Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release - Wikidata - awgldk - TriplyDB

Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release

Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release

http://www.wikidata.org/entity/Q34590412

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The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex RNase H activity: structure, specificity, and function in reverse transcription Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD Murine leukemia virus reverse transcriptase: structural comparison with HIV-1 reverse transcriptase Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription The use of polyoxometalates in protein crystallography – An attempt to widen a well-known bottleneck A relaxed active site after exon ligation by the group I intron Insights into RNA/DNA hybrid recognition and processing by RNase H from the crystal structure of a non-specific enzyme-dsDNA complex Structure and function of an RNase H domain at the heart of the spliceosome Functional and structural characterization of the integrase from the prototype foamy virus Running in Reverse: The Structural Basis for Translocation Polarity in Hexameric Helicases Structural Basis for the Inhibition of RNase H Activity of HIV-1 Reverse Transcriptase by RNase H Active Site-Directed Inhibitors A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain Crystal Structures of RNase H2 in Complex with Nucleic Acid Reveal the Mechanism of RNA-DNA Junction Recognition and Cleavage Structural and Binding Analysis of Pyrimidinol Carboxylic Acid and N-Hydroxy Quinazolinedione HIV-1 RNase H Inhibitors Structural and Biochemical Basis for Development of Influenza Virus Inhibitors Targeting the PA Endonuclease Structural and functional insight into the mechanism of an alkaline exonuclease from Laribacter hongkongensis Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution Defects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune disease The Structure of the Herpes Simplex Virus DNA-Packaging Terminase pUL15 Nuclease Domain Suggests an Evolutionary Lineage among Eukaryotic and Prokaryotic Viruses 3′-Processing and strand transfer catalysed by retroviral integrasein crystallo Structure and characterization of RNase H3 from Aquifex aeolicus Novel complex MAD phasing and RNase H structural insights using selenium oligonucleotides Crystal structure of metagenome-derived LC9-RNase H1 with atypical DEDN active site motif Crystal structure of RNase H3–substrate complex reveals parallel evolution of RNA/DNA hybrid recognition The hepatitis B virus ribonuclease H is sensitive to inhibitors of the human immunodeficiency virus ribonuclease H and integrase enzymes A Computational Model for Predicting RNase H Domain of Retrovirus Retroviral DNA Integration The RNase H-like superfamily: new members, comparative structural analysis and evolutionary classification.Role of N-terminal extension of Bacillus stearothermophilus RNase H2 and C-terminal extension of Thermotoga maritima RNase H2.In-Silico docking of HIV-1 integrase inhibitors reveals a novel drug type acting on an enzyme/DNA reaction intermediate.Catalytic mechanism of RNA backbone cleavage by ribonuclease H from quantum mechanics/molecular mechanics simulations.The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain.Novel approaches to inhibiting HIV-1 replication.Evidence from molecular dynamics simulations of conformational preorganization in the ribonuclease H active site.Phosphate steering by Flap Endonuclease 1 promotes 5'-flap specificity and incision to prevent genome instability.Argonautes confront new small RNAs.The use of divalent metal ions by type II topoisomerases.HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors.

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P2860

Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release

http://www.wikidata.org/entity/Q34590412

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006 թվականի ապրիլին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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Stepwise analyses of metal ion ...... abilization to product release

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SJ.EMBOJ.7601076

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The EMBO Journal

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Stepwise analyses of metal ion ...... abilization to product release

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Marcin Nowotny

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Wei Yang

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P2860

A general two-metal-ion mechanism for catalytic RNA

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Transition state stabilization by a catalytic RNA

Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein

The role of metals in catalysis by the restriction endonuclease BamHI

Rapid automated molecular replacement by evolutionary search

Purified Argonaute2 and an siRNA form recombinant human RISC

Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice

Crystal structure of Argonaute and its implications for RISC slicer activity

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1924-1933

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10.1038/SJ.EMBOJ.7601076

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9

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25

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16601679

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