ReviewThe Biochemical journal1997
The DNA damage-recognition problem in human and other eukaryotic cells: the XPA damage binding protein.
Review in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 96 citations in OpenAlex.
- The XPA Protein-Life under Precise Control.Cells · 2022Review
- Differences in peripheral neuropathy in xeroderma pigmentosum complementation groups A and D as evaluated by nerve conduction studies.BMC neurology · 2021Article
- Enhanced Antitumor Response to Immune Checkpoint Blockade Exerted by Cisplatin-Induced Mutagenesis in a Murine Melanoma Model.Frontiers in oncology · 2021Article
- DNA Repair Repertoire of the Enigmatic Hydra.Frontiers in genetics · 2021Review
- The Reactions of HMolecules (Basel, Switzerland) · 2020Article
- Mapping p38α mitogen-activated protein kinase signaling by proximity-dependent labeling.Protein science : a publication of the Protein Society · 2020Article
- Polynuclear ruthenium organometallic compounds induce DNA damage in human cells identified by the nucleotide excision repair factor XPC.Bioscience reports · 2019Article
- Characterizing the Binding Interactions between DNA-Binding Proteins, XPA and XPE: A Molecular Dynamics Approach.ACS omega · 2018Article
- Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates.The Journal of biological chemistry · 2017Article
- XPA: A key scaffold for human nucleotide excision repair.DNA repair · 2016Review
- Metal binding mediated conformational change of XPA protein:a potential cytotoxic mechanism of nickel in the nucleotide excision repair.Journal of molecular modeling · 2016Article
- A new structural insight into XPA-DNA interactions.Bioscience reports · 2014Article
- Redefining the DNA-binding domain of human XPA.Journal of the American Chemical Society · 2014Article
- Structural and sequence similarities of hydra xeroderma pigmentosum A protein to human homolog suggest early evolution and conservation.BioMed research international · 2013Article
- Reduced level of ribonucleotide reductase R2 subunits increases dependence on homologous recombination repair of cisplatin-induced DNA damage.Molecular pharmacology · 2011Article
- A functional analysis of G23A polymorphism and the alternative splicing in the expression of the XPA gene.Cellular & molecular biology letters · 2010Article
- Localization of xeroderma pigmentosum group A protein and replication protein A on damaged DNA in nucleotide excision repair.Nucleic acids research · 2010Article
- Checkpoint kinase ATR promotes nucleotide excision repair of UV-induced DNA damage via physical interaction with xeroderma pigmentosum group A.The Journal of biological chemistry · 2009Article
- Erythropoietin overrides the triggering effect of DNA platination products in a mouse model of cisplatin-induced neuropathy.BMC neuroscience · 2009Article
- Other proteins interacting with XP proteins.Advances in experimental medicine and biology · 2008Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The capacity of human and other eukaryotic cells to recognize a disparate variety of damaged sites in DNA, and selectively excise and repair them, resides in a deceptively small simple protein, a 38-42 kDa zinc-finger binding protein, XPA (xeroderma pigmentosum group A), that has no inherent catalytic properties. One key to its damage-recognition ability resides in a DNA-binding domain which combines a zinc finger and a single-strand binding region which may infiltrate small single-stranded regions caused by helix-destabilizing lesions. Another is the augmentation of its binding capacity by interactions with other single-stranded binding proteins and helicases which co-operate in the binding and are unloaded at the binding site to facilitate further unwinding of the DNA and subsequent catalysis. The properties of these reactions suggest there must be considerable conformational changes in XPA and associated proteins to provide a flexible fit to a wide variety of damaged structures in the DNA.
Indexed as
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.