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

Structural basis of Bloom syndrome (BS) causing mutations in the BLM helicase domain.

Molecular medicine (Cambridge, Mass.) - 1 Mar 2000

Rong S B, Väliaho J, Vihinen M

Abstract excerpt

BACKGROUND: Bloom syndrome (BS) is characterized by mutations within the BLM gene. The Bloom syndrome protein (BLM) has similarity to the RecQ subfamily of DNA helicases, which contain seven conserved helicase domains and share significant sequence and structural similarity with the Rep and PcrA DNA helicases. We modeled the three-dimensional structure of the BLM helicase domain to analyze the structural basis of...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Bloom Syndrome
Share to Databases, Factual

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Helicases

Share to Protein Structure, Tertiary

Share to RecQ Helicases

Share to Sequence Homology, Amino Acid

Share to Static Electricity

Source

Open in PubMed Open full text

Identifiers

PMID: 10965492
PMCID: PMC1949943

Genes

BLM

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of Bloom syndrome (BS) causing mutations in the BLM helicase domain.PMID 10965492Read ↗

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

Biochemical Properties of Naturally Occurring Human Bloom Helicase VariantsSemantic proximity Read ↗

Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.Semantic proximity Read ↗

Bloom syndrome and the underlying causes of genetic instability.Semantic proximity Read ↗

Role of the Bloom's syndrome helicase in maintenance of genome stability.Semantic proximity Read ↗

[Bloom syndrome].Semantic proximity Read ↗

Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNA.Semantic proximity Read ↗

The C-terminal domain of the Bloom syndrome DNA helicase is essential for genomic stability.Semantic proximity Read ↗

A case of Bloom syndrome manifesting with therapy-related myelodysplastic syndromes harboring a novel BLM gene variant.Semantic proximity Read ↗

Clinical features of Bloom syndrome and function of the causative gene, BLM helicaseSemantic proximity Read ↗

The DNA helicase activity of BLM is necessary for the correction of the genomic instability of bloom syndrome cells.Semantic proximity Read ↗

Genomic instability and cancer: lessons from analysis of Bloom's syndrome.Semantic proximity Read ↗

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