{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T18:31:43Z","timestamp":1791225103011,"version":"4.1.0"},"reference-count":22,"publisher":"National Academy of Sciences","issue":"39","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2008,9,30]]},"abstract":"<jats:p>\n                    Rifamycin antibacterial agents inhibit bacterial RNA polymerase (RNAP) by binding to a site adjacent to the RNAP active center and preventing synthesis of RNA products &gt;2\u20133 nt in length. Recently, Artsimovitch\n                    <jats:italic>et al.<\/jats:italic>\n                    [(2005)\n                    <jats:italic>Cell<\/jats:italic>\n                    122:351\u2013363] proposed that rifamycins function by allosteric modulation of binding of Mg\n                    <jats:sup>2+<\/jats:sup>\n                    to the RNAP active center and presented three lines of biochemical evidence consistent with this proposal. Here, we show that rifamycins do not affect the affinity of binding of Mg\n                    <jats:sup>2+<\/jats:sup>\n                    to the RNAP active center, and we reassess the three lines of biochemical evidence, obtaining results not supportive of the proposal. We conclude that rifamycins do not function by allosteric modulation of binding of Mg\n                    <jats:sup>2+<\/jats:sup>\n                    to the RNAP active center.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0802822105","type":"journal-article","created":{"date-parts":[[2008,9,11]],"date-time":"2008-09-11T21:10:06Z","timestamp":1221167406000},"page":"14820-14825","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":83,"title":["Rifamycins do not function by allosteric modulation of binding of Mg\n                    <sup>2+<\/sup>\n                    to the RNA polymerase active center"],"prefix":"10.1073","volume":"105","author":[{"given":"Andrey","family":"Feklistov","sequence":"first","affiliation":[{"name":"*Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021;"},{"name":"Public Health Research Institute, 225 Warren Street, Newark, NJ 07103;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vladimir","family":"Mekler","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry, Rutgers University, Piscataway, NJ 08854; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Qiaorong","family":"Jiang","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry, Rutgers University, Piscataway, NJ 08854; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lars F.","family":"Westblade","sequence":"additional","affiliation":[{"name":"*Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herbert","family":"Irschik","sequence":"additional","affiliation":[{"name":"Helmholtz-Zentrum f\u00fcr Infektions Forschung, D38124 Braunschweig, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rolf","family":"Jansen","sequence":"additional","affiliation":[{"name":"Helmholtz-Zentrum f\u00fcr Infektions Forschung, D38124 Braunschweig, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arkady","family":"Mustaev","sequence":"additional","affiliation":[{"name":"Public Health Research Institute, 225 Warren Street, Newark, NJ 07103;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seth A.","family":"Darst","sequence":"additional","affiliation":[{"name":"*Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10021;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard H.","family":"Ebright","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, Waksman Institute, and Department of Chemistry, Rutgers University, Piscataway, NJ 08854; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2008,9,30]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1021\/cr030112j"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0005-2787(67)90147-5"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(72)90534-7"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(17)34269-2"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1970.tb01066.x"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(01)00286-0"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2005.07.014"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.273.5271.107"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.13.6641"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81515-9"},{"key":"e_1_3_3_11_2","first-page":"397","volume-title":"RNA Polymerase","author":"Wehrli W","year":"1976","unstructured":"W Wehrli, J Handschin, W Wunderli RNA Polymerase, eds MJ Chamberlin, R Losick (Cold Spring Harbor Lab Press, Cold Spring Harbor, NY), pp. 397\u2013412 (1976)."},{"key":"e_1_3_3_12_2","first-page":"369","volume-title":"RNA Polymerase","author":"Barh W","year":"1976","unstructured":"W Barh, W Stender, K-H Scheit, T Jovin RNA Polymerase, eds MJ Chamberlin, R Losick (Cold Spring Harbor Lab Press, Cold Spring Harbor, NY), pp. 369\u2013396 (1976)."},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(88)90517-7"},{"key":"e_1_3_3_14_2","first-page":"127","article-title":"Nucleotide substitutions in the rpoB gene leading to rifampicin resistance of E. coli RNA polymerase","volume":"10","author":"Lisitsyn NA","year":"1984","unstructured":"NA Lisitsyn, SO Gur'ev, ED Sverdlov, EP Moiseeva, VG Nikiforov, Nucleotide substitutions in the rpoB gene leading to rifampicin resistance of E. coli RNA polymerase. 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