Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A role of basic residues and the putative intercalating phenylalanine of the HMG-1 box B in DNA supercoiling and binding to four-way DNA junctions.

The Journal of biological chemistry - 17 Nov 2000

Stros M, Muselíková E

Abstract excerpt

HMG (high mobility group) 1 is a chromosomal protein with two homologous DNA-binding domains, the HMG boxes A and B. HMG-1, like its individual HMG boxes, can recognize structural distortion of DNA, such as four-way DNA junctions (4WJs), that are very likely to have features common to their natural, yet unknown, cellular binding targets. HMG-1 can also bend/loop DNA and introduce negative supercoils in the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Circular Dichroism
Share to DNA, Superhelical

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA Topoisomerases, Type I

Share to Electrophoresis, Agar Gel

Share to High Mobility Group Proteins

Share to HMGB1 Protein

Share to Phenylalanine

Share to Static Electricity

Source

Identifiers

PMID: 10962007
DOI: 10.1074/jbc.M007167200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A role of basic residues and the putative intercalating phenylalanine of the HMG-1 box B in DNA supercoiling and binding to four-way DNA junctions.PMID 10962007Read ↗

Formation of large nucleoprotein complexes upon binding of the high-mobility-group (HMG) box B-domain of HMG1 protein to supercoiled DNA.Semantic proximity Read ↗

Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA.Semantic proximity Read ↗

HMGB1: The jack‐of‐all‐trades protein is a master DNA repair mechanicSemantic proximity Read ↗

A critical role in structure-specific DNA binding for the acetylatable lysine residues in HMGB1.Semantic proximity Read ↗

Alanine mutagenesis of high-mobility-group-protein-1 box B (HMG1-B).Semantic proximity Read ↗

The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity.Semantic proximity Read ↗

Characterization of the interaction of wheat HMGa with linear and four-way junction DNAs.Semantic proximity Read ↗

HMG box A in HMG2 protein functions as a mediator of DNA structural alteration together with box B.Semantic proximity Read ↗

Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein.Semantic proximity Read ↗

High mobility group protein B1 enhances DNA repair and chromatin modification after DNA damage.Semantic proximity Read ↗

HMGB1-mediated DNA bending: Distinct roles in increasing p53 binding to DNA and the transactivation of p53-responsive gene promoters.Semantic proximity Read ↗

High affinity interaction of dipteran high mobility group (HMG) proteins 1 with DNA is modulated by COOH-terminal regions flanking the HMG box domain.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.