Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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The nucleoid protein Dps binds genomic DNA of Escherichia coli in a non-random manner.The Oligomeric Form of the Escherichia coli Dps Protein Depends on the Availability of Iron Ions.

P2860

Q41363557-3059C8DA-B221-455A-8B6B-B9A1B80F706E Q47430379-7E21D5C8-181E-43F2-B19D-F5BE62B5AC51

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Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

@ast

Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

@ast

Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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P1476

Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

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P2093

Alexander A Timchenko

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

Diana V Burkova

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

Elena V Preobrazhenskaya

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

Olga N Ozoline

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

Uliana S Shvyreva

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

Valiriy G Artiukhov

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

Vladislav V Melekhov

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P2860

Structure of the Escherichia coli leucine-responsive regulatory protein Lrp reveals a novel octameric assembly

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

The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties

Structural studies on the second Mycobacterium smegmatis Dps: invariant and variable features of structure, assembly and function

The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding

The shape of the DNA minor groove directs binding by the DNA-bending protein Fis

The design involved in PapI and Lrp regulation of the pap operon

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

Crystal structure of an IHF-DNA complex: a protein-induced DNA U-turn

The crystal structure of Dps, a ferritin homolog that binds and protects DNA

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e0126504

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scholarly article

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10.1371/JOURNAL.PONE.0126504

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English

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

P478

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

P50

Maria N Tutukina

Sergey Antipov

P577

2015-05-15T00:00:00Z

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

P5875

277896665

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25978038

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P932

4433220

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Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

about

P2860

P2860

Modes of Escherichia coli Dps Interaction with DNA as Revealed by Atomic Force Microscopy

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932