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

Purification of nuclear proteins that bind to cisplatin-damaged DNA. Identity with high mobility group proteins 1 and 2.

1 Jul 1992

Abstract excerpt

The biochemical processes responsible for the recognition and repair of cisplatin-damaged DNA in human cells are not well understood. We have developed a damaged DNA affinity precipitation technique that allows the direct visualization and characterization of cellular proteins that bind to cisplatin-damaged DNA. The method separates damaged DNA-binding proteins from complex radiolabeled cell mixtures and further...

Read the complete abstract on PubMed

Topics

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

Share to DNA and Nucleic Acid Chemistry
Share to DNA Repair Mechanisms
Share to Metal complexes synthesis and properties

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 1618852
DOI: 10.1016/s0021-9258(18)42242-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Purification of nuclear proteins that bind to cisplatin-damaged DNA. Identity with high mobility group proteins 1 and 2.PMID 1618852Read ↗

Identification of Mammalian Proteins Cross-linked to DNA by Ionizing RadiationSemantic proximity Read ↗

Human Ku Autoantigen Binds Cisplatin-damaged DNA but Fails to Stimulate Human DNA-activated Protein KinaseSemantic proximity Read ↗

Recognition and repair of DNA-cisplatin adducts.Semantic proximity Read ↗

The “adductome”: a limited repertoire of adducted proteins in human cellsSemantic proximity Read ↗

Interaction of FACT, SSRP1, and the High Mobility Group (HMG) Domain of SSRP1 with DNA Damaged by the Anticancer Drug CisplatinSemantic proximity Read ↗

HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision nuclease.Semantic proximity Read ↗

Differential human nucleotide excision repair of paired and mispaired cisplatin-DNA adductsSemantic proximity Read ↗

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

Inhibition of nucleotide excision repair by high mobility group protein HMGA1.Semantic proximity Read ↗

Adduct-specific monoclonal antibodies for the measurement of cisplatin-induced DNA lesions in individual cell nucleiSemantic proximity Read ↗

Differential expression of proteins in radioresistant and radiosensitive human squamous carcinoma cells.Semantic proximity Read ↗

Affinity purification and partial characterization of a yeast multiprotein complex for nucleotide excision repair using histidine-tagged Rad14 protein.Semantic proximity Read ↗

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