Thermodynamic and molecular analysis of the AbrB-binding sites within the phyC-region of Bacillus amyloliquefaciens FZB45.

about

Substitutional analysis of the C-terminal domain of AbrB revealed its essential role in DNA-binding activity.

P2860

Q35169416-68B60AEB-9FC9-4985-9E88-AC3216BB37E7

P2860

Thermodynamic and molecular analysis of the AbrB-binding sites within the phyC-region of Bacillus amyloliquefaciens FZB45.

Item

http://www.wikidata.org/entity/Q38329364

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年学术文章

@wuu

2011年学术文章

@zh-cn

2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Thermodynamic and molecular an ...... amyloliquefaciens FZB45.

@en

type

Item

label

Thermodynamic and molecular an ...... amyloliquefaciens FZB45.

@en

prefLabel

Thermodynamic and molecular an ...... amyloliquefaciens FZB45.

@en

P1476

Thermodynamic and molecular an ...... amyloliquefaciens FZB45.

@en

P2093

Oliwia Makarewicz

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

Rainer Borriss

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

Svetlana Neubauer

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

P2860

Insights into the Nature of DNA Binding of AbrB-like Transcription Factors

AbrB-like transcription factors assume a swapped hairpin fold that is evolutionarily related to double-psi beta barrels.

DNA-binding activity of amino-terminal domains of the Bacillus subtilis AbrB protein

Independent and interchangeable multimerization domains of the AbrB, Abh, and SpoVT global regulatory proteins.

Bacillus subtilis sporulation and stationary phase gene expression.

Dual role of the PhoP approximately P response regulator: Bacillus amyloliquefaciens FZB45 phytase gene transcription is directed by positive and negative interactions with the phyC promoter.

NMR structure of AbhN and comparison with AbrBN: FIRST insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins

In vitro binding affinity of the Bacillus subtilis AbrB protein to six different DNA target regions.

Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote

Regulation of Bacillus subtilis sigmaH (spo0H) and AbrB in response to changes in external pH.

P2888

s00438-011-0666-4

P304

111-122

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

P31

scholarly article

P356

10.1007/S00438-011-0666-4

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

P433

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

P478

287

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

P577

2011-12-20T00:00:00Z

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

P5875

51901450

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

P698

22183144

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

Thermodynamic and molecular analysis of the AbrB-binding sites within the phyC-region of Bacillus amyloliquefaciens FZB45.

about

P2860

P2860

Thermodynamic and molecular analysis of the AbrB-binding sites within the phyC-region of Bacillus amyloliquefaciens FZB45.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P5875

P698