نتایج جستجو برای: flap endonuclease 1

تعداد نتایج: 2775035  

Journal: :Cancer genomics & proteomics 2016
Jen-Sheng Pei Wen-Shin Chang Pei-Chen Hsu Chia-Wen Tsai Chin-Mu Hsu Hong-Xue Ji Chieh-Lun Hsiao Yuan-Nian Hsu Da-Tian Bau

AIM Flap endonuclease 1 (FEN1) is one of the most important proteins in maintaining genome stability and preventing carcinogenesis. In recent years, the contribution of two variants of FEN1, rs174538 and rs4246215, regarding cancer risk have been investigated in lung, breast, liver, esophageal, gastric, colorectal cancer and glioma. However, it has not been revealed whether rs174538 and rs42462...

Journal: :Genetics 2005
Eric W Refsland Dennis M Livingston

Among replication mutations that destabilize CAG repeat tracts, mutations of RAD27, encoding the flap endonuclease, and CDC9, encoding DNA ligase I, increase the incidence of repeat tract expansions to the greatest extent. Both enzymes bind to proliferating cell nuclear antigen (PCNA). To understand whether weakening their interactions leads to CAG repeat tract expansions, we have employed alle...

Journal: :Nucleic acids research 1999
G J Sharples L M Corbett P McGlynn

The Rap protein of phage lambda is an endonuclease that nicks branched DNA structures. It has been proposed that Rap can nick D-loops formed during phage recombination to generate splice products without the need for the formation of a 4-strand (Holliday) junction. The structure specificity of Rap was investigated using a variety of branched DNA molecules made by annealing partially complementa...

Journal: :The Journal of biological chemistry 2005
Wensheng Wang Robert A Bambara

Flap endonuclease 1 (FEN1) participates in removal of RNA primers of Okazaki fragments, several DNA repair pathways, and genome stability maintenance. Defects in yeast FEN1 produce chromosomal instability, hyper-recombination, and sequence duplication. These occur because flaps produced during replication are not promptly removed. Long-lived flaps sustain breaks and form misaligned bubble struc...

2012
Rajendra Prasad Jason G. Williams Esther W. Hou Samuel H. Wilson

During mammalian base excision repair (BER) of lesion-containing DNA, it is proposed that toxic strand-break intermediates generated throughout the pathway are sequestered and passed from one step to the next until repair is complete. This stepwise process is termed substrate channeling. A working model evaluated here is that a complex of BER factors may facilitate the BER process. FLAG-tagged ...

Journal: :The Journal of biological chemistry 1998
D K Srivastava B J Berg R Prasad J T Molina W A Beard A E Tomkinson S H Wilson

Base excision repair (BER) is one of the cellular defense mechanisms repairing damage to nucleoside 5'-monophosphate residues in genomic DNA. This repair pathway is initiated by spontaneous or enzymatic N-glycosidic bond cleavage creating an abasic or apurinic-apyrimidinic (AP) site in double-stranded DNA. Class II AP endonuclease, deoxyribonucleotide phosphate (dRP) lyase, DNA synthesis, and D...

Journal: :Cell 2011
Susan E. Tsutakawa Scott Classen Brian R. Chapados Andrew S. Arvai L. David Finger Grant Guenther Christopher G. Tomlinson Peter Thompson Altaf H. Sarker Binghui Shen Priscilla K. Cooper Jane A. Grasby John A. Tainer

Flap endonuclease (FEN1), essential for DNA replication and repair, removes RNA and DNA 5' flaps. FEN1 5' nuclease superfamily members acting in nucleotide excision repair (XPG), mismatch repair (EXO1), and homologous recombination (GEN1) paradoxically incise structurally distinct bubbles, ends, or Holliday junctions, respectively. Here, structural and functional analyses of human FEN1:DNA comp...

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