A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
about
Structures of coxsackievirus, rhinovirus, and poliovirus polymerase elongation complexes solved by engineering RNA mediated crystal contactsPerturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongationStructural basis of viral RNA-dependent RNA polymerase catalysis and translocationHigh-throughput screening identification of poliovirus RNA-dependent RNA polymerase inhibitorsStructure-function relationships underlying the replication fidelity of viral RNA-dependent RNA polymerases.Coxsackievirus B3 mutator strains are attenuated in vivo.Design of a Genetically Stable High Fidelity Coxsackievirus B3 Polymerase That Attenuates Virus Growth in Vivo.SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication.Polymerase/DNA interactions and enzymatic activity: multi-parameter analysis with electro-switchable biosurfaces.Streamlined determination of processive run length and mechanochemical coupling of nucleic acid motor activities.Understanding the Mechanism of the Broad-Spectrum Antiviral Activity of Favipiravir (T-705): Key Role of the F1 Motif of the Viral Polymerase.An in vitro fluorescence based study of initiation of RNA synthesis by influenza B polymerase.ATP Is an Allosteric Inhibitor of Coxsackievirus B3 Polymerase.Poliovirus polymerase residue 5 plays a critical role in elongation complex stability.A template RNA entry channel in the fingers domain of the poliovirus polymerase.Measurement of incorporation kinetics of non-fluorescent native nucleotides by DNA polymerases using fluorescence microscopy.
P2860
Q27678100-F2513504-2132-4109-A496-A4E9BFF80612Q28651848-4F5A97F0-33CD-4648-9AD3-1A1DA61DF01CQ28829956-D4914623-5531-4A06-A90E-4CE7FED93E93Q33948876-EEE02CCC-8A21-46F3-B3B1-3336C12451E2Q34992586-011DC4CE-0A3F-4672-96B4-498A09C48511Q36187182-C945225F-F2C3-4062-B606-5980B7FECACCQ37065691-AC04F3B6-9A4F-47CE-94BB-35327D1CF0D0Q37415451-2EF4605F-4002-49A6-8365-610A8014F538Q38984819-BD8E3197-6243-4A48-9F2E-99F4A5766157Q39987218-DF7DAE48-34A7-457C-B94C-9C118C6D5319Q40255981-DB448604-9B85-471A-AACF-56D5C571E290Q40362747-9C089C5B-1EFC-4581-A27B-D4A17796E9F7Q40693100-4FDBB390-813C-43B0-8979-02341C0FC1A1Q41807692-4AD8F220-A4B1-42FD-BD7E-67666BA76812Q42548730-0A9E41BD-A477-4814-981B-748168F41F0DQ46840914-5C4AD1E0-943D-4652-BFA5-E265655145FF
P2860
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 03 May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
@en
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates.
@nl
type
label
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
@en
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates.
@nl
prefLabel
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
@en
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates.
@nl
P2093
P2860
P356
P1476
A quantitative stopped-flow fluorescence assay for measuring polymerase elongation rates
@en
P2093
Grace Campagnola
Olve B Peersen
P2860
P356
10.1016/J.AB.2009.04.035
P407
P577
2009-05-03T00:00:00Z