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

Biochemical characterization of the structure-specific DNA-binding protein Cmb1 from Schizosaccharomyces pombe.

Journal of molecular biology - 22 Jun 2001

Sassoon J, Lilie H, Baumann U, Kohli J

Abstract excerpt

Cmb1, a novel HMG box protein from Schizosaccharomyces pombe, has been characterized biochemically using glutaraldehyde cross-linking, gel-filtration and analytical ultracentrifugation. It was identified as a monomeric, non-spherical protein, with a tendency to aggregate in solution. Limited prot...

Read the complete abstract on PubMed

Topics

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

Share to Base Pair Mismatch
Share to Chromatography, Gel
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cross-Linking Reagents

Share to High Mobility Group Proteins

Share to Schizosaccharomyces pombe Proteins

Share to Solutions

Share to Ultracentrifugation

Source

Identifiers

PMID: 11399082
DOI: 10.1006/jmbi.2001.4723

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026. Prepared record publication-11399082-2026-08-31.1. Manifest publication-graph-cohort-2026-08-31.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 31 Aug 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Biochemical characterization of the structure-specific DNA-binding protein Cmb1 from Schizosaccharomyces pombe.PMID 11399082Read ↗

Mutagenesis of the HMGB (high-mobility group B) protein Cmb1 (cytosine-mismatch binding 1) of Schizosaccharomyces pombe: effects on recognition of DNA mismatches and damage.Semantic proximity Read ↗

Evidence for Involvement of HMGB1 Protein in Human DNA Mismatch RepairSemantic proximity Read ↗

Mismatch repair in Schizosaccharomyces pombe requires the mutL homologous gene pms1: molecular cloning and functional analysis.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 ↗

O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.Semantic proximity Read ↗

Identification of two mismatch-binding activities in protein extracts of Schizosaccharomyces pombe.Semantic proximity Read ↗

Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase.Semantic proximity Read ↗

Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein.Semantic proximity Read ↗

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 ↗

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.Semantic proximity Read ↗

Oligomerization of Hmo1 mediated by box A is essential for DNA binding in vitro and in vivo.Semantic proximity Read ↗

Cdm1, the smallest subunit of DNA polymerase d in the fission yeast Schizosaccharomyces pombe, is non-essential for growth and division.Semantic proximity Read ↗

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