-
1
-
-
26944435515
-
Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation
-
Algire M.A., Maag D., Lorsch J.R. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 2005, 20:251-262.
-
(2005)
Mol. Cell
, vol.20
, pp. 251-262
-
-
Algire, M.A.1
Maag, D.2
Lorsch, J.R.3
-
2
-
-
0034307347
-
A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate invivo
-
Asano K., Clayton J., Shalev A., Hinnebusch A.G. A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate invivo. Genes Dev. 2000, 14:2534-2546.
-
(2000)
Genes Dev.
, vol.14
, pp. 2534-2546
-
-
Asano, K.1
Clayton, J.2
Shalev, A.3
Hinnebusch, A.G.4
-
3
-
-
84924262489
-
Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex
-
Aylett C.H., Boehringer D., Erzberger J.P., Schaefer T., Ban N. Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex. Nat. Struct. Mol. Biol. 2015, 22:269-271.
-
(2015)
Nat. Struct. Mol. Biol.
, vol.22
, pp. 269-271
-
-
Aylett, C.H.1
Boehringer, D.2
Erzberger, J.P.3
Schaefer, T.4
Ban, N.5
-
4
-
-
84878580683
-
Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles
-
Bai X.C., Fernandez I.S., McMullan G., Scheres S.H. Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. Elife 2013, 2:e00461.
-
(2013)
Elife
, vol.2
, pp. e00461
-
-
Bai, X.C.1
Fernandez, I.S.2
McMullan, G.3
Scheres, S.H.4
-
5
-
-
83855162728
-
The structure of the eukaryotic ribosome at 3.0Å resolution
-
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G., Yusupov M. The structure of the eukaryotic ribosome at 3.0Å resolution. Science 2011, 334:1524-1529.
-
(2011)
Science
, vol.334
, pp. 1524-1529
-
-
Ben-Shem, A.1
Garreau de Loubresse, N.2
Melnikov, S.3
Jenner, L.4
Yusupova, G.5
Yusupov, M.6
-
6
-
-
84921777915
-
Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
-
Brown A., Long F., Nicholls R.A., Toots J., Emsley P., Murshudov G. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D Biol. Crystallogr. 2015, 71:136-153.
-
(2015)
Acta Crystallogr. D Biol. Crystallogr.
, vol.71
, pp. 136-153
-
-
Brown, A.1
Long, F.2
Nicholls, R.A.3
Toots, J.4
Emsley, P.5
Murshudov, G.6
-
7
-
-
77956713468
-
The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons
-
Chiu W.L., Wagner S., Herrmannová A., Burela L., Zhang F., Saini A.K., Valásek L., Hinnebusch A.G. The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol. Cell. Biol. 2010, 30:4415-4434.
-
(2010)
Mol. Cell. Biol.
, vol.30
, pp. 4415-4434
-
-
Chiu, W.L.1
Wagner, S.2
Herrmannová, A.3
Burela, L.4
Zhang, F.5
Saini, A.K.6
Valásek, L.7
Hinnebusch, A.G.8
-
8
-
-
77956657467
-
The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning
-
Cuchalová L., Kouba T., Herrmannová A., Dányi I., Chiu W.L., Valásek L. The RNA recognition motif of eukaryotic translation initiation factor 3g (eIF3g) is required for resumption of scanning of posttermination ribosomes for reinitiation on GCN4 and together with eIF3i stimulates linear scanning. Mol. Cell. Biol. 2010, 30:4671-4686.
-
(2010)
Mol. Cell. Biol.
, vol.30
, pp. 4671-4686
-
-
Cuchalová, L.1
Kouba, T.2
Herrmannová, A.3
Dányi, I.4
Chiu, W.L.5
Valásek, L.6
-
9
-
-
66149112273
-
The PyMOL Molecular Graphics System
-
DeLano, W.L. (2006). The PyMOL Molecular Graphics System. http://www.pymol.org.
-
(2006)
-
-
DeLano, W.L.1
-
10
-
-
0024297814
-
Mutations at a Zn(II) finger motif in the yeast eIF-2 beta gene alter ribosomal start-site selection during the scanning process
-
Donahue T.F., Cigan A.M., Pabich E.K., Valavicius B.C. Mutations at a Zn(II) finger motif in the yeast eIF-2 beta gene alter ribosomal start-site selection during the scanning process. Cell 1988, 54:621-632.
-
(1988)
Cell
, vol.54
, pp. 621-632
-
-
Donahue, T.F.1
Cigan, A.M.2
Pabich, E.K.3
Valavicius, B.C.4
-
11
-
-
50049130690
-
Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNA(Met) and AUG selection
-
Dong J., Nanda J.S., Rahman H., Pruitt M.R., Shin B.S., Wong C.M., Lorsch J.R., Hinnebusch A.G. Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNA(Met) and AUG selection. Genes Dev. 2008, 22:2242-2255.
-
(2008)
Genes Dev.
, vol.22
, pp. 2242-2255
-
-
Dong, J.1
Nanda, J.S.2
Rahman, H.3
Pruitt, M.R.4
Shin, B.S.5
Wong, C.M.6
Lorsch, J.R.7
Hinnebusch, A.G.8
-
12
-
-
84884809999
-
Spectrin domain of eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex
-
Dong Z., Qi J., Peng H., Liu J., Zhang J.T. Spectrin domain of eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex. J.Biol. Chem. 2013, 288:27951-27959.
-
(2013)
J.Biol. Chem.
, vol.288
, pp. 27951-27959
-
-
Dong, Z.1
Qi, J.2
Peng, H.3
Liu, J.4
Zhang, J.T.5
-
13
-
-
84896812774
-
Conserved residues in yeast initiator tRNA calibrate initiation accuracy by regulating preinitiation complex stability at the start codon
-
Dong J., Munoz A., Kolitz S.E., Saini A.K., Chiu W.L., Rahman H., Lorsch J.R., Hinnebusch A.G. Conserved residues in yeast initiator tRNA calibrate initiation accuracy by regulating preinitiation complex stability at the start codon. Genes Dev. 2014, 28:502-520.
-
(2014)
Genes Dev.
, vol.28
, pp. 502-520
-
-
Dong, J.1
Munoz, A.2
Kolitz, S.E.3
Saini, A.K.4
Chiu, W.L.5
Rahman, H.6
Lorsch, J.R.7
Hinnebusch, A.G.8
-
14
-
-
77949535720
-
Features and development of Coot
-
Emsley P., Lohkamp B., Scott W.G., Cowtan K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 2010, 66:486-501.
-
(2010)
Acta Crystallogr. D Biol. Crystallogr.
, vol.66
, pp. 486-501
-
-
Emsley, P.1
Lohkamp, B.2
Scott, W.G.3
Cowtan, K.4
-
15
-
-
84907323467
-
Molecular architecture of the 40S{dot operator}eIF1{dot operator}eIF3 translation initiation complex
-
Erzberger J.P., Stengel F., Pellarin R., Zhang S., Schaefer T., Aylett C.H., Cimermančič P., Boehringer D., Sali A., Aebersold R., Ban N. Molecular architecture of the 40S{dot operator}eIF1{dot operator}eIF3 translation initiation complex. Cell 2014, 158:1123-1135.
-
(2014)
Cell
, vol.158
, pp. 1123-1135
-
-
Erzberger, J.P.1
Stengel, F.2
Pellarin, R.3
Zhang, S.4
Schaefer, T.5
Aylett, C.H.6
Cimermančič, P.7
Boehringer, D.8
Sali, A.9
Aebersold, R.10
Ban, N.11
-
16
-
-
0033522507
-
Structure and interactions of the translation initiation factor eIF1
-
Fletcher C.M., Pestova T.V., Hellen C.U., Wagner G. Structure and interactions of the translation initiation factor eIF1. EMBO J. 1999, 18:2631-2637.
-
(1999)
EMBO J.
, vol.18
, pp. 2631-2637
-
-
Fletcher, C.M.1
Pestova, T.V.2
Hellen, C.U.3
Wagner, G.4
-
17
-
-
84878333225
-
Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29
-
Hashem Y., des Georges A., Dhote V., Langlois R., Liao H.Y., Grassucci R.A., Hellen C.U., Pestova T.V., Frank J. Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29. Cell 2013, 153:1108-1119.
-
(2013)
Cell
, vol.153
, pp. 1108-1119
-
-
Hashem, Y.1
des Georges, A.2
Dhote, V.3
Langlois, R.4
Liao, H.Y.5
Grassucci, R.A.6
Hellen, C.U.7
Pestova, T.V.8
Frank, J.9
-
18
-
-
84863338242
-
Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly
-
Herrmannová A., Daujotyte D., Yang J.C., Cuchalová L., Gorrec F., Wagner S., Dányi I., Lukavsky P.J., Valásek L.S. Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly. Nucleic Acids Res. 2012, 40:2294-2311.
-
(2012)
Nucleic Acids Res.
, vol.40
, pp. 2294-2311
-
-
Herrmannová, A.1
Daujotyte, D.2
Yang, J.C.3
Cuchalová, L.4
Gorrec, F.5
Wagner, S.6
Dányi, I.7
Lukavsky, P.J.8
Valásek, L.S.9
-
19
-
-
27144510561
-
Translational regulation of GCN4 and the general amino acid control of yeast
-
Hinnebusch A.G. Translational regulation of GCN4 and the general amino acid control of yeast. Annu. Rev. Microbiol. 2005, 59:407-450.
-
(2005)
Annu. Rev. Microbiol.
, vol.59
, pp. 407-450
-
-
Hinnebusch, A.G.1
-
20
-
-
33748924333
-
EIF3: a versatile scaffold for translation initiation complexes
-
Hinnebusch A.G. eIF3: a versatile scaffold for translation initiation complexes. Trends Biochem. Sci. 2006, 31:553-562.
-
(2006)
Trends Biochem. Sci.
, vol.31
, pp. 553-562
-
-
Hinnebusch, A.G.1
-
21
-
-
84902193122
-
The scanning mechanism of eukaryotic translation initiation
-
Hinnebusch A.G. The scanning mechanism of eukaryotic translation initiation. Annu. Rev. Biochem. 2014, 83:779-812.
-
(2014)
Annu. Rev. Biochem.
, vol.83
, pp. 779-812
-
-
Hinnebusch, A.G.1
-
22
-
-
84863889691
-
The mechanism of eukaryotic translation initiation: new insights and challenges
-
Hinnebusch A.G., Lorsch J.R. The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb. Perspect. Biol. 2012, 4. 10.1101/cshperspect.a011544.
-
(2012)
Cold Spring Harb. Perspect. Biol.
, vol.4
-
-
Hinnebusch, A.G.1
Lorsch, J.R.2
-
23
-
-
84908332647
-
Structural changes enable start codon recognition by the eukaryotic translation initiation complex
-
Hussain T., Llacer J.L., Fernandez I.S., Munoz A., Martin-Marcos P., Savva C.G., Lorsch J.R., Hinnebusch A.G., Ramakrishnan V. Structural changes enable start codon recognition by the eukaryotic translation initiation complex. Cell 2014, 159:597-607.
-
(2014)
Cell
, vol.159
, pp. 597-607
-
-
Hussain, T.1
Llacer, J.L.2
Fernandez, I.S.3
Munoz, A.4
Martin-Marcos, P.5
Savva, C.G.6
Lorsch, J.R.7
Hinnebusch, A.G.8
Ramakrishnan, V.9
-
24
-
-
75149196287
-
The mechanism of eukaryotic translation initiation and principles of its regulation
-
Jackson R.J., Hellen C.U., Pestova T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol. 2010, 11:113-127.
-
(2010)
Nat. Rev. Mol. Cell Biol.
, vol.11
, pp. 113-127
-
-
Jackson, R.J.1
Hellen, C.U.2
Pestova, T.V.3
-
25
-
-
84865259445
-
Functional characterization of the role of the N-terminal domain of the c/Nip1 subunit of eukaryotic initiation factor 3 (eIF3) in AUG recognition
-
Karásková M., Gunišová S., Herrmannová A., Wagner S., Munzarová V., Valášek L. Functional characterization of the role of the N-terminal domain of the c/Nip1 subunit of eukaryotic initiation factor 3 (eIF3) in AUG recognition. J.Biol. Chem. 2012, 287:28420-28434.
-
(2012)
J.Biol. Chem.
, vol.287
, pp. 28420-28434
-
-
Karásková, M.1
Gunišová, S.2
Herrmannová, A.3
Wagner, S.4
Munzarová, V.5
Valášek, L.6
-
26
-
-
84894623755
-
Quantifying the local resolution of cryo-EM density maps
-
Kucukelbir A., Sigworth F.J., Tagare H.D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 2014, 11:63-65.
-
(2014)
Nat. Methods
, vol.11
, pp. 63-65
-
-
Kucukelbir, A.1
Sigworth, F.J.2
Tagare, H.D.3
-
27
-
-
84881666192
-
The initiation of mammalian protein synthesis and mRNA scanning mechanism
-
Lomakin I.B., Steitz T.A. The initiation of mammalian protein synthesis and mRNA scanning mechanism. Nature 2013, 500:307-311.
-
(2013)
Nature
, vol.500
, pp. 307-311
-
-
Lomakin, I.B.1
Steitz, T.A.2
-
28
-
-
31344481752
-
Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection
-
Maag D., Algire M.A., Lorsch J.R. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. J.Mol. Biol. 2006, 356:724-737.
-
(2006)
J.Mol. Biol.
, vol.356
, pp. 724-737
-
-
Maag, D.1
Algire, M.A.2
Lorsch, J.R.3
-
29
-
-
83255187893
-
Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons
-
Martin-Marcos P., Cheung Y.N., Hinnebusch A.G. Functional elements in initiation factors 1, 1A, and 2β discriminate against poor AUG context and non-AUG start codons. Mol. Cell. Biol. 2011, 31:4814-4831.
-
(2011)
Mol. Cell. Biol.
, vol.31
, pp. 4814-4831
-
-
Martin-Marcos, P.1
Cheung, Y.N.2
Hinnebusch, A.G.3
-
30
-
-
84892748582
-
Enhanced eIF1 binding to the 40S ribosome impedes conformational rearrangements of the preinitiation complex and elevates initiation accuracy
-
Martin-Marcos P., Nanda J.S., Luna R.E., Zhang F., Saini A.K., Cherkasova V.A., Wagner G., Lorsch J.R., Hinnebusch A.G. Enhanced eIF1 binding to the 40S ribosome impedes conformational rearrangements of the preinitiation complex and elevates initiation accuracy. RNA 2014, 20:150-167.
-
(2014)
RNA
, vol.20
, pp. 150-167
-
-
Martin-Marcos, P.1
Nanda, J.S.2
Luna, R.E.3
Zhang, F.4
Saini, A.K.5
Cherkasova, V.A.6
Wagner, G.7
Lorsch, J.R.8
Hinnebusch, A.G.9
-
31
-
-
0038441501
-
Accurate determination of local defocus and specimen tilt in electron microscopy
-
Mindell J.A., Grigorieff N. Accurate determination of local defocus and specimen tilt in electron microscopy. J.Struct. Biol. 2003, 142:334-347.
-
(2003)
J.Struct. Biol.
, vol.142
, pp. 334-347
-
-
Mindell, J.A.1
Grigorieff, N.2
-
32
-
-
84874310624
-
Coordinated movements of eukaryotic translation initiation factors eIF1, eIF1A, and eIF5 trigger phosphate release from eIF2 in response to start codon recognition by the ribosomal preinitiation complex
-
Nanda J.S., Saini A.K., Muñoz A.M., Hinnebusch A.G., Lorsch J.R. Coordinated movements of eukaryotic translation initiation factors eIF1, eIF1A, and eIF5 trigger phosphate release from eIF2 in response to start codon recognition by the ribosomal preinitiation complex. J.Biol. Chem. 2013, 288:5316-5329.
-
(2013)
J.Biol. Chem.
, vol.288
, pp. 5316-5329
-
-
Nanda, J.S.1
Saini, A.K.2
Muñoz, A.M.3
Hinnebusch, A.G.4
Lorsch, J.R.5
-
33
-
-
34047263278
-
The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome
-
Passmore L.A., Schmeing T.M., Maag D., Applefield D.J., Acker M.G., Algire M.A., Lorsch J.R., Ramakrishnan V. The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol. Cell 2007, 26:41-50.
-
(2007)
Mol. Cell
, vol.26
, pp. 41-50
-
-
Passmore, L.A.1
Schmeing, T.M.2
Maag, D.3
Applefield, D.J.4
Acker, M.G.5
Algire, M.A.6
Lorsch, J.R.7
Ramakrishnan, V.8
-
34
-
-
0037112055
-
The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
-
Pestova T.V., Kolupaeva V.G. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection. Genes Dev. 2002, 16:2906-2922.
-
(2002)
Genes Dev.
, vol.16
, pp. 2906-2922
-
-
Pestova, T.V.1
Kolupaeva, V.G.2
-
35
-
-
0032572776
-
Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
-
Pestova T.V., Borukhov S.I., Hellen C.U. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature 1998, 394:854-859.
-
(1998)
Nature
, vol.394
, pp. 854-859
-
-
Pestova, T.V.1
Borukhov, S.I.2
Hellen, C.U.3
-
36
-
-
4444221565
-
UCSF Chimera-a visualization system for exploratory research and analysis
-
Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., Ferrin T.E. UCSF Chimera-a visualization system for exploratory research and analysis. J.Comput. Chem. 2004, 25:1605-1612.
-
(2004)
J.Comput. Chem.
, vol.25
, pp. 1605-1612
-
-
Pettersen, E.F.1
Goddard, T.D.2
Huang, C.C.3
Couch, G.S.4
Greenblatt, D.M.5
Meng, E.C.6
Ferrin, T.E.7
-
37
-
-
44649095899
-
Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
-
Pisarev A.V., Kolupaeva V.G., Yusupov M.M., Hellen C.U., Pestova T.V. Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes. EMBO J. 2008, 27:1609-1621.
-
(2008)
EMBO J.
, vol.27
, pp. 1609-1621
-
-
Pisarev, A.V.1
Kolupaeva, V.G.2
Yusupov, M.M.3
Hellen, C.U.4
Pestova, T.V.5
-
38
-
-
79951510534
-
Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
-
Rabl J., Leibundgut M., Ataide S.F., Haag A., Ban N. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 2011, 331:730-736.
-
(2011)
Science
, vol.331
, pp. 730-736
-
-
Rabl, J.1
Leibundgut, M.2
Ataide, S.F.3
Haag, A.4
Ban, N.5
-
39
-
-
38149140938
-
Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection
-
Reibarkh M., Yamamoto Y., Singh C.R., del Rio F., Fahmy A., Lee B., Luna R.E., Ii M., Wagner G., Asano K. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J.Biol. Chem. 2008, 283:1094-1103.
-
(2008)
J.Biol. Chem.
, vol.283
, pp. 1094-1103
-
-
Reibarkh, M.1
Yamamoto, Y.2
Singh, C.R.3
del Rio, F.4
Fahmy, A.5
Lee, B.6
Luna, R.E.7
Ii, M.8
Wagner, G.9
Asano, K.10
-
40
-
-
0142042865
-
Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
-
Rosenthal P.B., Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J.Mol. Biol. 2003, 333:721-745.
-
(2003)
J.Mol. Biol.
, vol.333
, pp. 721-745
-
-
Rosenthal, P.B.1
Henderson, R.2
-
41
-
-
84868444740
-
RELION: implementation of a Bayesian approach to cryo-EM structure determination
-
Scheres S.H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J.Struct. Biol. 2012, 180:519-530.
-
(2012)
J.Struct. Biol.
, vol.180
, pp. 519-530
-
-
Scheres, S.H.1
-
42
-
-
84866078359
-
Prevention of overfitting in cryo-EM structure determination
-
Scheres S.H., Chen S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 2012, 9:853-854.
-
(2012)
Nat. Methods
, vol.9
, pp. 853-854
-
-
Scheres, S.H.1
Chen, S.2
-
43
-
-
28544439977
-
Structural roles for human translation factor eIF3 in initiation of protein synthesis
-
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E. Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 2005, 310:1513-1515.
-
(2005)
Science
, vol.310
, pp. 1513-1515
-
-
Siridechadilok, B.1
Fraser, C.S.2
Hall, R.J.3
Doudna, J.A.4
Nogales, E.5
-
44
-
-
33748350921
-
Structure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 region
-
Sokabe M., Yao M., Sakai N., Toya S., Tanaka I. Structure of archaeal translational initiation factor 2 betagamma-GDP reveals significant conformational change of the beta-subunit and switch 1 region. Proc. Natl. Acad. Sci. USA 2006, 103:13016-13021.
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 13016-13021
-
-
Sokabe, M.1
Yao, M.2
Sakai, N.3
Toya, S.4
Tanaka, I.5
-
45
-
-
50149109434
-
Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits
-
Stolboushkina E., Nikonov S., Nikulin A., Bläsi U., Manstein D.J., Fedorov R., Garber M., Nikonov O. Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits. J.Mol. Biol. 2008, 382:680-691.
-
(2008)
J.Mol. Biol.
, vol.382
, pp. 680-691
-
-
Stolboushkina, E.1
Nikonov, S.2
Nikulin, A.3
Bläsi, U.4
Manstein, D.J.5
Fedorov, R.6
Garber, M.7
Nikonov, O.8
-
46
-
-
84863624560
-
'Ribozoomin'-translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs)
-
Valásek L.S. 'Ribozoomin'-translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs). Curr. Protein Pept. Sci. 2012, 13:305-330.
-
(2012)
Curr. Protein Pept. Sci.
, vol.13
, pp. 305-330
-
-
Valásek, L.S.1
-
47
-
-
0036846237
-
Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation invivo
-
Valásek L., Nielsen K.H., Hinnebusch A.G. Direct eIF2-eIF3 contact in the multifactor complex is important for translation initiation invivo. EMBO J. 2002, 21:5886-5898.
-
(2002)
EMBO J.
, vol.21
, pp. 5886-5898
-
-
Valásek, L.1
Nielsen, K.H.2
Hinnebusch, A.G.3
-
48
-
-
0037444342
-
The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome invivo
-
Valásek L., Mathew A.A., Shin B.S., Nielsen K.H., Szamecz B., Hinnebusch A.G. The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome invivo. Genes Dev. 2003, 17:786-799.
-
(2003)
Genes Dev.
, vol.17
, pp. 786-799
-
-
Valásek, L.1
Mathew, A.A.2
Shin, B.S.3
Nielsen, K.H.4
Szamecz, B.5
Hinnebusch, A.G.6
-
49
-
-
6344291066
-
Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection
-
Valásek L., Nielsen K.H., Zhang F., Fekete C.A., Hinnebusch A.G. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol. Cell. Biol. 2004, 24:9437-9455.
-
(2004)
Mol. Cell. Biol.
, vol.24
, pp. 9437-9455
-
-
Valásek, L.1
Nielsen, K.H.2
Zhang, F.3
Fekete, C.A.4
Hinnebusch, A.G.5
-
50
-
-
84870391186
-
Structural insights into eukaryotic ribosomes and the initiation of translation
-
Voigts-Hoffmann F., Klinge S., Ban N. Structural insights into eukaryotic ribosomes and the initiation of translation. Curr. Opin. Struct. Biol. 2012, 22:768-777.
-
(2012)
Curr. Opin. Struct. Biol.
, vol.22
, pp. 768-777
-
-
Voigts-Hoffmann, F.1
Klinge, S.2
Ban, N.3
-
51
-
-
84881474410
-
The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A
-
Weisser M., Voigts-Hoffmann F., Rabl J., Leibundgut M., Ban N. The crystal structure of the eukaryotic 40S ribosomal subunit in complex with eIF1 and eIF1A. Nat. Struct. Mol. Biol. 2013, 20:1015-1017.
-
(2013)
Nat. Struct. Mol. Biol.
, vol.20
, pp. 1015-1017
-
-
Weisser, M.1
Voigts-Hoffmann, F.2
Rabl, J.3
Leibundgut, M.4
Ban, N.5
-
52
-
-
36749037829
-
Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states
-
Yatime L., Mechulam Y., Blanquet S., Schmitt E. Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states. Proc. Natl. Acad. Sci. USA 2007, 104:18445-18450.
-
(2007)
Proc. Natl. Acad. Sci. USA
, vol.104
, pp. 18445-18450
-
-
Yatime, L.1
Mechulam, Y.2
Blanquet, S.3
Schmitt, E.4
-
53
-
-
69849092725
-
Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing
-
Yu Y., Marintchev A., Kolupaeva V.G., Unbehaun A., Veryasova T., Lai S.C., Hong P., Wagner G., Hellen C.U., Pestova T.V. Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing. Nucleic Acids Res. 2009, 37:5167-5182.
-
(2009)
Nucleic Acids Res.
, vol.37
, pp. 5167-5182
-
-
Yu, Y.1
Marintchev, A.2
Kolupaeva, V.G.3
Unbehaun, A.4
Veryasova, T.5
Lai, S.C.6
Hong, P.7
Wagner, G.8
Hellen, C.U.9
Pestova, T.V.10
-
54
-
-
84941027177
-
Conformational changes in the P site and mRNA entry channel evoked by AUG recognition in yeast translation preinitiation complexes
-
Zhang F., Saini A.K., Shin B.S., Nanda J., Hinnebusch A.G. Conformational changes in the P site and mRNA entry channel evoked by AUG recognition in yeast translation preinitiation complexes. Nucleic Acids Res. 2015, 43:2293-2312.
-
(2015)
Nucleic Acids Res.
, vol.43
, pp. 2293-2312
-
-
Zhang, F.1
Saini, A.K.2
Shin, B.S.3
Nanda, J.4
Hinnebusch, A.G.5
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