Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

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StpA and Hha stimulate pausing by RNA polymerase by promoting DNA-DNA bridging of H-NS filaments.Modulation of H-NS transcriptional silencing by magnesium.A single molecule analysis of H-NS uncouples DNA binding affinity from DNA specificity

P2860

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P2860

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

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http://www.wikidata.org/entity/Q47433869

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2017 nî lūn-bûn

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2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh-hant

name

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

@en

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

@nl

type

Item

label

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

@en

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

@nl

prefLabel

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

@en

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

@nl

P1476

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells

@en

P2093

Jie Yan

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

Qingnan Tang

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

Ricksen S Winardhi

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

Yunfeng Gao

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

P2860

How do site-specific DNA-binding proteins find their targets?

Chromosome organization by a nucleoid-associated protein in live bacteria

Live-cell superresolution microscopy reveals the organization of RNA polymerase in the bacterial nucleoid

H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein

The H-NS dimerization domain defines a new fold contributing to DNA recognition

Functional Specificity of a Hox Protein Mediated by the Recognition of Minor Groove Structure

H-NS forms a superhelical protein scaffold for DNA condensation

Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins

Indirect DNA Readout by an H-NS Related Protein: Structure of the DNA Complex of the C-Terminal Domain of Ler

Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from Escherichia coli

P304

12560-12565

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

P31

scholarly article

P356

10.1073/PNAS.1716721114

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

Linda J Kenney

Yong Hwee Foo

P577

2017-11-06T00:00:00Z

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

P698

29109287

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

P932

5703333

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

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

about

P2860

P2860

Charged residues in the H-NS linker drive DNA binding and gene silencing in single cells.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932