Insights into substrate binding and catalytic mechanism of human tyrosyl-DNA phosphodiesterase (Tdp1) from vanadate and tungstate-inhibited structures
about
Substrate specificity of tyrosyl-DNA phosphodiesterase I (Tdp1)Novel high-throughput electrochemiluminescent assay for identification of human tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors and characterization of furamidine (NSC 305831) as an inhibitor of Tdp1Increased expression and activity of repair genes TDP1 and XPF in non-small cell lung cancerDrugging topoisomerases: lessons and challengesThe catalytic scaffold of the haloalkanoic acid dehalogenase enzyme superfamily acts as a mold for the trigonal bipyramidal transition stateAn ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutaseTungstate as a Transition State Analog for Catalysis by Alkaline PhosphataseTyrosyl-DNA phosphodiesterase (Tdp1) participates in the repair of Top2-mediated DNA damageDesign and synthesis of fluorescent substrates for human tyrosyl-DNA phosphodiesterase I.Identification of phosphotyrosine mimetic inhibitors of human tyrosyl-DNA phosphodiesterase I by a novel AlphaScreen high-throughput assayInhibitors of human tyrosyl-DNA phospodiesterase (hTdp1) developed by virtual screening using ligand-based pharmacophores.Structures of the phosphorylated and VO(3)-bound 2H-phosphatase domain of Sts-2.Design, synthesis, and biological evaluation of O-2-modified indenoisoquinolines as dual topoisomerase I-tyrosyl-DNA phosphodiesterase I inhibitors.Yeast Tdp1 regulates the fidelity of nonhomologous end joining.Biochemical assays for the discovery of TDP1 inhibitorsHuman Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages.The power of vanadate in crystallographic investigations of phosphoryl transfer enzymes.Effects of DNA and protein size on substrate cleavage by human tyrosyl-DNA phosphodiesterase 1.Tyrosyl-DNA Phosphodiesterase 1 (Tdp1) inhibitorsTyrosyl-DNA phosphodiesterase I catalytic mutants reveal an alternative nucleophile that can catalyze substrate cleavagePhospholipase D: enzymology, functionality, and chemical modulationStructure-function studies of a plant tyrosyl-DNA phosphodiesterase provide novel insights into DNA repair mechanisms of Arabidopsis thalianaSynthesis and biological evaluation of the first dual tyrosyl-DNA phosphodiesterase I (Tdp1)-topoisomerase I (Top1) inhibitors.How similar are enzyme active site geometries derived from quantum mechanical theozymes to crystal structures of enzyme-inhibitor complexes? Implications for enzyme design.Synthesis and biological evaluation of indenoisoquinolines that inhibit both tyrosyl-DNA phosphodiesterase I (Tdp1) and topoisomerase I (Top1)Repair of topoisomerase I-mediated DNA damage.Tyrosyl-DNA phosphodiesterase as a target for anticancer therapy4-Pregnen-21-ol-3,20-dione-21-(4-bromobenzenesulfonate) (NSC 88915) and related novel steroid derivatives as tyrosyl-DNA phosphodiesterase (Tdp1) inhibitors.Tyrosyl-DNA phosphodiesterase I resolves both naturally and chemically induced DNA adducts and its potential as a therapeutic target.Structure Modeling of Human Tyrosyl-DNA Phosphodiesterase 1 and Screening for Its Inhibitors.Vanadate-based transition-state analog inhibitors of Cre-LoxP recombinationPre-steady state kinetics of DNA binding and abasic site hydrolysis by tyrosyl-DNA phosphodiesterase 1.SUMO modification of the neuroprotective protein TDP1 facilitates chromosomal single-strand break repair.A novel mechanism for the scission of double-stranded DNA: BfiI cuts both 3'-5' and 5'-3' strands by rotating a single active siteTyrosyl-DNA phosphodiesterase 1 initiates repair of apurinic/apyrimidinic sites.Structural basis for DNA 3'-end processing by human tyrosyl-DNA phosphodiesterase 1.GPCR Modulation of Thieno[2,3-b]pyridine Anti-Proliferative Agents.Investigation into Improving the Aqueous Solubility of the Thieno[2,3-b]pyridine Anti-Proliferative Agents.The Human Tyrosyl-DNA Phosphodiesterase 1 (hTdp1) Inhibitor NSC120686 as an Exploratory Tool to Investigate Plant Tdp1 Genes.Novel group of tyrosyl-DNA-phosphodiesterase 1 inhibitors based on disaccharide nucleosides as drug prototypes for anti-cancer therapy
P2860
Q24299565-D994F2E2-0FB0-423D-BA0B-88A34F71EAF7Q24311803-0B13ADA4-8801-4249-B757-2142E0C273D2Q24318465-EE8E9EDB-26CA-4C83-83EF-C7F11EC66886Q27000099-EB03DFF6-FBC7-4CFF-B85F-36222A89EEB7Q27650273-1D99EED7-344E-411B-BD4F-D66C185D843AQ27673515-18A28447-E062-4780-A4B5-530DF929EE71Q27704888-017452E8-F502-45E8-A678-1045B15F9AA4Q27934837-644E8B04-CE9F-4E2E-A6F4-4959DCBCF718Q30837074-7607528C-FCF7-419F-ACC2-08B0C89B2C50Q33399360-9681EE60-887D-4C16-87FB-01B2AAA6CDFDQ33517282-786AE0F8-5865-46FD-AD96-B7116DFED3BEQ33644549-FBE3BA65-FED3-4E13-97F2-062122E90897Q33662415-3AED85CB-18E6-4D3C-B897-E92E969A9F0CQ33732769-15456357-ED8D-4FA5-A9E9-7EDAC9F45649Q34021070-F79C9469-08D7-44B2-831F-741E1D798FECQ34312801-3877A8A4-C6D4-4388-9454-1362FAED4301Q34369961-AC0D8EA5-29A7-4F4A-AF56-705229D62BABQ35152316-9D79756D-6D62-4D0C-998A-E6E0FF3CC838Q35167579-6334622B-E632-45EE-878E-DC465793538BQ35172933-B87557CE-7982-4EE2-874D-DB01486F5516Q35599714-CBE26F39-284A-4129-B4E5-92DE497E9130Q35832629-B9FA68C0-E1E0-4C5E-9E3A-1B9B1282F570Q35954578-55F23295-2C2A-4551-9C71-3B79527A3FEDQ36393515-36D78239-CA4C-45A2-8462-E49C702103C3Q36524994-969925A7-1F1D-4876-AB4D-D2771EAC5CBEQ36557533-7B834D5D-0C73-4E61-AE75-6635D6F496D7Q36744910-5CFC57C5-C5F1-4810-B22F-795C58F1C429Q37445367-163FAF78-7A2B-423A-B04F-A2B975E3208AQ38261264-0931BCFB-9674-4B5F-A3C2-C449138FFC39Q38287674-A57CD0F6-9258-4D6E-BEAB-F0676AB9BB70Q38351515-022288A3-DC07-4713-9CC9-B3EDE325E27EQ39337130-D62029C6-4B21-438B-9AF5-4651FD51ECC7Q39380131-CD8AB0D8-8CCA-433D-BC3C-932A869CC6E3Q39986656-E625A87D-999F-4F39-898D-AA4C2C944E23Q42022533-A6C497CB-8D17-42AE-9179-9A2BB667E7A3Q47236725-FB291CBD-FA11-4830-8D2C-308C5654E555Q47274809-03425459-94E9-45FB-893E-4F1BFB9B2B1FQ47720805-9EF55BBC-4362-458F-BBE3-CF3E08259170Q55340676-AC539D6E-B724-4406-830F-EA3C5EEEA1E8Q58759037-F6A807D2-3D36-4322-9745-A86C581FC57B
P2860
Insights into substrate binding and catalytic mechanism of human tyrosyl-DNA phosphodiesterase (Tdp1) from vanadate and tungstate-inhibited structures
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Insights into substrate bindin ...... tungstate-inhibited structures
@ast
Insights into substrate bindin ...... tungstate-inhibited structures
@en
Insights into substrate bindin ...... tungstate-inhibited structures
@nl
type
label
Insights into substrate bindin ...... tungstate-inhibited structures
@ast
Insights into substrate bindin ...... tungstate-inhibited structures
@en
Insights into substrate bindin ...... tungstate-inhibited structures
@nl
prefLabel
Insights into substrate bindin ...... tungstate-inhibited structures
@ast
Insights into substrate bindin ...... tungstate-inhibited structures
@en
Insights into substrate bindin ...... tungstate-inhibited structures
@nl
P2093
P1476
Insights into substrate bindin ...... tungstate-inhibited structures
@en
P2093
Douglas R Davies
Heidrun Interthal
James J Champoux
Wim G J Hol
P304
P356
10.1016/S0022-2836(02)01154-3
P407
P577
2002-12-13T00:00:00Z