Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.

about

The ring-shaped hexameric helicases that function at DNA replication forks.Helicase promotes replication re-initiation from an RNA transcript.

P2860

Q48146728-5BE1EFBD-2828-4D91-BB29-027B5D85466F Q55262145-9F37D0D2-5172-43AE-8EAC-E04920AA304B

P2860

Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.

Item

http://www.wikidata.org/entity/Q38949218

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

@wuu

2017年论文

@zh

2017年论文

@zh-cn

name

Cryo-EM structure of the repli ...... ns coordinating DNA synthesis.

@en

type

Item

label

Cryo-EM structure of the repli ...... ns coordinating DNA synthesis.

@en

prefLabel

Cryo-EM structure of the repli ...... ns coordinating DNA synthesis.

@en

P1476

Cryo-EM structure of the repli ...... ns coordinating DNA synthesis.

@en

P2093

Arkadiusz W Kulczyk

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

Charles C Richardson

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

Peter Meyer

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

P2860

The architecture of a eukaryotic replisome.

Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.

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

Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7

Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis

The crystal structure of the bifunctional primase-helicase of bacteriophage T7

Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution

DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase

DNA-induced switch from independent to sequential dTTP hydrolysis in the bacteriophage T7 DNA helicase

P304

E1848-E1856

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

P31

scholarly article

P356

10.1073/PNAS.1701252114

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

P407

English

P433

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

P478

114

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

P50

Piotr Sliz

Arne Möller

P577

2017-02-21T00:00:00Z

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

P698

28223502

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

P921

cryogenic electron microscopy

P932

5347612

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

Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.

about

P2860

P2860

Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932