about
DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin.Role of the acidic tail of high mobility group protein B1 (HMGB1) in protein stability and DNA bendingCharacterization of an Entamoeba histolytica high-mobility-group box protein induced during intestinal infection.HMGB1: the jack-of-all-trades protein is a master DNA repair mechanic.Biophysical characterization of DNA binding from single molecule force measurementsSingle-molecule analysis of RAG-mediated V(D)J DNA cleavage.High-resolution mapping of architectural DNA binding protein facilitation of a DNA repression loop in Escherichia coli.Mitochondrial transcription factor A serves as a danger signal by augmenting plasmacytoid dendritic cell responses to DNA.DNA-Segment-Facilitated Dissociation of Fis and NHP6A from DNA Detected via Single-Molecule Mechanical Response.Single-molecule FRET analysis of DNA binding and bending by yeast HMGB protein Nhp6ASingle-molecule kinetics reveal microscopic mechanism by which High-Mobility Group B proteins alter DNA flexibility.Mechanism of DNA flexibility enhancement by HMGB proteins.Distinct double- and single-stranded DNA binding of E. coli replicative DNA polymerase III alpha subunit.Optical tweezers experiments resolve distinct modes of DNA-protein binding.Single-molecule studies of high-mobility group B architectural DNA bending proteins.Feeling inter- or intramolecular interactions with the polymer chain as probe: recent progress in SMFS studies on macromolecular interactions.High mobility group box 1 promotes tumor cell migration through epigenetic silencing of semaphorin 3A.The HMGB1 C-Terminal Tail Regulates DNA BendingEukaryotic HMGB proteins as replacements for HU in E. coli repression loop formation.Determination of the number of proteins bound non-specifically to DNA.Basic N-terminus of yeast Nhp6A regulates the mechanism of its DNA flexibility enhancementUnderstanding apparent DNA flexibility enhancement by HU and HMGB architectural proteinsDNA stretching as a probe for nucleic acid interactions: Reply to Comments on "Biophysical characterization of DNA binding from single molecule force measurements" by Kathy R. Chaurasiya, Thayaparan Paramanathan, Micah J. McCauley, Mark C. Williams.Enhancement of DNA flexibility in vitro and in vivo by HMGB box A proteins carrying box B residues.Protein Flexibility and Synergy of HMG Domains Underlie U-Turn Bending of DNA by TFAM in Solution.
P2860
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P2860
description
2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2007
@ast
im Dezember 2007 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2007/12/07)
@sk
vědecký článek publikovaný v roce 2007
@cs
wetenschappelijk artikel (gepubliceerd op 2007/12/07)
@nl
наукова стаття, опублікована в грудні 2007
@uk
مقالة علمية (نشرت في 7-12-2007)
@ar
name
HMGB binding to DNA: single and double box motifs
@ast
HMGB binding to DNA: single and double box motifs
@en
HMGB binding to DNA: single and double box motifs
@nl
type
label
HMGB binding to DNA: single and double box motifs
@ast
HMGB binding to DNA: single and double box motifs
@en
HMGB binding to DNA: single and double box motifs
@nl
prefLabel
HMGB binding to DNA: single and double box motifs
@ast
HMGB binding to DNA: single and double box motifs
@en
HMGB binding to DNA: single and double box motifs
@nl
P2093
P2860
P1476
HMGB binding to DNA: single and double box motifs
@en
P2093
Jeff Zimmerman
L James Maher
Micah J McCauley
P2860
P304
P356
10.1016/J.JMB.2007.09.073
P407
P577
2007-09-29T00:00:00Z