Structural basis of gate-DNA breakage and resealing by type II topoisomerases
about
DNA cleavage and opening reactions of human topoisomerase IIα are regulated via Mg2+-mediated dynamic bending of gate-DNADrugging topoisomerases: lessons and challengesStructural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistanceStructure of QnrB1, a Plasmid-mediated Fluoroquinolone Resistance FactorStructural basis of type II topoisomerase inhibition by the anticancer drug etoposideThe Structure of DNA-Bound Human Topoisomerase II Alpha: Conformational Mechanisms for Coordinating Inter-Subunit Interactions with DNA CleavageStructure of a topoisomerase II–DNA–nucleotide complex reveals a new control mechanism for ATPase activityStructure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transportOn the structural basis and design guidelines for type II topoisomerase-targeting anticancer drugsDirect control of type IIA topoisomerase activity by a chromosomally encoded regulatory proteinApplication of a novel microtitre plate-based assay for the discovery of new inhibitors of DNA gyrase and DNA topoisomerase VIExploring the active site of the Streptococcus pneumoniae topoisomerase IV-DNA cleavage complex with novel 7,8-bridged fluoroquinolonesRecovery of the poisoned topoisomerase II for DNA religation: coordinated motion of the cleavage core revealed with the microsecond atomistic simulation.Fluoroquinolone-gyrase-DNA complexes: two modes of drug binding.Thiophene antibacterials that allosterically stabilize DNA-cleavage complexes with DNA gyraseThe impact of the C-terminal domain on the interaction of human DNA topoisomerase II α and β with DNA.Role of the water-metal ion bridge in mediating interactions between quinolones and Escherichia coli topoisomerase IV.Exploiting bacterial DNA gyrase as a drug target: current state and perspectives.Solution structures of DNA-bound gyrase.Molecular characterization of fluoroquinolone resistance in Mycobacterium tuberculosis: functional analysis of gyrA mutation at position 74.Bacillus anthracis GrlAV96A topoisomerase IV, a quinolone resistance mutation that does not affect the water-metal ion bridgeBypassing fluoroquinolone resistance with quinazolinediones: studies of drug-gyrase-DNA complexes having implications for drug design.Use of divalent metal ions in the DNA cleavage reaction of topoisomerase IV.Characterization of the novel DNA gyrase inhibitor AZD0914: low resistance potential and lack of cross-resistance in Neisseria gonorrhoeae.Direct measurement of DNA bending by type IIA topoisomerases: implications for non-equilibrium topology simplificationAll tangled up: how cells direct, manage and exploit topoisomerase function.Local sensing of global DNA topology: from crossover geometry to type II topoisomerase processivityStructure based in silico analysis of quinolone resistance in clinical isolates of Salmonella Typhi from India.Drug interactions with Bacillus anthracis topoisomerase IV: biochemical basis for quinolone action and resistance.Protective effect of Qnr on agents other than quinolones that target DNA gyrase.Structure-based design of novel combinatorially generated NBTIs as potential DNA gyrase inhibitors against various Staphylococcus aureus mutant strains.Fluoroquinolones stimulate the DNA cleavage activity of topoisomerase IV by promoting the binding of Mg(2+) to the second metal binding site.Crystal structure and stability of gyrase-fluoroquinolone cleaved complexes from Mycobacterium tuberculosis.Mycobacterium fluoroquinolone resistance protein B, a novel small GTPase, is involved in the regulation of DNA gyrase and drug resistance.Topoisomerase IV-quinolone interactions are mediated through a water-metal ion bridge: mechanistic basis of quinolone resistance.Suppression of gyrase-mediated resistance by C7 aryl fluoroquinolones.The role of DNA bending in type IIA topoisomerase function.Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomeraseDistinct regions of the Escherichia coli ParC C-terminal domain are required for substrate discrimination by topoisomerase IV.Mechanism of quinolone action and resistance.
P2860
Q24305044-E754D7E7-7D2B-4D51-BCAC-779E22C03811Q27000099-CF850AAE-EBAB-40CB-BFAE-B27644A19FA0Q27664216-D8073086-D923-428A-BBF1-01784BE6B901Q27667906-FCD453FA-22E1-418D-A9D4-C8D62B130282Q27670929-E78A65A8-3510-4153-82F8-B3F4D8F66D67Q27670934-CFEF88AF-CCFF-4672-8182-C9F291B31F75Q27673758-4C28DA53-4877-4EFD-945E-64655FA20890Q27679776-58A3DC02-76CD-4E36-AA34-FBF07C0DC139Q27679956-52AF6EF9-0F73-4822-96FF-D8EB6AD8459EQ27684534-0727B59A-EFD2-407C-BD83-BA5AA926CEAAQ28486816-9E346E82-9D99-4E98-A8E3-34ABF748113AQ28828291-F94A9BF4-F822-4AEE-BE3D-36EF2DF6E92DQ30661486-CBAC7DA6-3432-4F82-B465-A4E74BA23090Q33556083-E3315A1E-0D18-461A-85E6-1307AFEF412BQ33782498-C1AA38BB-55DF-458F-A1FA-C9CA32F59486Q33831806-0EF682D8-F6FC-442D-B2F6-486F1993B45EQ34119765-E93EC33A-63EC-4B73-AB5F-36F69E57ADDDQ34214929-FD610E87-AC5F-4FD2-B922-198822F13FBFQ34513886-65FFA8BE-13A7-4E5B-BEE4-0D34642AB51EQ34529276-ECAEEE1D-EC16-4571-8044-0246D7457719Q34597404-3DBD03B1-8893-4194-B4F0-65B105BFAB06Q34756857-B3A8704B-93A6-4947-B841-206D6AC24E37Q35040946-F52CD9B2-07D1-4E70-A361-4602784048B1Q35076809-2872AE99-A172-4C3E-83B6-D821B1F0F69AQ35120752-005939BB-9F64-4FE8-82F0-056523062CFEQ35154537-B1315678-5ECA-42A8-9049-443F1194F024Q35468217-A9EAE40B-0D7E-445C-9DD2-6000D5539237Q35626961-F8E4738D-0634-41C2-AE8A-460A1605628AQ35682250-7C8CEC3E-362E-456E-AB2E-0A560F691934Q36158288-B4654E37-5C0A-4176-9F9B-156E240EC9DCQ36394817-B27D8227-96B2-4A3C-A2EA-56BBE026A233Q36483838-F5445145-6830-4675-8065-9ED0F4C05A33Q36607637-DDC92BF7-B9BF-43B4-95CD-385F4CCF929FQ36619820-7A0C7EDC-6730-4B61-9DAA-55BC2A48C6C8Q36783606-D065EF3F-68D7-4BBC-97CF-EB5F19F99562Q36817994-7F6D46D6-BA34-4AEB-8280-558096712578Q36878467-5C546BCD-FFBB-429F-BFAA-BA81559C1002Q37148510-AFBE0D98-DBB0-4DD2-AAC6-F63B3DC75E5CQ37394413-70FE36A9-4566-443F-8D4B-95DC3058D1B3Q37701591-A006D69D-5469-4505-840A-025F606821EF
P2860
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
description
2010 nî lūn-bûn
@nan
2010 թուականին հրատարակուած գիտական յօդուած
@hyw
2010 թվականին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@ast
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@en
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@nl
type
label
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@ast
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@en
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@nl
altLabel
Structural Basis of Gate-DNA Breakage and Resealing by Type II Topoisomerases
@en
prefLabel
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@ast
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@en
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@nl
P2093
P2860
P3181
P1433
P1476
Structural basis of gate-DNA breakage and resealing by type II topoisomerases
@en
P2093
Dennis A Veselkov
Ivan Laponogov
Katherine E McAuley
L Mark Fisher
Mark R Sanderson
Xiao-Su Pan
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0011338
P407
P577
2010-01-01T00:00:00Z