Isolation and characterization of suppressors of two Escherichia coli dnaG mutations, dnaG2903 and parB.

Item

http://www.wikidata.org/entity/Q42967541

description

1997 nî lūn-bûn

@nan

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

1997年论文

@zh

1997年论文

@zh-cn

name

Isolation and characterization ...... mutations, dnaG2903 and parB.

@en

Isolation and characterization ...... mutations, dnaG2903 and parB.

@nl

type

Item

label

Isolation and characterization ...... mutations, dnaG2903 and parB.

@en

Isolation and characterization ...... mutations, dnaG2903 and parB.

@nl

prefLabel

Isolation and characterization ...... mutations, dnaG2903 and parB.

@en

Isolation and characterization ...... mutations, dnaG2903 and parB.

@nl

P1476

Isolation and characterization ...... mutations, dnaG2903 and parB.

@en

P2093

Britton RA

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

Lupski JR

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

P2860

Conditional mutations in the yeast DNA primase genes affect different aspects of DNA metabolism and interactions in the DNA polymerase alpha-primase complex.

The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library

Antimutator mutations in the alpha subunit of Escherichia coli DNA polymerase III: identification of the responsible mutations and alignment with other DNA polymerases

Prokaryotic DNA replication.

Domains of Escherichia coli primase: functional activity of a 47-kDa N-terminal proteolytic fragment

Determination of the precise location and orientation of the Escherichia coli dnaE gene

Phenethyl alcohol resistance in Escherichia coli. 3. A temperature-sensitive mutation(dnaP) affecting DNA replication.

A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli.

Initiation of enzymatic replication at the origin of the Escherichia coli chromosome: primase as the sole priming enzyme

Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork.

P304

867-875

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

P31

scholarly article

P407

English

P433

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

P478

145

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

P577

1997-04-01T00:00:00Z

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

P698

9093842

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

P932

1207892

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