A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1. - sprookjes - yvandenbroek - TriplyDB

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

http://www.wikidata.org/entity/Q42626728

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The fidelity of DNA synthesis by eukaryotic replicative and translesion synthesis polymerases Bypass of DNA lesions generated during anticancer treatment with cisplatin by DNA polymerase eta The structure of a high fidelity DNA polymerase bound to a mismatched nucleotide reveals an "ajar" intermediate conformation in the nucleotide selection mechanism.Structure of the 2-Aminopurine-Cytosine Base Pair Formed in the Polymerase Active Site of the RB69 Y567A-DNA Polymerase Effect of N2-guanyl modifications on early steps in catalysis of polymerization by Sulfolobus solfataricus P2 DNA polymerase Dpo4 T239W.Fluorescence resonance energy transfer studies of DNA polymerase β: the critical role of fingers domain movements and a novel non-covalent step during nucleotide selection.Effect of A and B metal ion site occupancy on conformational changes in an RB69 DNA polymerase ternary complex.Conformational dynamics of Thermus aquaticus DNA polymerase I during catalysis.DNA conformational changes at the primer-template junction regulate the fidelity of replication by DNA polymerase.Mechanism of inhibition for BMS-791325, a novel non-nucleoside inhibitor of hepatitis C virus NS5B polymerase.Conformational dynamics of a Y-family DNA polymerase during substrate binding and catalysis as revealed by interdomain Förster resonance energy transfer.Single-molecule microscopy reveals new insights into nucleotide selection by DNA polymerase I.Single-molecule investigation of substrate binding kinetics and protein conformational dynamics of a B-family replicative DNA polymerase.Single-molecule measurements of synthesis by DNA polymerase with base-pair resolution.Recent insight into the kinetic mechanisms and conformational dynamics of Y-Family DNA polymerases.Discrimination between right and wrong purine dNTPs by DNA polymerase I from Bacillus stearothermophilus.Interaction of human DNA polymerase alpha and DNA polymerase I from Bacillus stearothermophilus with hypoxanthine and 8-oxoguanine nucleotides.B family DNA polymerases asymmetrically recognize pyrimidines and purines.Effect of N-2-acetylaminofluorene and 2-aminofluorene adducts on DNA binding and synthesis by yeast DNA polymerase eta.dNTP-dependent conformational transitions in the fingers subdomain of Klentaq1 DNA polymerase: insights into the role of the "nucleotide-binding" state.An intramolecular FRET system monitors fingers subdomain opening in Klentaq1.I260Q DNA polymerase β highlights precatalytic conformational rearrangements critical for fidelity

P2860

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P2860

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

http://www.wikidata.org/entity/Q42626728

description

2007 nî lūn-bûn

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2007年の論文

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2007年論文

@yue

2007年論文

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2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

2007年论文

@zh

2007年论文

@zh-cn

name

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@en

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@nl

type

label

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@en

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@nl

prefLabel

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@en

A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@nl

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Journal of Biological Chemistry

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A pre-equilibrium before nucleotide binding limits fingers subdomain closure by Klentaq1.

@en

P2093

Gabriel Waksman

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Paul J Rothwell

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P2860

Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation

Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA.

Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability

Crystal structures of a ddATP-, ddTTP-, ddCTP, and ddGTP- trapped ternary complex of Klentaq1: insights into nucleotide incorporation and selectivity

Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation.

DNA structure and aspartate 276 influence nucleotide binding to human DNA polymerase beta. Implication for the identity of the rate-limiting conformational change.

Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors.

Multiparameter single-molecule fluorescence spectroscopy reveals heterogeneity of HIV-1 reverse transcriptase:primer/template complexes.

Structure and mechanism of DNA polymerases.

Refined model for primer/template binding by HIV-1 reverse transcriptase: pre-steady-state kinetic analyses of primer/template binding and nucleotide incorporation events distinguish between different binding modes depending on the nature of the nuc

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28884-28892

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scholarly article

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10.1074/JBC.M704824200

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39

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282

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2007-07-18T00:00:00Z

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17640877

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