(Q74486176)

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Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC

scientific article published on 01 April 1998

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11 November 2019

Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC (English)

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11 November 2019

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C San Martin

1

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11 November 2019

M Radermacher

2

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11 November 2019

B Wolpensinger

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11 November 2019

A Engel

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11 November 2019

C S Miles

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11 November 2019

N E Dixon

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11 November 2019

J M Carazo

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11 November 2019

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1 April 1998

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11 November 2019

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11 November 2019

6

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11 November 2019

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11 November 2019

501-509

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11 November 2019

Mechanisms of helicase-catalyzed DNA unwinding

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A structural model for the Escherichia coli DnaB helicase based on electron microscopy data.

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The HexamericE. coliDnaB Helicase can Exist in Different Quarternary States

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Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs.

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Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer.

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Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with a replication fork

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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases

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Identifiers

10.1016/S0969-2126(98)00051-3

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9562559%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9562559%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

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