Structure of the replication terminus-terminator protein complex as probed by affinity cleavage. - Wikidata - awgldk - TriplyDB

Structure of the replication terminus-terminator protein complex as probed by affinity cleavage.

Structure of the replication terminus-terminator protein complex as probed by affinity cleavage.

http://www.wikidata.org/entity/Q37289061

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Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase.A 3D puzzle approach to building protein-DNA structures.Termination of DNA replication of bacterial and plasmid chromosomes.Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex.Bordetella pertussis fim3 gene regulation by BvgA: phosphorylation controls the formation of inactive vs. active transcription complexes.Mechanistic insights into replication termination as revealed by investigations of the Reb1-Ter3 complex of Schizosaccharomyces pombe.Architecture of the bacteriophage T4 activator MotA/promoter DNA interaction during sigma appropriation A single domain of the replication termination protein of Bacillus subtilis is involved in arresting both DnaB helicase and RNA polymerase.

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P2860

Structure of the replication terminus-terminator protein complex as probed by affinity cleavage.

http://www.wikidata.org/entity/Q37289061

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on October 1996

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Structure of the replication t ...... s probed by affinity cleavage.

@en

Structure of the replication t ...... s probed by affinity cleavage.

@nl

type

label

Structure of the replication t ...... s probed by affinity cleavage.

@en

Structure of the replication t ...... s probed by affinity cleavage.

@nl

prefLabel

Structure of the replication t ...... s probed by affinity cleavage.

@en

Structure of the replication t ...... s probed by affinity cleavage.

@nl

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PNAS.93.20.10647

P1433

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

P1476

Structure of the replication t ...... s probed by affinity cleavage.

@en

P2093

D Bastia

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

D E Bussiere

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

F Wang

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

K S Pai

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

S W White

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

P2860

Crystal structure of the replication terminator protein from B. subtilis at 2.6 A

Sequential replication of Bacillus subtilis chromosome. I. Comparison of marker frequencies in exponential and stationary growth phases

Sequential replication of the Bacillus subtilis chromosome. II. Isotopic transfer experiments.

The relationship between sequence-specific termination of DNA replication and transcription.

The replication terminator protein of the gram-positive bacterium Bacillus subtilis functions as a polar contrahelicase in gram-negative Escherichia coli

Orientation of the LexA DNA-binding motif on operator DNA as inferred from cysteine-mediated phenyl azide crosslinking.

Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelate

Efficient site-directed mutagenesis using uracil-containing DNA.

The dimer-dimer interaction surface of the replication terminator protein of Bacillus subtilis and termination of DNA replication.

Termination of DNA replication in vitro: requirement for stereospecific interaction between two dimers of the replication terminator protein of Bacillus subtilis and with the terminator site to elicit polar contrahelicase and fork impedance.

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10647-10652

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scholarly article

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10.1073/PNAS.93.20.10647

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1996-10-01T00:00:00Z

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14350674

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P698

8855233

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P921

protein structure

P932

38208

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