-
1
-
-
0033578701
-
Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
-
Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., and Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell 98 (1999) 811-824
-
(1999)
Cell
, vol.98
, pp. 811-824
-
-
Zhang, G.1
Campbell, E.A.2
Minakhin, L.3
Richter, C.4
Severinov, K.5
Darst, S.A.6
-
2
-
-
0035827346
-
Structural basis of transcription: RNA polymerase II at 2.8 Ångstrom resolution
-
Cramer P., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: RNA polymerase II at 2.8 Ångstrom resolution. Science 292 (2001) 1863-1876
-
(2001)
Science
, vol.292
, pp. 1863-1876
-
-
Cramer, P.1
Bushnell, D.A.2
Kornberg, R.D.3
-
3
-
-
0035827332
-
Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution
-
Gnatt A.L., Cramer P., Fu J., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: an RNA polymerase II elongation complex at 3.3 Å resolution. Science 292 (2001) 1876-1882
-
(2001)
Science
, vol.292
, pp. 1876-1882
-
-
Gnatt, A.L.1
Cramer, P.2
Fu, J.3
Bushnell, D.A.4
Kornberg, R.D.5
-
5
-
-
10944232674
-
Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS
-
Kettenberger H., Armache K.-J., and Cramer P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol Cell 16 (2004) 955-965
-
(2004)
Mol Cell
, vol.16
, pp. 955-965
-
-
Kettenberger, H.1
Armache, K.-J.2
Cramer, P.3
-
6
-
-
33645119890
-
Structural perspective on mutations affecting the function of multisubunit RNA polymerases
-
Trinh V., Langelier M.-F., Archambault J., and Coulombe B. Structural perspective on mutations affecting the function of multisubunit RNA polymerases. Microbiol Mol Biol Rev 70 (2006) 12-36
-
(2006)
Microbiol Mol Biol Rev
, vol.70
, pp. 12-36
-
-
Trinh, V.1
Langelier, M.-F.2
Archambault, J.3
Coulombe, B.4
-
7
-
-
0034691146
-
Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals
-
Artsimovitch I., and Landick R. Pausing by bacterial RNA polymerase is mediated by mechanistically distinct classes of signals. Proc Natl Acad Sci USA 97 (2000) 7090-7095
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 7090-7095
-
-
Artsimovitch, I.1
Landick, R.2
-
8
-
-
0031059249
-
Transcriptional arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3′-end of the RNA intact and extruded
-
Komissarova N., and Kashlev M. Transcriptional arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3′-end of the RNA intact and extruded. Proc Natl Acad Sci USA 94 (1997) 1755-1760
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 1755-1760
-
-
Komissarova, N.1
Kashlev, M.2
-
9
-
-
0031552174
-
The RNA-DNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase
-
Nudler E., Mustaev A., Lukhtanov E., and Goldfarb A. The RNA-DNA hybrid maintains the register of transcription by preventing backtracking of RNA polymerase. Cell 89 (1997) 33-41
-
(1997)
Cell
, vol.89
, pp. 33-41
-
-
Nudler, E.1
Mustaev, A.2
Lukhtanov, E.3
Goldfarb, A.4
-
10
-
-
0030584091
-
Promoter proximal sequences modulate RNA polymerase II elongation by a novel mechanism
-
Reeder T.C., and Hawley D.K. Promoter proximal sequences modulate RNA polymerase II elongation by a novel mechanism. Cell 87 (1996) 767-777
-
(1996)
Cell
, vol.87
, pp. 767-777
-
-
Reeder, T.C.1
Hawley, D.K.2
-
11
-
-
0043244877
-
Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase
-
Opalka N., Chlenov M., Chacon P., Rice W.J., Wriggers W., and Darst S.A. Structure and function of the transcription elongation factor GreB bound to bacterial RNA polymerase. Cell 114 (2003) 335-345
-
(2003)
Cell
, vol.114
, pp. 335-345
-
-
Opalka, N.1
Chlenov, M.2
Chacon, P.3
Rice, W.J.4
Wriggers, W.5
Darst, S.A.6
-
12
-
-
4043108470
-
Regulation through the secondary channel-structural framework for ppGpp-DksA synergism during transcription
-
Perederina A., Svetlov V., Vassylyeva M.N., Tahirov T.H., Yokoyama S., Artsimovitch I., and Vassylyev D.G. Regulation through the secondary channel-structural framework for ppGpp-DksA synergism during transcription. Cell 118 (2004) 297-309
-
(2004)
Cell
, vol.118
, pp. 297-309
-
-
Perederina, A.1
Svetlov, V.2
Vassylyeva, M.N.3
Tahirov, T.H.4
Yokoyama, S.5
Artsimovitch, I.6
Vassylyev, D.G.7
-
13
-
-
0347994909
-
Donation of catalytic residues to RNA polymerase active center by transcription factor Gre
-
Sosunova E., Sosunov V., Kozlov M., Nikiforov V., Goldfarb A., and Mustaev A. Donation of catalytic residues to RNA polymerase active center by transcription factor Gre. Proc Natl Acad Sci USA 100 (2003) 15469-15474
-
(2003)
Proc Natl Acad Sci USA
, vol.100
, pp. 15469-15474
-
-
Sosunova, E.1
Sosunov, V.2
Kozlov, M.3
Nikiforov, V.4
Goldfarb, A.5
Mustaev, A.6
-
14
-
-
66349138227
-
Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution
-
Wang D., Bushnell D.A., Huang X., Westover K.D., Levitt M., and Kornberg R.D. Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution. Science 324 (2009) 1203-1206
-
(2009)
Science
, vol.324
, pp. 1203-1206
-
-
Wang, D.1
Bushnell, D.A.2
Huang, X.3
Westover, K.D.4
Levitt, M.5
Kornberg, R.D.6
-
15
-
-
10644237908
-
Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center
-
Batada N.N., Westover K.D., Bushnell D.A., Levitt M., and Kornberg R.D. Diffusion of nucleoside triphosphates and role of the entry site to the RNA polymerase II active center. Proc Natl Acad Sci USA 101 (2004) 17361-17364
-
(2004)
Proc Natl Acad Sci USA
, vol.101
, pp. 17361-17364
-
-
Batada, N.N.1
Westover, K.D.2
Bushnell, D.A.3
Levitt, M.4
Kornberg, R.D.5
-
16
-
-
27944496101
-
NTP-entry routes in multi-subunit RNA polymerases
-
Landick R. NTP-entry routes in multi-subunit RNA polymerases. Trends Biochem Sci 30 (2005) 651-654
-
(2005)
Trends Biochem Sci
, vol.30
, pp. 651-654
-
-
Landick, R.1
-
17
-
-
34447513771
-
Structural basis for substrate loading in bacterial rna polymerase
-
This paper presents the first structure of an elongation complex for a bacterial RNAP. The authors observed important conformational changes in the trigger loop, fork loop 2, and β-pincer. These conformational changes have lead to the suggestion that the synchronized movements of these structures are involved in translocation and nucleotide loading.
-
Vassylyev D.G., Vassylyeva M.N., Zhang J., Palangat M., Artsimovitch I., and Landick R. Structural basis for substrate loading in bacterial rna polymerase. Nature 448 (2007) 163-168. This paper presents the first structure of an elongation complex for a bacterial RNAP. The authors observed important conformational changes in the trigger loop, fork loop 2, and β-pincer. These conformational changes have lead to the suggestion that the synchronized movements of these structures are involved in translocation and nucleotide loading.
-
(2007)
Nature
, vol.448
, pp. 163-168
-
-
Vassylyev, D.G.1
Vassylyeva, M.N.2
Zhang, J.3
Palangat, M.4
Artsimovitch, I.5
Landick, R.6
-
18
-
-
33751235874
-
Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis
-
This paper was the first to show that the trigger loop was able to adopt multiple conformations and provided the structural basis for the trigger loop centric models for nucleotide incorporation.
-
Wang D., Bushnell D.A., Westover K.D., Kaplan C.D., and Kornberg R.D. Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis. Cell 127 (2006) 941-954. This paper was the first to show that the trigger loop was able to adopt multiple conformations and provided the structural basis for the trigger loop centric models for nucleotide incorporation.
-
(2006)
Cell
, vol.127
, pp. 941-954
-
-
Wang, D.1
Bushnell, D.A.2
Westover, K.D.3
Kaplan, C.D.4
Kornberg, R.D.5
-
19
-
-
44449103640
-
The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by α-amanitin
-
Kaplan C.D., Larsson K.-M., and Kornberg R.D. The RNA polymerase II trigger loop functions in substrate selection and is directly targeted by α-amanitin. Mol Cell 30 (2008) 547-556
-
(2008)
Mol Cell
, vol.30
, pp. 547-556
-
-
Kaplan, C.D.1
Larsson, K.-M.2
Kornberg, R.D.3
-
20
-
-
49449102926
-
Structural basis of transcription inhibition by α-amanitin and implications for RNA polymerase II translocation
-
Brueckner F., and Cramer P. Structural basis of transcription inhibition by α-amanitin and implications for RNA polymerase II translocation. Nat Struct Mol Biol 15 (2008) 811-818
-
(2008)
Nat Struct Mol Biol
, vol.15
, pp. 811-818
-
-
Brueckner, F.1
Cramer, P.2
-
21
-
-
66549126163
-
A movie of the RNA polymerase nucleotide addition cycle
-
Brueckner F., Ortiz J., and Cramer P. A movie of the RNA polymerase nucleotide addition cycle. Curr Opin Struct Biol 19 (2009) 294-299
-
(2009)
Curr Opin Struct Biol
, vol.19
, pp. 294-299
-
-
Brueckner, F.1
Ortiz, J.2
Cramer, P.3
-
22
-
-
4444228491
-
Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism
-
Zhang C., and Burton Z.F. Transcription factors IIF and IIS and nucleoside triphosphate substrates as dynamic probes of the human RNA polymerase II mechanism. J Mol Biol 342 (2004) 1085-1099
-
(2004)
J Mol Biol
, vol.342
, pp. 1085-1099
-
-
Zhang, C.1
Burton, Z.F.2
-
23
-
-
12944324227
-
A ratchet mechanism of transcription elongation and its control
-
Bar-Nahum G., Epshtein V., Ruckenstein A.E., Rafikov R., Mustaev A., and Nudler E. A ratchet mechanism of transcription elongation and its control. Cell 120 (2005) 183-193
-
(2005)
Cell
, vol.120
, pp. 183-193
-
-
Bar-Nahum, G.1
Epshtein, V.2
Ruckenstein, A.E.3
Rafikov, R.4
Mustaev, A.5
Nudler, E.6
-
24
-
-
36849078192
-
Mechanism of transcriptional stalling at cisplatin-damaged DNA
-
Damsma G.E., Alt A., Brueckner F., Carell T., and Cramer P. Mechanism of transcriptional stalling at cisplatin-damaged DNA. Nat Struct Mol Biol 14 (2008) 1127-1133
-
(2008)
Nat Struct Mol Biol
, vol.14
, pp. 1127-1133
-
-
Damsma, G.E.1
Alt, A.2
Brueckner, F.3
Carell, T.4
Cramer, P.5
-
25
-
-
44449094019
-
Transient reversal of RNA polymerase II active site closing controls fidelity of transcription elongation
-
Using a combination of footprinting and kinetics, this paper demonstrates that the rate of nucleotide incorporation does not correlate with the fraction of elongation complexes in the post-translocated state and that nucleotide misincorporation is governed by sequestration of the NTP into the catalytic site.
-
Kireeva M.L., Nedialkov Y.A., Cremona G.H., Purtov Y.A., Lubkowska L., Malagon F., Burton Z.F., Strathern J.N., and Kashlev M. Transient reversal of RNA polymerase II active site closing controls fidelity of transcription elongation. Mol Cell 30 (2008) 557-566. Using a combination of footprinting and kinetics, this paper demonstrates that the rate of nucleotide incorporation does not correlate with the fraction of elongation complexes in the post-translocated state and that nucleotide misincorporation is governed by sequestration of the NTP into the catalytic site.
-
(2008)
Mol Cell
, vol.30
, pp. 557-566
-
-
Kireeva, M.L.1
Nedialkov, Y.A.2
Cremona, G.H.3
Purtov, Y.A.4
Lubkowska, L.5
Malagon, F.6
Burton, Z.F.7
Strathern, J.N.8
Kashlev, M.9
-
26
-
-
0030950638
-
RNA polymerase switches between inactivated and activated states by translocating back and forth along the DNA and the RNA
-
Komissarova N., and Kashlev M. RNA polymerase switches between inactivated and activated states by translocating back and forth along the DNA and the RNA. J Biol Chem 272 (1997) 15329-15338
-
(1997)
J Biol Chem
, vol.272
, pp. 15329-15338
-
-
Komissarova, N.1
Kashlev, M.2
-
27
-
-
0037073062
-
The many conformational states of RNA polymerase elongation complexes and their roles in the regulation of transcription
-
Erie D.A. The many conformational states of RNA polymerase elongation complexes and their roles in the regulation of transcription. Biochim Biophys Acta 1577 (2002) 224-239
-
(2002)
Biochim Biophys Acta
, vol.1577
, pp. 224-239
-
-
Erie, D.A.1
-
28
-
-
0027761137
-
Multiple RNA polymerase conformations and GreA: control of the fidelity of transcription
-
Erie D.A., Hajiseyedjavadi O., Young M.C., and Hippel P.H.v. Multiple RNA polymerase conformations and GreA: control of the fidelity of transcription. Science 262 (1993) 867-873
-
(1993)
Science
, vol.262
, pp. 867-873
-
-
Erie, D.A.1
Hajiseyedjavadi, O.2
Young, M.C.3
Hippel, P.H.v.4
-
29
-
-
33745808766
-
Kinetic investigation of Escherichia coli RNA polymerase mutants that influence nucleotide discrimination and transcription fidelity
-
Holmes S.F., Santangelo T.J., Cunningham C.K., Roberts J.W., and Erie D.A. Kinetic investigation of Escherichia coli RNA polymerase mutants that influence nucleotide discrimination and transcription fidelity. J Biol Chem 281 (2006) 18677-18683
-
(2006)
J Biol Chem
, vol.281
, pp. 18677-18683
-
-
Holmes, S.F.1
Santangelo, T.J.2
Cunningham, C.K.3
Roberts, J.W.4
Erie, D.A.5
-
30
-
-
0035958552
-
Allosteric binding of nucleoside triphosphates to RNA polymerase regulates transcription elongation
-
This paper provided the first evidence that RNAP contains a non-catalytic templated NTP binding site. The data in this paper suggested that NTP binding to this site allosterically enhances the rate of nucleotide incorporation.
-
Foster J.E., Holmes S.F., and Erie D.A. Allosteric binding of nucleoside triphosphates to RNA polymerase regulates transcription elongation. Cell 106 (2001) 243-252. This paper provided the first evidence that RNAP contains a non-catalytic templated NTP binding site. The data in this paper suggested that NTP binding to this site allosterically enhances the rate of nucleotide incorporation.
-
(2001)
Cell
, vol.106
, pp. 243-252
-
-
Foster, J.E.1
Holmes, S.F.2
Erie, D.A.3
-
31
-
-
0041315524
-
Downstream DNA sequence effects on transcription elongation: allosteric binding of nucleoside triphosphates facilitates translocation via a ratchet motion
-
This paper examines the kinetics of nucleotide incorporation, and the authors present a structural analysis showing that fork loop 2 and its surrounding structures contain all the components of a nucleotide-binding site. The authors propose a model in which templated NTPs bind to fork loop 2 (in the main channel) and facilitate nucleotide incorporation.
-
Holmes S.F., and Erie D.A. Downstream DNA sequence effects on transcription elongation: allosteric binding of nucleoside triphosphates facilitates translocation via a ratchet motion. J Biol Chem 278 (2003) 35597-35608. This paper examines the kinetics of nucleotide incorporation, and the authors present a structural analysis showing that fork loop 2 and its surrounding structures contain all the components of a nucleotide-binding site. The authors propose a model in which templated NTPs bind to fork loop 2 (in the main channel) and facilitate nucleotide incorporation.
-
(2003)
J Biol Chem
, vol.278
, pp. 35597-35608
-
-
Holmes, S.F.1
Erie, D.A.2
-
32
-
-
18944368782
-
Dynamic error correction and regulation of downstream bubble opening by human RNA polymerase II
-
This paper demonstrates that in RNAP II, the rate of sequestration of a substrate nucleotide in the active site is significantly faster than the rate of bond formation. Additional findings in this paper show that the presence of templated downstream nucleotides increases fidelity of RNAP.
-
Gong X.Q., Zhang C., Feig M., and Burton Z.F. Dynamic error correction and regulation of downstream bubble opening by human RNA polymerase II. Mol Cell 18 (2005) 461-470. This paper demonstrates that in RNAP II, the rate of sequestration of a substrate nucleotide in the active site is significantly faster than the rate of bond formation. Additional findings in this paper show that the presence of templated downstream nucleotides increases fidelity of RNAP.
-
(2005)
Mol Cell
, vol.18
, pp. 461-470
-
-
Gong, X.Q.1
Zhang, C.2
Feig, M.3
Burton, Z.F.4
-
33
-
-
27744534862
-
NTP-driven translocation and regulation of downstream template opening by multi-subunit RNA polymerases
-
Burton Z.F., Feig M., Gong X.Q., Zhang C., Nedialkov Y.A., and Xiong Y. NTP-driven translocation and regulation of downstream template opening by multi-subunit RNA polymerases. Biochem Cell Biol 83 (2005) 486-496
-
(2005)
Biochem Cell Biol
, vol.83
, pp. 486-496
-
-
Burton, Z.F.1
Feig, M.2
Gong, X.Q.3
Zhang, C.4
Nedialkov, Y.A.5
Xiong, Y.6
-
34
-
-
0037705379
-
NTP-driven translocation by human RNA polymerase II
-
This paper presents the first examination of the kinetics of nucleotide incorporation by RNAP II. The authors suggest that RNAP utilizes a nucleotide-driven model of translocation. In addition, the authors proposed the idea that the main channel, and not the secondary channel, may be the main route by which NTPs enter the catalytic site.
-
Nedialkov Y.A., Gong X.Q., Hovde S.L., Yamaguchi Y., Handa H., Geiger J.H., Yan H., and Burton Z.F. NTP-driven translocation by human RNA polymerase II. J Biol Chem 278 (2003) 18303-18312. This paper presents the first examination of the kinetics of nucleotide incorporation by RNAP II. The authors suggest that RNAP utilizes a nucleotide-driven model of translocation. In addition, the authors proposed the idea that the main channel, and not the secondary channel, may be the main route by which NTPs enter the catalytic site.
-
(2003)
J Biol Chem
, vol.278
, pp. 18303-18312
-
-
Nedialkov, Y.A.1
Gong, X.Q.2
Hovde, S.L.3
Yamaguchi, Y.4
Handa, H.5
Geiger, J.H.6
Yan, H.7
Burton, Z.F.8
-
35
-
-
37549044288
-
A tunable ratchet driving human RNA polymerse II translocation adjusted by accurately templated nucleoside triphosphates loaded at downstream sites and by elongation factors
-
Xiong Y., and Burton Z.F. A tunable ratchet driving human RNA polymerse II translocation adjusted by accurately templated nucleoside triphosphates loaded at downstream sites and by elongation factors. J Biol Chem 282 (2007) 36582-36592
-
(2007)
J Biol Chem
, vol.282
, pp. 36582-36592
-
-
Xiong, Y.1
Burton, Z.F.2
-
36
-
-
48749102174
-
Rapid kinetic analysis of transcription elongation by Escherichia coli RNA polymerase
-
This paper demonstrates that the presence of a downstream templated NTP increases the rate of pyrophosphate release from the previous nucleotide incorporation event; providing the first indication of the functional role of the secondary binding site in the nucleotide addition cycle.
-
Johnson R.S., Strausbauch M., Cooper R., and Register J.K. Rapid kinetic analysis of transcription elongation by Escherichia coli RNA polymerase. J Mol Biol 381 (2008) 1106-1113. This paper demonstrates that the presence of a downstream templated NTP increases the rate of pyrophosphate release from the previous nucleotide incorporation event; providing the first indication of the functional role of the secondary binding site in the nucleotide addition cycle.
-
(2008)
J Mol Biol
, vol.381
, pp. 1106-1113
-
-
Johnson, R.S.1
Strausbauch, M.2
Cooper, R.3
Register, J.K.4
-
37
-
-
0028962338
-
Translocation of the Escherichia coli transcription complex observed in the registers 11 to 20:'Jumping'of RNA polymerase and asymmetric expansion and contraction of the 'transcription bubble'
-
Zaychikov E., Denissova L., and Heumann H. Translocation of the Escherichia coli transcription complex observed in the registers 11 to 20:'Jumping'of RNA polymerase and asymmetric expansion and contraction of the 'transcription bubble'. Proc Natl Acad Sci USA 92 (1995) 1739-1743
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 1739-1743
-
-
Zaychikov, E.1
Denissova, L.2
Heumann, H.3
-
38
-
-
34547204502
-
A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing
-
Toulokhonov I., Zhang J., Palangat M., and Landick R. A central role of the RNA polymerase trigger loop in active-site rearrangement during transcriptional pausing. Mol Cell 27 (2007) 406-419
-
(2007)
Mol Cell
, vol.27
, pp. 406-419
-
-
Toulokhonov, I.1
Zhang, J.2
Palangat, M.3
Landick, R.4
-
39
-
-
67249110911
-
Structure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data
-
Meyer P.A., Suh M.-H., Mincheng Z., and Fu J. Structure of the 12-subunit RNA polymerase II refined with the aid of anomalous diffraction data. J Biol Chem 284 (2009) 12933-12939
-
(2009)
J Biol Chem
, vol.284
, pp. 12933-12939
-
-
Meyer, P.A.1
Suh, M.-H.2
Mincheng, Z.3
Fu, J.4
-
40
-
-
67449116330
-
Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA
-
Sydow J.F., Brueckner F., Cheung A.C., Damsma G.E., Dengl S., Lehmann E., Vassylyev D., and Cramer P. Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA. Mol Cell 34 (2009) 710-721
-
(2009)
Mol Cell
, vol.34
, pp. 710-721
-
-
Sydow, J.F.1
Brueckner, F.2
Cheung, A.C.3
Damsma, G.E.4
Dengl, S.5
Lehmann, E.6
Vassylyev, D.7
Cramer, P.8
-
41
-
-
39149093390
-
Structure-function analysis of the RNA polymerase cleft loops elucidates initial transcription, DNA unwinding and RNA displacement
-
Naji S., Bertero M.G., Spitalny P., Cramer P., and Thomm M. Structure-function analysis of the RNA polymerase cleft loops elucidates initial transcription, DNA unwinding and RNA displacement. Nucleic Acids Res 36 (2008) 676-687
-
(2008)
Nucleic Acids Res
, vol.36
, pp. 676-687
-
-
Naji, S.1
Bertero, M.G.2
Spitalny, P.3
Cramer, P.4
Thomm, M.5
-
42
-
-
8344234112
-
Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center
-
Westover K.D., Bushnell D.A., and Kornberg R.D. Structural basis of transcription: nucleotide selection by rotation in the RNA polymerase II active center. Cell 119 (2004) 481-489
-
(2004)
Cell
, vol.119
, pp. 481-489
-
-
Westover, K.D.1
Bushnell, D.A.2
Kornberg, R.D.3
-
43
-
-
2942696237
-
Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the rna polymerase secondary channel
-
Mukhopadhyay J., Sineva E., Knight J., Levy R.M., and Ebright R.H. Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the rna polymerase secondary channel. Mol Cell 14 (2004) 739-751
-
(2004)
Mol Cell
, vol.14
, pp. 739-751
-
-
Mukhopadhyay, J.1
Sineva, E.2
Knight, J.3
Levy, R.M.4
Ebright, R.H.5
-
44
-
-
0034725870
-
A structural model of transcription elongation
-
Korzheva N., Mustaev A., Kozlov M., Malhotra A., Nikiforov V., Goldfarb A., and Darst S.A. A structural model of transcription elongation. Science 289 (2000) 619-625
-
(2000)
Science
, vol.289
, pp. 619-625
-
-
Korzheva, N.1
Mustaev, A.2
Kozlov, M.3
Malhotra, A.4
Nikiforov, V.5
Goldfarb, A.6
Darst, S.A.7
-
45
-
-
2042475439
-
Structural basis for transcription regulation by alarmone ppGpp
-
Artsimovitch I., Patlan V., Sekine S.-I., Vassylyeva M.N., Hosaka T., Ochi K., Yokoyama S., and Vassylyev D.G. Structural basis for transcription regulation by alarmone ppGpp. Cell 117 (2004) 299-310
-
(2004)
Cell
, vol.117
, pp. 299-310
-
-
Artsimovitch, I.1
Patlan, V.2
Sekine, S.-I.3
Vassylyeva, M.N.4
Hosaka, T.5
Ochi, K.6
Yokoyama, S.7
Vassylyev, D.G.8
|