Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA. - Wikidata - wikimedia - TriplyDB

Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA.

Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA.

http://www.wikidata.org/entity/Q34723624

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Single-molecule approaches embrace molecular cohorts DNA dynamics and single-molecule biology Single-molecule dynamics and mechanisms of metalloregulators and metallochaperones Concentration-dependent exchange of replication protein A on single-stranded DNA revealed by single-molecule imaging Histone H1 compacts DNA under force and during chromatin assembly Physical manipulation of the Escherichia coli chromosome reveals its soft nature Single molecule techniques in DNA repair: a primer Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis.Single molecule fluorescence methodologies for investigating transcription factor binding kinetics to nucleosomes and DNA.Protein dynamics during presynaptic-complex assembly on individual single-stranded DNA molecules DNA topology confers sequence specificity to nonspecific architectural proteins.RPA antagonizes microhomology-mediated repair of DNA double-strand breaks.Extending the range for force calibration in magnetic tweezers Concentration- and chromosome-organization-dependent regulator unbinding from DNA for transcription regulation in living cells.Multivalency governs HP1α association dynamics with the silent chromatin state.DNA-Segment-Facilitated Dissociation of Fis and NHP6A from DNA Detected via Single-Molecule Mechanical Response.Protein dynamics of human RPA and RAD51 on ssDNA during assembly and disassembly of the RAD51 filament.Human RAD52 interactions with replication protein A and the RAD51 presynaptic complex.Forces, fluctuations, and self-organization in the nucleus Single-molecule FRET analysis of DNA binding and bending by yeast HMGB protein Nhp6A Translation initiation factor 3 regulates switching between different modes of ribosomal subunit joining.Optical Methods to Study Protein-DNA Interactions in Vitro and in Living Cells at the Single-Molecule Level.Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends.Single-molecule kinetics reveal microscopic mechanism by which High-Mobility Group B proteins alter DNA flexibility.DNA concentration-dependent dissociation of EcoRI: direct transfer or reaction during hopping.Mechanisms of small molecule-DNA interactions probed by single-molecule force spectroscopy.Facilitated Dissociation of a Nucleoid Protein from the Bacterial Chromosome.Molecular stripping, targets and decoys as modulators of oscillations in the NF-κB/IκBα/DNA genetic network.Nucleosomes accelerate transcription factor dissociation.Single-molecule studies of high-mobility group B architectural DNA bending proteins.Multiple-binding-site mechanism explains concentration-dependent unbinding rates of DNA-binding proteins.Advances in magnetic tweezers for single molecule and cell biophysics.Frequent exchange of the DNA polymerase during bacterial chromosome replication.Single-molecule fluorescence studies on DNA looping Counting proteins bound to a single DNA molecule.Ligand-induced changes of the apparent transition-state position in mechanical protein unfolding Variation of the folding and dynamics of the Escherichia coli chromosome with growth conditions.Binding-rebinding dynamics of proteins interacting nonspecifically with a long DNA molecule.The promoter-search mechanism of Escherichia coli RNA polymerase is dominated by three-dimensional diffusion A general mechanism for competitor-induced dissociation of molecular complexes.

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P2860

Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA.

http://www.wikidata.org/entity/Q34723624

description

2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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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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name

Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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type

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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Nucleic Acids Research

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Concentration-dependent exchan ...... bound to double-stranded DNA.

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P2093

John F Marko

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John S Graham

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Reid C Johnson

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P2860

The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin

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

The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding

Flexible DNA bending in HU-DNA cocrystal structures

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

Near-field-magnetic-tweezer manipulation of single DNA molecules.

The HU regulon is composed of genes responding to anaerobiosis, acid stress, high osmolarity and SOS induction.

Nhp6: a small but powerful effector of chromatin structure in Saccharomyces cerevisiae

Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid

Mechanism of interaction between single-stranded DNA binding protein and DNA

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2249-2259

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scholarly article

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10.1093/NAR/GKQ1140

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6

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39

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2010-11-21T00:00:00Z

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49629070

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21097894

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3064784

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