Probing protein-DNA interactions by unzipping a single DNA double helix. - Test2 - elhamkhani - TriplyDB

Probing protein-DNA interactions by unzipping a single DNA double helix.

Probing protein-DNA interactions by unzipping a single DNA double helix.

http://www.wikidata.org/entity/Q34178541

about

Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase Optical trapping.Determination of protein-DNA binding constants and specificities from statistical analyses of single molecules: MutS-DNA interactions A257T linker region mutant of T7 helicase-primase protein is defective in DNA loading and rescued by T7 DNA polymerase Impediment of E. coli UvrD by DNA-destabilizing force reveals a strained-inchworm mechanism of DNA unwinding High-resolution, single-molecule measurements of biomolecular motion.DNA Y structure: a versatile, multidimensional single molecule assay.Detection of forces and displacements along the axial direction in an optical trap Unzipping single DNA molecules to study nucleosome structure and dynamics.Probing single-stranded DNA conformational flexibility using fluorescence spectroscopy A sticky chain model of the elongation and unfolding of Escherichia coli P pili under stress Mg2+-induced compaction of single RNA molecules monitored by tethered particle microscopy A force-based, parallel assay for the quantification of protein-DNA interactions.Parallel force assay for protein-protein interactions.Probing ribosomal protein-RNA interactions with an external force.In vitro analysis of DNA-protein interactions by proximity ligation.Dynamic regulation of transcription factors by nucleosome remodeling Biocompatible and High Stiffness Nanophotonic Trap Array for Precise and Versatile Manipulation Optical Methods to Study Protein-DNA Interactions in Vitro and in Living Cells at the Single-Molecule Level.Analyzing the forces binding a restriction endonuclease to DNA using a synthetic nanopore Quantitative detection of small molecule/DNA complexes employing a force-based and label-free DNA-microarray.DNA looping mediates nucleosome transfer.Structural destabilization of DNA duplexes containing single-base lesions investigated by nanopore measurements DNA-protein binding force chip.Label-free free-solution nanoaperture optical tweezers for single molecule protein studies.ATP-induced helicase slippage reveals highly coordinated subunits.LexA-DNA bond strength by single molecule force spectroscopy.Dynamics of the DNA duplex formation studied by single molecule force measurements.Double nanohole optical tweezers visualize protein p53 suppressing unzipping of single DNA-hairpins.Single molecule high-throughput footprinting of small and large DNA ligands High-resolution dynamic mapping of histone-DNA interactions in a nucleosome.Single-molecule unzipping force analysis of HU-DNA complexes Single-molecule measurements of the CCR5 mRNA unfolding pathways.Synergistic action of RNA polymerases in overcoming the nucleosomal barrier.Single-molecule kinetics and footprinting of DNA bis-intercalation: the paradigmatic case of Thiocoraline.Intrinsic fluctuations lead to broad range of transduced forces in tethered-bead single-molecule experiments.Single-molecule DNA unzipping reveals asymmetric modulation of a transcription factor by its binding site sequence and context.Experimental measurement of binding energy, selectivity, and allostery using fluctuation theorems.A high throughput molecular force assay for protein-DNA interactions.Dynamic force spectroscopy of protein-DNA interactions by unzipping DNA.

P2860

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P2860

Probing protein-DNA interactions by unzipping a single DNA double helix.

http://www.wikidata.org/entity/Q34178541

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Probing protein-DNA interactions by unzipping a single DNA double helix.

@ast

Probing protein-DNA interactions by unzipping a single DNA double helix.

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Probing protein-DNA interactions by unzipping a single DNA double helix.

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type

label

Probing protein-DNA interactions by unzipping a single DNA double helix.

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Probing protein-DNA interactions by unzipping a single DNA double helix.

@en

Probing protein-DNA interactions by unzipping a single DNA double helix.

@nl

prefLabel

Probing protein-DNA interactions by unzipping a single DNA double helix.

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Probing protein-DNA interactions by unzipping a single DNA double helix.

@en

Probing protein-DNA interactions by unzipping a single DNA double helix.

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S0006-3495(02)75233-8

P1433

Biophysical Journal

P1476

Probing protein-DNA interactions by unzipping a single DNA double helix.

@en

P2093

Alla Shundrovsky

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

Benjamin C Jantzen

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

Michelle D Wang

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

Steven J Koch

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

P2860

Mechanical separation of the complementary strands of DNA.

Restriction enzyme BsoBI-DNA complex: a tunnel for recognition of degenerate DNA sequences and potential histidine catalysis

Stretching DNA with optical tweezers.

Whole-genome shotgun optical mapping of Deinococcus radiodurans.

Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure.

Processive translocation and DNA unwinding by individual RecBCD enzyme molecules.

High-resolution restriction maps of bacterial artificial chromosomes constructed by optical mapping

Transcription by single molecules of RNA polymerase observed by light microscopy.

Single-molecule studies of the effect of template tension on T7 DNA polymerase activity.

Mechanical disruption of individual nucleosomes reveals a reversible multistage release of DNA.

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1098-1105

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scholarly article

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10.1016/S0006-3495(02)75233-8

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2

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83

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2002-08-01T00:00:00Z

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11255298

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12124289

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1302211

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