ReviewInternational journal of molecular sciences2014
Structural biology of DNA (6-4) photoproducts formed by ultraviolet radiation and interactions with their binding proteins.
Review in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- UV photodamage pathways and the evolutionary selection of thymine over uracil in early genetic systems.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A critical review of ultra-violet light emitting diodes as a one water disinfection technology.Water research X · 2024Review
- Activation of Peroxisome Proliferator-Activated Receptor-β/δ (PPARβ/δ) in Keratinocytes by Endogenous Fatty Acids.Biomolecules · 2024Article
- Review
- Differing structures and dynamics of two photolesions portray verification differences by the human XPD helicase.Nucleic acids research · 2023Article
- Recent Applications of Melanin-like Nanoparticles as Antioxidant Agents.Antioxidants (Basel, Switzerland) · 2023Review
- Recent advances in quantum nanophotonics: plexcitonic and vibro-polaritonic strong coupling and its biomedical and chemical applications.Nanophotonics (Berlin, Germany) · 2023Review
- Impact of UV-C Irradiation on Bacterial Disinfection in a Drinking Water Purification System.Journal of microbiology and biotechnology · 2023Article
- Conformational Preferences of Pyridone Adenine Dinucleotides from Molecular Dynamics Simulations.International journal of molecular sciences · 2022Article
- Structural organization, evolution, and distribution of viral pyrimidine dimer-DNA glycosylases.Biophysical reviews · 2022Review
- Lignin Nanoparticles Deliver Novel Thymine Biomimetic Photo-Adducts with Antimelanoma Activity.International journal of molecular sciences · 2022Article
- Xeroderma Pigmentosum: General Aspects and Management.Journal of personalized medicine · 2021Review
- Nucleotide Excision Repair: From Molecular Defects to Neurological Abnormalities.International journal of molecular sciences · 2021Review
- X-ray and UV Radiation Damage of dsDNA/Protein Complexes.Molecules (Basel, Switzerland) · 2021Article
- Photoreceptor Diversification Accompanies the Evolution of Anthozoa.Molecular biology and evolution · 2021Article
- Challenging Cosmetic Innovation: The Skin Microbiota and Probiotics Protect the Skin from UV-Induced Damage.Microorganisms · 2021Review
- Thymine dissociation and dimer formation: A Raman and synchronous fluorescence spectroscopic study.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Review
- γH2AX in the S Phase after UV Irradiation Corresponds to DNA Replication and Does Not Report on the Extent of DNA Damage.Molecular and cellular biology · 2020Article
- Anticancer Activity ofNutrients · 2020Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exposure to the ultraviolet component of sunlight causes DNA damage, which subsequently leads to mutations, cellular transformation, and cell death. DNA photoproducts with (6-4) pyrimidine-pyrimidone adducts are more mutagenic than cyclobutane pyrimidine dimers. These lesions must be repaired because of the high mutagenic potential of (6-4) photoproducts. We here reviewed the structures of (6-4) photoproducts, particularly the detailed structures of the (6-4) lesion and (6-4) lesion-containing double-stranded DNA. We also focused on interactions with their binding proteins such as antibody Fabs, (6-4) photolyase, and nucleotide excision repair protein. The (6-4) photoproducts that bound to these proteins had common structural features: The 5'-side thymine and 3'-side pyrimidone bases of the T(6-4)T segment were in half-chair and planar conformations, respectively, and both bases were positioned nearly perpendicularly to each other. Interactions with binding proteins showed that the DNA helices flanking the T(6-4)T segment were largely kinked, and the flipped-out T(6-4)T segment was recognized by these proteins. These proteins had distinctive binding-site structures that were appropriate for their functions.
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