Structure of HIV-1 Reverse Transcriptase with the Inhibitor β-Thujaplicinol Bound at the RNase H Active Site
about
Structural Basis for the Inhibition of RNase H Activity of HIV-1 Reverse Transcriptase by RNase H Active Site-Directed InhibitorsStructural and Binding Analysis of Pyrimidinol Carboxylic Acid and N-Hydroxy Quinazolinedione HIV-1 RNase H InhibitorsSynthesis, Activity, and Structural Analysis of Novel α-Hydroxytropolone Inhibitors of Human Immunodeficiency Virus Reverse Transcriptase-Associated Ribonuclease HComplexes of HIV-1 RT, NNRTI and RNA/DNA hybrid reveal a structure compatible with RNA degradationStructural and Inhibition Studies of the RNase H Function of Xenotropic Murine Leukemia Virus-Related Virus Reverse TranscriptaseCrystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virusStructure of a Dihydroxycoumarin Active-Site Inhibitor in Complex with the RNase H Domain of HIV-1 Reverse Transcriptase and Structure–Activity Analysis of Inhibitor AnalogsStructures of HIV-1 RT-RNA/DNA ternary complexes with dATP and nevirapine reveal conformational flexibility of RNA/DNA: insights into requirements for RNase H cleavageStructural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic InstabilityThe hepatitis B virus ribonuclease H is sensitive to inhibitors of the human immunodeficiency virus ribonuclease H and integrase enzymesVirtual screening models for prediction of HIV-1 RT associated RNase H inhibitionInhibitor ranking through QM based chelation calculations for virtual screening of HIV-1 RNase H inhibitionRibonuclease H/DNA Polymerase HIV-1 Reverse Transcriptase Dual Inhibitor: Mechanistic Studies on the Allosteric Mode of Action of Isatin-Based Compound RMNC6Evidence from molecular dynamics simulations of conformational preorganization in the ribonuclease H active site.Inhibition of the ribonuclease H activity of HIV-1 reverse transcriptase by GSK5750 correlates with slow enzyme-inhibitor dissociation.Inhibition of foamy virus reverse transcriptase by human immunodeficiency virus type 1 RNase H inhibitorsIdentification of alternative binding sites for inhibitors of HIV-1 ribonuclease H through comparative analysis of virtual enrichment studiesThe biology and synthesis of α-hydroxytropolones.HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors.Basic quinolinonyl diketo acid derivatives as inhibitors of HIV integrase and their activity against RNase H function of reverse transcriptase.Inhibitors of nucleotidyltransferase superfamily enzymes suppress herpes simplex virus replicationHydroxylated tropolones inhibit hepatitis B virus replication by blocking viral ribonuclease H activity.Design, synthesis, and biological evaluation of 1,3-diarylpropenones as dual inhibitors of HIV-1 reverse transcriptase.Expression of an Mg2+-dependent HIV-1 RNase H construct for drug screeningInhibition of the ANT(2")-Ia resistance enzyme and rescue of aminoglycoside antibiotic activity by synthetic α-hydroxytropolones.Mutagenesis of human immunodeficiency virus reverse transcriptase p51 subunit defines residues contributing to vinylogous urea inhibition of ribonuclease H activity.Interaction of HIV-1 reverse transcriptase ribonuclease H with an acylhydrazone inhibitor.Free Energy-Based Virtual Screening and Optimization of RNase H Inhibitors of HIV-1 Reverse Transcriptase.Synthetic α-Hydroxytropolones as Inhibitors of HIV Reverse Transcriptase Ribonuclease H Activity.Structural basis of the allosteric inhibitor interaction on the HIV-1 reverse transcriptase RNase H domain.Metal and ligand binding to the HIV-RNase H active site are remotely monitored by Ile556Two distinct modes of metal ion binding in the nuclease active site of a viral DNA-packaging terminase: insight into the two-metal-ion catalytic mechanism.Human immunodeficiency virus reverse transcriptase: 25 years of research, drug discovery, and promise.An oxidopyrylium cyclization/ring-opening route to polysubstituted α-hydroxytropolonesUnfolding the HIV-1 reverse transcriptase RNase H domain--how to lose a molecular tug-of-war.Synthetic α-Hydroxytropolones Inhibit Replication of Wild-Type and Acyclovir-Resistant Herpes Simplex Viruses.Characterization of the C-Terminal Nuclease Domain of Herpes Simplex Virus pUL15 as a Target of Nucleotidyltransferase InhibitorsInhibitors of HIV-1 Reverse Transcriptase-Associated Ribonuclease H Activity.3-Hydroxypyrimidine-2,4-diones as Selective Active Site Inhibitors of HIV Reverse Transcriptase-Associated RNase H: Design, Synthesis, and Biochemical Evaluations.Design, Synthesis, and Biological Evaluations of Hydroxypyridonecarboxylic Acids as Inhibitors of HIV Reverse Transcriptase Associated RNase H.
P2860
Q27661750-22BFD313-06C4-413B-98CD-5AE51132BDBAQ27667421-94320F2F-D191-4964-81F1-292E2FBAC71AQ27667836-43DDC605-5235-42CB-AD3D-39A120768962Q27675888-9D2E4E07-460B-460E-8180-300E385C1115Q27676777-5025C9E3-4010-4EBC-80D3-66C8E33D4AD5Q27677489-2F1CB8D4-97A8-4505-B647-8CA04CC2B3F4Q27683831-DC70BB9A-D4B5-4601-82E4-EE587E4D1F0EQ27684014-8107730F-A4F1-47D9-BABA-9726742FB1DDQ28074527-4D79A35C-356A-4F03-AC4E-D3267B7CE07BQ28485228-93B2DEF1-D34B-4410-ABF9-0C01606F4693Q28533482-7B8F43B5-11CA-4B87-86C1-7C601D923D99Q28539353-93621BF4-E8D8-4D99-9C7D-04754E46D079Q28552768-3DDF7626-D690-4F80-A6E1-61A23C74C27AQ33654266-AF20885A-E023-4A57-9C24-33135A0DDDBCQ33718515-7127F6E4-DC8D-49B7-9270-034EA483E8AEQ33798319-184D4FD0-BDC6-4560-A974-BA3FFB97F482Q33945786-4CF9BD82-E5FF-45FD-8A43-E8ABBD912E73Q33968209-A08B9942-0D9F-4813-909A-6D88A7D8D366Q34223771-584D8ABA-DD92-468F-8683-3D384FE98096Q34372481-2140502D-1B2B-4A57-88ED-C86E0AA5CAF4Q34597590-3E71990B-7372-4871-9C8B-933A0EF73F7AQ35105877-B815B720-4307-44F1-BB8E-6855F485E652Q35172317-60CF8581-423E-472D-93FF-520AC82E85B2Q35270807-2F30FC99-3962-4533-A2FA-18AAE1FD0828Q35302819-5957ED56-C35F-4B10-8ED6-16BD73CC3D76Q35763192-ECC06947-39CC-424C-B3C2-F36A35445ED7Q35874082-299EB388-AEF2-4893-A7BC-63F743F2CC5AQ36155983-398524C3-32FF-49A4-84C6-1E38EDC46888Q36250808-49EC455A-5D5F-4EFE-8418-3B7CF65A5F17Q36300994-12C5E72E-E7E1-47A7-AB2E-F48D0F97E365Q36368801-59A6B38D-F634-4208-9130-17780DE1DED0Q36370804-998DB0ED-5F32-4EB5-8475-5432E5540315Q36435971-BCC45F6C-772E-44EE-B119-DBF27673D972Q36456779-AD97A387-4564-4147-B11B-4F6945489EAAQ36627970-DCB9D3E1-B3C0-4968-A126-DA3B001C65C0Q36730096-A4DB6D77-1153-47C4-8D06-6D7546292828Q36760555-E846D77A-E21F-4650-85D9-AB2738A23F69Q36768814-BCE3C0BF-FF36-4A86-8963-8CBECAC0EC2DQ36913220-17E34A3B-D8C5-4955-B319-F7B088E809E7Q36940608-D62DDD31-2840-471C-A3FA-115AE6BD5A93
P2860
Structure of HIV-1 Reverse Transcriptase with the Inhibitor β-Thujaplicinol Bound at the RNase H Active Site
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@ast
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@en
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@nl
type
label
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@ast
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@en
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@nl
prefLabel
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@ast
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@en
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@nl
P2093
P2860
P3181
P1433
P1476
Structure of HIV-1 Reverse Tra ...... und at the RNase H Active Site
@en
P2093
Arthur D Clark
Chhaya Dharia
Daniel M Himmel
Joseph D Bauman
Kalyan Das
Karen A Maegley
Kevin Ryan
Michael J Hickey
Robert A Love
Simon Bergqvist
P2860
P304
P3181
P356
10.1016/J.STR.2009.09.016
P577
2009-12-09T00:00:00Z