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 data-driven structural model of hSSB1 (NABP2/OBFC2B) self-oligomerization.

Nucleic acids research - 21 Aug 2017

Touma Christine, Adams Mark N, Ashton Nicholas W, Mizzi Michael, El-Kamand Serene, Richard Derek J, Cubeddu Liza, Gamsjaeger Roland

Abstract excerpt

The maintenance of genome stability depends on the ability of the cell to repair DNA efficiently. Single-stranded DNA binding proteins (SSBs) play an important role in DNA processing events such as replication, recombination and repair. While the role of human single-stranded DNA binding protein 1 (hSSB1/NABP2/OBFC2B) in the repair of double-stranded breaks has been well established, we have recently shown that...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine
Share to DNA, Single-Stranded

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Magnetic Resonance Spectroscopy

Share to Mitochondrial Proteins

Share to Protein Multimerization

Share to Protein Structure, Quaternary

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 28609781
DOI: 10.1093/nar/gkx526
PMCID: PMC5737504

Genes

NABP2
SSB

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A data-driven structural model of hSSB1 (NABP2/OBFC2B) self-oligomerization.PMID 28609781Read ↗

A biophysical and structural analysis of DNA binding by oligomeric hSSB1 (NABP2/OBFC2B)Semantic proximity Read ↗

Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of “quasi-ordered” statesSemantic proximity Read ↗

Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer PlasticitySemantic proximity Read ↗

The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70.Semantic proximity Read ↗

The Impact of Single-Stranded DNA-Binding Protein SSB and Putative SSB-Interacting Proteins on Genome Integrity in the Thermophilic Crenarchaeon Sulfolobus acidocaldarius.Semantic proximity Read ↗

DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity.Semantic proximity Read ↗

The H-NS dimerization domain defines a new fold contributing to DNA recognition.Semantic proximity Read ↗

Activation mechanism of Small Heat Shock Protein HSPB5 revealed by disease-associated mutantsSemantic proximity Read ↗

Characterization of a single-stranded DNA-binding protein from Klebsiella pneumoniae: mutation at either Arg73 or Ser76 causes a less cooperative complex on DNA.Semantic proximity Read ↗

Understanding of the activity of a protein involved in DNA repair by biochemical, structural and <i>in silico</i> approachesSemantic proximity Read ↗

hSSB1 interacts directly with the MRN complex stimulating its recruitment to DNA double-strand breaks and its endo-nuclease activity.Semantic proximity Read ↗

Tertiary structure and conformational dynamics of the anti-amyloidogenic chaperone DNAJB6b at atomistic resolutionSemantic proximity Read ↗

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