Human Fanconi anemia complementation group a protein stimulates the 5' flap endonuclease activity of FEN1. [PDF]
In eukaryotic cells, Flap endonuclease 1 (FEN1) is a major structure-specific endonuclease that processes 5' flapped structures during maturation of lagging strand DNA synthesis, long patch base excision repair, and rescue of stalled replication forks ...
Liangyue Qian +4 more
doaj +5 more sources
Damage-dependent regulation of MUS81-EME1 by Fanconi anemia complementation group A protein. [PDF]
MUS81-EME1 is a DNA endonuclease involved in replication-coupled repair of DNA interstrand cross-links (ICLs). A prevalent hypothetical role of MUS81-EME1 in ICL repair is to unhook the damage by incising the leading strand at the 3' side of an ICL lesion.
Benitez A +8 more
europepmc +4 more sources
A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M [PDF]
Fanconi anemia is a genetic disease characterized by genomic instability and cancer predisposition. Nine genes involved in Fanconi anemia have been identified; their products participate in a DNA damage-response network involving BRCA1 and BRCA2 (refs. 2,3).
Meetei, A R +13 more
openaire +6 more sources
Identification of FANCG as a prognostic factor for prostate cancer [PDF]
Background To ascertain role of the fanconi anemia complementation group G (FANCG) gene in prostate cancer (PCa) and the suitability of the FANCG gene as a prognostic biomarker for PCa.
Wenlong Gao +4 more
doaj +2 more sources
Betulinic Acid Suppresses UBE2T Expression via MAPK/ERK Inhibition to Block FANCI and FANCD2 Monoubiquitination in Glioblastoma. [PDF]
ABSTRACT Platinum‐based chemotherapy remains a cornerstone of glioma treatment, yet resistance driven by the Fanconi anaemia (FA) DNA repair pathway limits efficacy. Here, we identified betulinic acid (BA) as a potent inhibitor of FA pathway activation.
Bao Y, Wang M.
europepmc +2 more sources
Individuals with Fanconi anemia (FA), a rare genetic bone marrow failure syndrome, have an increased risk of young‐onset head and neck squamous cell carcinomas (SCCs) and esophageal SCC.
Jasmine D. Peake +8 more
doaj +1 more source
Fanconi Anemia Complementation Group A (FANCA) Protein Has Intrinsic Affinity for Nucleic Acids with Preference for Single-stranded Forms [PDF]
The Fanconi anemia complementation group A (FANCA) gene is one of 15 disease-causing genes and has been found to be mutated in ∼60% of Fanconi anemia patients. Using purified protein, we report that human FANCA has intrinsic affinity for nucleic acids.
Fenghua, Yuan +7 more
openaire +2 more sources
Fanconi anemia (FA) binding protein FAAP20 stabilizes FA complementation group A (FANCA) and participates in interstrand cross-link repair [PDF]
The Fanconi anemia (FA) pathway participates in interstrand cross-link (ICL) repair and the maintenance of genomic stability. The FA core complex consists of eight FA proteins and two Fanconi anemia-associated proteins (FAAP24 and FAAP100). The FA core complex has ubiquitin ligase activity responsible for monoubiquitination of the FANCI-FANCD2 (ID ...
Chen, J +5 more
openaire +4 more sources
Background Ferroptosis is related to the immunosuppression of tumors and plays a critical role in cancer progression. Fanconi anemia complementation group D2 (FANCD2) is a vital gene that regulates ferroptosis.
Xiaowei Tang +10 more
doaj +1 more source
A deficiency in a 230 kDa DNA repair protein in Fanconi anemia complementation group A cells is corrected by the FANCA cDNA [PDF]
Cells from individuals with the cancer-prone, inherited disorder Fanconi anemia (FA) are hypersensitive to DNA interstrand cross-linking agents and this hypersensitivity correlates with a defect in ability to repair this type of damage to their DNA. We have isolated a DNA endonuclease complex from the nuclei of normal human cells which is involved in ...
D W, Brois +5 more
openaire +2 more sources

