1995.732_a.x
/ Eur. J. Biochem. / Osmo-expression and fast two-step purification of Escherichia coli translation termination factor RF-3 by Mortensen (1995)10.1016/0014-5793(95)01531-0
/ FEBS Letters / Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution by Bocharov (1996)10.1016/S0014-5793(98)00121-5
/ FEBS Letters / Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10 by Bocharov (1998)10.1007/BF00197809
/ J. Biomol. NMR / NMRPipe: a multidimensional spectral processing system based on UNIX pipes by Delaglio (1995)10.1002/prot.20449
/ Proteins: Struct. Funct. Genet. / The CCPN data model for NMR spectroscopy: development of a software pipeline by Vranken (2005)10.1016/0263-7855(96)00009-4
/ J. Mol. Graph. / MOLMOL: a program for display and analysis of macromolecular structures by Koradi (1996)
Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 28, 2006, 3:18 a.m.) |
Deposited | 4 years ago (Aug. 3, 2021, 5:46 p.m.) |
Indexed | 1 month, 3 weeks ago (July 2, 2025, 2:32 p.m.) |
Issued | 18 years, 7 months ago (Jan. 1, 2007) |
Published | 18 years, 7 months ago (Jan. 1, 2007) |
Published Print | 18 years, 7 months ago (Jan. 1, 2007) |
@article{Helgstrand_2007, title={The Ribosomal Stalk Binds to Translation Factors IF2, EF-Tu, EF-G and RF3 via a Conserved Region of the L12 C-terminal Domain}, volume={365}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2006.10.025}, DOI={10.1016/j.jmb.2006.10.025}, number={2}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Helgstrand, Magnus and Mandava, Chandra S. and Mulder, Frans A.A. and Liljas, Anders and Sanyal, Suparna and Akke, Mikael}, year={2007}, month=jan, pages={468–479} }