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

XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations.

Cell - 30 May 2008

Fan Li, Fuss Jill O, Cheng Quen J, Arvai Andrew S, Hammel Michal, Roberts Victoria A, Cooper Priscilla K, Tainer John A

Abstract excerpt

Mutations in XPD helicase, required for nucleotide excision repair (NER) as part of the transcription/repair complex TFIIH, cause three distinct phenotypes: cancer-prone xeroderma pigmentosum (XP), or aging disorders Cockayne syndrome (CS), and trichothiodystrophy (TTD). To clarify molecular differences underlying these diseases, we determined crystal structures of the XPD catalytic core from Sulfolobus...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Cockayne Syndrome

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to DNA Helicases

Share to Iron-Sulfur Proteins

Share to Structural Homology, Protein

Share to Xeroderma Pigmentosum

Share to Xeroderma Pigmentosum Group D Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 18510924
DOI: 10.1016/j.cell.2008.04.030
PMCID: PMC3055247

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

XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations.PMID 18510924Read ↗

Structure, function and evolution of the XPD family of iron-sulfur-containing 5'-->3' DNA helicases.Semantic proximity Read ↗

ARCH domain of XPD, an anchoring platform for CAK that conditions TFIIH DNA repair and transcription activities.Semantic proximity Read ↗

Human XPG nuclease structure, assembly, and activities with insights for neurodegeneration and cancer from pathogenic mutations.Semantic proximity Read ↗

The rem mutations in the ATP-binding groove of the Rad3/XPD helicase lead to Xeroderma pigmentosum-Cockayne syndrome-like phenotypes.Semantic proximity Read ↗

Role of XPD in cellular functions: To TFIIH and beyond.Semantic proximity Read ↗

Every protagonist has a sidekick: Structural aspects of human xeroderma pigmentosum-binding proteins in nucleotide excision repair.Semantic proximity Read ↗

Structural basis of TFIIH activation for nucleotide excision repairSemantic proximity Read ↗

Two individuals with features of both xeroderma pigmentosum and trichothiodystrophy highlight the complexity of the clinical outcomes of mutations in the XPD gene.Semantic proximity Read ↗

DNA helicases associated with genetic instability, cancer, and aging.Semantic proximity Read ↗

Mutations in XPD helicase prevent its interaction and regulation by p44, another subunit of TFIIH, resulting in Xeroderma pigmentosum (XP) and trichothiodystrophy (TTD) phenotypes.Semantic proximity Read ↗

DNA quality control by a lesion sensor pocket of the xeroderma pigmentosum group D helicase subunit of TFIIH.Semantic proximity Read ↗

XPD structure reveals its secrets.Semantic proximity Read ↗

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