Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase - Wikidata - awgldk - TriplyDB

Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

http://www.wikidata.org/entity/Q35590981

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Molecular traffic jams on DNA Towards physiological complexity with in vitro single-molecule biophysics DNA dynamics and single-molecule biology Structural insights into regulation and action of SWI2/SNF2 ATPases How RecBCD enzyme and Chi promote DNA break repair and recombination: a molecular biologist's view High-Throughput Universal DNA Curtain Arrays for Single-Molecule Fluorescence Imaging High-throughput single-molecule studies of protein-DNA interactions.Coherent optical spectroscopy in a biological semiconductor quantum dot-DNA hybrid system PcrA-mediated disruption of RecA nucleoprotein filaments--essential role of the ATPase activity of RecA Toward detection of DNA-bound proteins using solid-state nanopores: insights from computer simulations.Visualizing protein movement on DNA at the single-molecule level using DNA curtains Insights into the glycosylase search for damage from single-molecule fluorescence microscopy.Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate.Efficient modification of λ-DNA substrates for single-molecule studies.ParB spreading requires DNA bridging.Novel function of the Fanconi anemia group J or RECQ1 helicase to disrupt protein-DNA complexes in a replication protein A-stimulated manner.DNA interrogation by the CRISPR RNA-guided endonuclease Cas9.End resection at double-strand breaks: mechanism and regulation.Pif1 regulates telomere length by preferentially removing telomerase from long telomere ends Dark-field illumination on zero-mode waveguide/microfluidic hybrid chip reveals T4 replisomal protein interactions Mu transpososome and RecBCD nuclease collaborate in the repair of simple Mu insertions.Measuring intermolecular rupture forces with a combined TIRF-optical trap microscope and DNA curtains The RSC chromatin remodelling ATPase translocates DNA with high force and small step size.Nanofabrication for the analysis and manipulation of membranes.Exploring translocation of proteins on DNA by NMR Single-molecule studies of transcription: from one RNA polymerase at a time to the gene expression profile of a cell.Quantum dots find their stride in single molecule tracking.DNA motion capture reveals the mechanical properties of DNA at the mesoscale Single-molecule imaging reveals the mechanism of Exo1 regulation by single-stranded DNA binding proteins.Chromosome demise in the wake of ligase-deficient replication.The impact of DNA intercalators on DNA and DNA-processing enzymes elucidated through force-dependent binding kinetics.FRET studies of a landscape of Lac repressor-mediated DNA loops Combined versatile high-resolution optical tweezers and single-molecule fluorescence microscopy Single-stranded DNA curtains for real-time single-molecule visualization of protein-nucleic acid interactions.Assembly of DNA curtains using hydrogen silsesquioxane as a barrier to lipid diffusion.A method for labeling proteins with tags at the native genomic loci in budding yeast Dynamic DNA binding licenses a repair factor to bypass roadblocks in search of DNA lesions.Optical Methods to Study Protein-DNA Interactions in Vitro and in Living Cells at the Single-Molecule Level.Real-time single-molecule imaging reveals a direct interaction between UvrC and UvrB on DNA tightropes.Chemo-mechanical pushing of proteins along single-stranded DNA.

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

http://www.wikidata.org/entity/Q35590981

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2010 nî lūn-bûn

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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2010年论文

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2010年论文

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name

Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

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Eric C Greene

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

Ilya J Finkelstein

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

Mari-Liis Visnapuu

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

P2860

RecBCD enzyme switches lead motor subunits in response to chi recognition

RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity

Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks

DNA helicase Srs2 disrupts the Rad51 presynaptic filament

Processive translocation and DNA unwinding by individual RecBCD enzyme molecules.

Functional modulation of Escherichia coli RNA polymerase.

Probing transcription factor dynamics at the single-molecule level in a living cell.

Displacement of a DNA binding protein by Dda helicase

Visualizing single DNA-bound proteins using DNA as a scanning probe.

Characterization of elongating T7 and SP6 RNA polymerases and their response to a roadblock generated by a site-specific DNA binding protein.

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983-987

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scholarly article

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10.1038/NATURE09561

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7326

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468

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2010-11-24T00:00:00Z

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49635505

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1049552724

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21107319

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3230117

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