Crossref
journal-article
Elsevier BV
Biochimie (78)
Authors
2
- John Achenbach (first)
- Knud H. Nierhaus (additional)
References
58
Referenced
17
10.1007/s11084-007-9096-z
/ Orig. Life Evol. Biosphere / Question 6: early steps of evolution and some ideas about a simplified translational machinery by Nierhaus (2007)10.1016/S0021-9258(18)42890-6
/ J. Biol. Chem. / Kinetic and thermodynamic parameters for tRNA binding to the ribosome and for the translocation reaction by Schilling-Bartetzko (1992)10.1073/pnas.80.14.4213
/ Proc. Natl. Acad. Sci. U. S. A. / Testing an alternative model for the ribosomal peptide elongation cycle by Rheinberger (1983)10.1074/jbc.270.35.20473
/ J. Biol. Chem. / The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor by Triana-Alonso (1995)10.1083/jcb.150.3.447
/ J. Cell. Biol. / Visualization of tRNA movements on the Escherichia coli 70S ribosome during the elongation cycle by Agrawal (2000)10.1016/j.cell.2014.04.044
/ Cell / Regulation of the mammalian elongation cycle by subunit rolling: a eukaryotic-specific ribosome rearrangement by Budkevich (2014)10.1371/journal.pone.0058829
/ PLoS One / Crystal structure of 70S ribosome with both cognate tRNAs in the E and P sites representing an authentic elongation complex by Feng (2013)10.1093/nar/gki833
/ Nucleic Acids Res. / Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu by Dinos (2005){'key': '10.1016/j.biochi.2014.12.003_bib9', 'series-title': 'Recoding: Expansion of Decoding Rules Enriches Gene Expression', 'first-page': '345', 'author': 'Pech', 'year': '2010'}
/ Recoding: Expansion of Decoding Rules Enriches Gene Expression by Pech (2010)10.1038/35018597
/ Nature / A ratchet-like inter-subunit reorganization of the ribosome during translocation by Frank (2000)10.1016/j.molcel.2007.01.027
/ Mol. Cell / Structural basis for interaction of the ribosome with the switch regions of GTP-bound elongation factors by Connell (2007)10.1016/j.molcel.2011.07.040
/ Mol. Cell / Structure and dynamics of the mammalian ribosomal pretranslocation complex by Budkevich (2011)10.1038/nature09547
/ Nature / Head swivel on the ribosome facilitates translocation by means of intra-subunit tRNA hybrid sites by Ratje (2010)10.1016/S0092-8674(03)00476-8
/ Cell / Locking and unlocking of ribosomal motions by Valle (2003)10.1016/j.molcel.2008.03.012
/ Mol. Cell / Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation by Fei (2008)10.1073/pnas.0908597107
/ Proc. Natl. Acad. Sci. U. S. A. / Spontaneous formation of the unlocked state of the ribosome is a multistep process by Munro (2010)10.1126/science.1236086
/ Science / Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation by Zhou (2013)10.1073/pnas.1320387110
/ Proc. Natl. Acad. Sci. U. S. A. / Visualization of two transfer RNAs trapped in transit during elongation factor G-mediated translocation by Ramrath (2013)10.1073/pnas.1413731111
/ Proc. Natl. Acad. Sci. U. S. A. / Molecular mechanics of 30S subunit head rotation by Mohan (2014)10.1126/science.1060612
/ Science / Recognition of cognate transfer RNA by the 30S ribosomal subunit by Ogle (2001)10.1073/pnas.73.3.804
/ Proc. Natl. Acad. Sci. U. S. A. / Sequence-specific recognition of double helical nucleic acids by proteins by Seeman (1976)10.1038/nature10913
/ Nature / A new understanding of the decoding principle on the ribosome by Demeshkina (2012)10.1016/j.jmb.2014.04.029
/ J. Mol. Biol. / Flipping of the ribosomal a-site adenines provides a basis for tRNA selection by Zeng (2014)10.1016/j.jmb.2013.02.038
/ J. Mol. Biol. / Steric complementarity in the decoding center is important for tRNA selection by the ribosome by Khade (2013)10.1038/nsmb.2140
/ Nat. Struct. Mol. Biol. / Messenger RNA interactions in the decoding center control the rate of translocation by Khade (2011)10.1038/nsmb.2869
/ Nat. Struct. Mol. Biol. / EF-G catalyzes tRNA translocation by disrupting interactions between decoding center and codon–anticodon duplex by Liu (2014)10.1016/j.molcel.2009.06.028
/ Mol. Cell / EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis by Tsuboi (2009)10.1038/nsmb.2661
/ Nat. Struct. Mol. Biol. / Translocation at work by Achenbach (2013){'year': '2014', 'series-title': '70S-Scanning Initiation, a Novel and Frequent Initiation Mode of Ribosomal Translation in Bacteria', 'author': 'Yamamoto', 'key': '10.1016/j.biochi.2014.12.003_bib29'}
/ 70S-Scanning Initiation, a Novel and Frequent Initiation Mode of Ribosomal Translation in Bacteria by Yamamoto (2014)10.1126/science.1117230
/ Science / Structures of the bacterial ribosome at 3.5 A resolution by Schuwirth (2005)10.1073/pnas.1201288109
/ Proc. Natl. Acad. Sci. U. S. A. / Structural characterization of mRNA-tRNA translocation intermediates by Agirrezabala (2012)10.1126/science.1179709
/ Science / The structure of the ribosome with elongation factor G trapped in the posttranslocational state by Gao (2009)10.1126/science.1255030
/ Science / How the ribosome hands the A-site tRNA to the P site during EF-G-catalyzed translocation by Zhou (2014)10.1038/nsmb.1790
/ Nat. Struct. Mol. Biol. / Structural aspects of messenger RNA reading frame maintenance by the ribosome by Jenner (2010)10.1038/nsmb.2645
/ Nat. Struct. Mol. Biol. / Structure of EF-G-ribosome complex in a pretranslocation state by Chen (2013)10.1126/science.1235490
/ Science / Elongation factor G bound to the ribosome in an intermediate state of translocation by Tourigny (2013)10.1073/pnas.0813180106
/ Proc. Natl. Acad. Sci. U. S. A. / Following movement of the L1 stalk between three functional states in single ribosomes by Cornish (2009)10.1111/j.1432-1033.1980.tb07222.x
/ Eur. J. Biochem. / Functional studies on ribosomes lacking protein L1 from mutant Escherichia coli by Subramanian (1980)10.1016/S0021-9258(17)44610-2
/ J. Biol. Chem. / Ribosomal protein L1 from Escherichia coli. Its role in the binding of tRNA to the ribosome and in elongation factor G-dependent GTP hydrolysis by Sander (1983)10.1038/385037a0
/ Nature / Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome by Rodnina (1997)10.1016/j.jmb.2004.08.097
/ J. Mol. Biol. / Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation by Peske (2004)10.1126/science.1084571
/ Science / Catalysis of ribosomal translocation by sparsomycin by Fredrick (2003)10.1038/349117a0
/ Nature / The GTPase superfamily: conserved structure and molecular mechanism by Bourne (1991)10.1016/S0092-8674(03)00478-1
/ Cell / Peptidyl-tRNA regulates the GTPase activity of translational factors by Zavialov (2003)10.1016/j.molcel.2007.01.014
/ Mol. Cell / Kinetically competent intermediates in the translocation step of protein synthesis by Pan (2007)10.1021/cb8002946
/ ACS Chem. Biol. / Ribosomal translocation: one step closer to the molecular mechanism by Shoji (2009)10.1038/365126a0
/ Nature / Crystal structure of active elongation factor Tu reveals major domain rearrangements by Berchtold (1993)10.1016/S0021-9258(18)34241-8
/ J. Biol. Chem. / The site of action of alpha-sarcin on eukaryotic ribosomes. The sequence at the alpha-sarcin cleavage site in 28 S ribosomal ribonucleic acid by Endo (1982)10.1016/0300-9084(87)90225-2
/ Biochimie / Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors by Hausner (1987)10.4161/rna.7.5.12467
/ RNA Biol. / Ribosome-associated GTPases: the role of RNA for GTPase activation by Clementi (2010)10.1126/science.1194460
/ Science / The mechanism for activation of GTP hydrolysis on the ribosome by Voorhees (2010)10.1126/science.1235970
/ Science / Control of ribosomal subunit rotation by elongation factor G by Pulk (2013)10.1261/rna.031187.111
/ Rna / Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome by Zhou (2012)10.1073/pnas.1311423110
/ Proc. Natl. Acad. Sci. U. S. A. / Structure of the ribosome with elongation factor G trapped in the pretranslocation state by Brilot (2013)10.1016/0006-291X(69)90934-6
/ Biochem. Biophys. Res. Commun. / Formation of the ribosome-G factor-GDP complex in the presence of fusidic acid by Bodley (1969)10.1002/j.1460-2075.1994.tb06676.x
/ EMBO J. / Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus by Ævarsson (1994)10.3109/10409230903307311
/ Crit. Rev. Biochem. Mol. Biol. / The A–Z of bacterial translation inhibitors by Wilson (2009)10.1038/nsmb1243
/ Nat. Struct. Mol. Biol. / The antibiotic viomycin traps the ribosome in an intermediate state of translocation by Ermolenko (2007)
Dates
Type | When |
---|---|
Created | 10 years, 8 months ago (Dec. 13, 2014, 2:03 a.m.) |
Deposited | 3 years, 4 months ago (April 24, 2022, 6:55 a.m.) |
Indexed | 3 months, 3 weeks ago (May 13, 2025, 1:09 p.m.) |
Issued | 10 years, 2 months ago (July 1, 2015) |
Published | 10 years, 2 months ago (July 1, 2015) |
Published Print | 10 years, 2 months ago (July 1, 2015) |
Funders
1
Charité – Universitätsmedizin Berlin, Germany
10.13039/501100002839
Charité – Universitätsmedizin BerlinRegion: Europe
pri (For-profit companies (industry))
Labels
1
- Medical School - Charité - University Medicine Berlin
@article{Achenbach_2015, title={The mechanics of ribosomal translocation}, volume={114}, ISSN={0300-9084}, url={http://dx.doi.org/10.1016/j.biochi.2014.12.003}, DOI={10.1016/j.biochi.2014.12.003}, journal={Biochimie}, publisher={Elsevier BV}, author={Achenbach, John and Nierhaus, Knud H.}, year={2015}, month=jul, pages={80–89} }