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Visualizing the Path of DNA through Proteins Using DREEM Imaging.

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

http://www.wikidata.org/entity/Q37592119

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Of Rings and Rods: Regulating Cohesin Entrapment of DNA to Generate Intra- and Intermolecular Tethers Enhanced electrostatic force microscopy reveals higher-order DNA looping mediated by the telomeric protein TRF2.TRF2-Mediated Control of Telomere DNA Topology as a Mechanism for Chromosome-End Protection Studying protein-DNA interactions using atomic force microscopy.Nucleosome-like, Single-stranded DNA (ssDNA)-Histone Octamer Complexes and the Implication for DNA Double Strand Break Repair.Using Atomic Force Microscopy to Characterize the Conformational Properties of Proteins and Protein-DNA Complexes That Carry Out DNA Repair.A model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes

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Visualizing the Path of DNA through Proteins Using DREEM Imaging.

http://www.wikidata.org/entity/Q37592119

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 06 January 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

@en

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

@nl

type

label

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

@en

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

@nl

prefLabel

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

@en

Visualizing the Path of DNA through Proteins Using DREEM Imaging.

@nl

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J.MOLCEL.2015.12.012

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Visualizing the Path of DNA through Proteins Using DREEM Imaging.

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Dong Wu

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Dorothy A Erie

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Hong Wang

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Kira C Bradford

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Parminder Kaur

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Zimeng M Li

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P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis.

New insights into nucleosome and chromatin structure: an ordered state or a disordered affair?

Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch

Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo

Structure of the human MutSalpha DNA lesion recognition complex

Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair

Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.

Molecular architecture of a eukaryotic translational initiation complex.

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315-323

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scholarly article

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10.1016/J.MOLCEL.2015.12.012

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