Structural Biology of Bacterial RNA Polymerase
Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural infor...
Ausführliche Beschreibung
Autor*in: |
Katsuhiko S. Murakami [verfasserIn] |
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Englisch |
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2015 |
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In: Biomolecules - MDPI AG, 2013, 5(2015), 2, Seite 848-864 |
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Übergeordnetes Werk: |
volume:5 ; year:2015 ; number:2 ; pages:848-864 |
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DOI / URN: |
10.3390/biom5020848 |
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Katalog-ID: |
DOAJ025620703 |
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10.3390/biom5020848 doi (DE-627)DOAJ025620703 (DE-599)DOAJ4d32257079ae4653b08ac4df498c1bfb DE-627 ger DE-627 rakwb eng QR1-502 Katsuhiko S. Murakami verfasserin aut Structural Biology of Bacterial RNA Polymerase 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. bacterial RNA polymerase transcription core enzyme holoenzyme σ factor transcription factor anti-σ factor X-ray crystallography NMR inhibitor antibiotic Microbiology In Biomolecules MDPI AG, 2013 5(2015), 2, Seite 848-864 (DE-627)735688915 (DE-600)2701262-1 2218273X nnns volume:5 year:2015 number:2 pages:848-864 https://doi.org/10.3390/biom5020848 kostenfrei https://doaj.org/article/4d32257079ae4653b08ac4df498c1bfb kostenfrei http://www.mdpi.com/2218-273X/5/2/848 kostenfrei https://doaj.org/toc/2218-273X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 2 848-864 |
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10.3390/biom5020848 doi (DE-627)DOAJ025620703 (DE-599)DOAJ4d32257079ae4653b08ac4df498c1bfb DE-627 ger DE-627 rakwb eng QR1-502 Katsuhiko S. Murakami verfasserin aut Structural Biology of Bacterial RNA Polymerase 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. bacterial RNA polymerase transcription core enzyme holoenzyme σ factor transcription factor anti-σ factor X-ray crystallography NMR inhibitor antibiotic Microbiology In Biomolecules MDPI AG, 2013 5(2015), 2, Seite 848-864 (DE-627)735688915 (DE-600)2701262-1 2218273X nnns volume:5 year:2015 number:2 pages:848-864 https://doi.org/10.3390/biom5020848 kostenfrei https://doaj.org/article/4d32257079ae4653b08ac4df498c1bfb kostenfrei http://www.mdpi.com/2218-273X/5/2/848 kostenfrei https://doaj.org/toc/2218-273X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 2 848-864 |
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10.3390/biom5020848 doi (DE-627)DOAJ025620703 (DE-599)DOAJ4d32257079ae4653b08ac4df498c1bfb DE-627 ger DE-627 rakwb eng QR1-502 Katsuhiko S. Murakami verfasserin aut Structural Biology of Bacterial RNA Polymerase 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. bacterial RNA polymerase transcription core enzyme holoenzyme σ factor transcription factor anti-σ factor X-ray crystallography NMR inhibitor antibiotic Microbiology In Biomolecules MDPI AG, 2013 5(2015), 2, Seite 848-864 (DE-627)735688915 (DE-600)2701262-1 2218273X nnns volume:5 year:2015 number:2 pages:848-864 https://doi.org/10.3390/biom5020848 kostenfrei https://doaj.org/article/4d32257079ae4653b08ac4df498c1bfb kostenfrei http://www.mdpi.com/2218-273X/5/2/848 kostenfrei https://doaj.org/toc/2218-273X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 2 848-864 |
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10.3390/biom5020848 doi (DE-627)DOAJ025620703 (DE-599)DOAJ4d32257079ae4653b08ac4df498c1bfb DE-627 ger DE-627 rakwb eng QR1-502 Katsuhiko S. Murakami verfasserin aut Structural Biology of Bacterial RNA Polymerase 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. bacterial RNA polymerase transcription core enzyme holoenzyme σ factor transcription factor anti-σ factor X-ray crystallography NMR inhibitor antibiotic Microbiology In Biomolecules MDPI AG, 2013 5(2015), 2, Seite 848-864 (DE-627)735688915 (DE-600)2701262-1 2218273X nnns volume:5 year:2015 number:2 pages:848-864 https://doi.org/10.3390/biom5020848 kostenfrei https://doaj.org/article/4d32257079ae4653b08ac4df498c1bfb kostenfrei http://www.mdpi.com/2218-273X/5/2/848 kostenfrei https://doaj.org/toc/2218-273X Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 5 2015 2 848-864 |
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Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. |
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Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. |
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Since its discovery and characterization in the early 1960s (Hurwitz, J. The discovery of RNA polymerase. J. Biol. Chem. 2005, 280, 42477–42485), an enormous amount of biochemical, biophysical and genetic data has been collected on bacterial RNA polymerase (RNAP). In the late 1990s, structural information pertaining to bacterial RNAP has emerged that provided unprecedented insights into the function and mechanism of RNA transcription. In this review, I list all structures related to bacterial RNAP (as determined by X-ray crystallography and NMR methods available from the Protein Data Bank), describe their contributions to bacterial transcription research and discuss the role that small molecules play in inhibiting bacterial RNA transcription. |
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score |
7.4014225 |