The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling. - Wikidata - awgldk - TriplyDB

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

http://www.wikidata.org/entity/Q37357506

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Structural and functional analyses of disease-causing missense mutations in Bloom syndrome protein Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase Structural basis of mechanochemical coupling in a hexameric molecular motor The hexameric helicase DnaB adopts a nonplanar conformation during translocation.It takes two to tango: defining an essential second active site in pyridoxal 5'-phosphate synthase.Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension Molecular basis for recognition of nucleoside triphosphate by gene 4 helicase of bacteriophage T7.The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target The glutamate switch of bacteriophage T7 DNA helicase: role in coupling nucleotide triphosphate (NTP) and DNA binding to NTP hydrolysis.Coupling dTTP hydrolysis with DNA unwinding by the DNA helicase of bacteriophage T7.The arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling.Multimeric BLM is dissociated upon ATP hydrolysis and functions as monomers in resolving DNA structures Understanding helicases as a means of virus control.Mechanisms of a ring shaped helicase Physiological and biochemical defects in carboxyl-terminal mutants of mitochondrial DNA helicase.On helicases and other motor proteins.Multiple active centers of multi-subunit RNA polymerases.Promiscuous usage of nucleotides by the DNA helicase of bacteriophage T7: determinants of nucleotide specificity.Structure of the hexameric HerA ATPase reveals a mechanism of translocation-coupled DNA-end processing in archaea.Defective dissociation of a "slow" RecA mutant protein imparts an Escherichia coli growth defect.Complementation of one RecA protein point mutation by another. Evidence for trans catalysis of ATP hydrolysis.Hybrid Methods Reveal Multiple Flexibly Linked DNA Polymerases within the Bacteriophage T7 Replisome.Disorder-order folding transitions underlie catalysis in the helicase motor of SecA

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The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

http://www.wikidata.org/entity/Q37357506

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on March 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@en

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@nl

type

label

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@en

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@nl

prefLabel

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@en

The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@nl

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PNAS.0400968101

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Proceedings of the National Academy of Sciences of the United States of America

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The arginine finger of bacteriophage T7 gene 4 helicase: role in energy coupling.

@en

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Charles C Richardson

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Donald E Johnson

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Donald J Crampton

http://www.w3.org/2001/XMLSchema#string

Shenyuan Guo

http://www.w3.org/2001/XMLSchema#string

P2860

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Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase

Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7

Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

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4373-4378

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scholarly article

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10.1073/PNAS.0400968101

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13

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101

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2004-03-01T00:00:00Z

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8630497

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384754

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