Flap endonuclease 1: a central component of DNA metabolism.
- Yuan Liu, H. Kao, R. Bambara
- BiologyAnnual Review of Biochemistry
- 9 June 2004
FEN1 is a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions and interacts with other nucleases and helicases that allow it to act efficiently on structured flaps.
Cleavage Specificity of Saccharomyces cerevisiae Flap Endonuclease 1 Suggests a Double-Flap Structure as the Cellular Substrate*
- H. Kao, L. A. Henricksen, Yuan Liu, R. Bambara
- BiologyJournal of Biological Chemistry
- 26 April 2002
Results suggest that the double-flap substrate is formed and cleaved during eukaryotic DNA replication in vivo.
Strand transfer events during HIV-1 reverse transcription.
- V. P. Basu, Min Song, Lu Gao, S. Rigby, M. N. Hanson, R. Bambara
- BiologyVirus Research
- 1 June 2008
Ataxia Telangiectasia Mutated (ATM) and ATM and Rad3-related Protein Exhibit Selective Target Specificities in Response to Different Forms of DNA Damage*
- C. Helt, W. Cliby, P. Keng, R. Bambara, M. O’Reilly
- Biology, ChemistryJournal of Biological Chemistry
- 14 January 2005
Activated ATM and ATR exhibit selective substrate specificity in response to different genotoxic agents as revealed by activation of these kinases in cells exposed to IR, UV, and hyperoxia.
Regulatory Roles of p21 and Apurinic/Apyrimidinic Endonuclease 1 in Base Excision Repair*
- S. Tom, T. Ranalli, V. Podust, R. Bambara
- BiologyJournal of Biological Chemistry
- 28 December 2001
It is shown that p21 also inhibits PCNA stimulation of long patch base excision repair (BER) in vitro and proposed that APE1 serves as an assembly and coordination factor for long patch BER proteins, which implies that BER can be regulated differentially.
Mechanism Whereby Proliferating Cell Nuclear Antigen Stimulates Flap Endonuclease 1*
- S. Tom, L. A. Henricksen, R. Bambara
- BiologyJournal of Biological Chemistry
- 7 April 2000
Human flap endonuclease 1 (FEN1), an essential DNA replication protein, cleaves substrates with unannealed 5′-tails by PCNA, and results indicate that after FEN1 tracks to the cleavage site, PCNA enhances F EN1 binding stability, allowing for greater cleavage efficiency.
Enzymes and Reactions at the Eukaryotic DNA Replication Fork*
- R. Bambara, R. Murante, L. A. Henricksen
- BiologyJournal of Biological Chemistry
- 21 February 1997
This work will focus on recent findings concerning specific enzymatic reactions necessary for the growth of the eukaryotic replication fork.
Macrophage Tropism of HIV-1 Depends on Efficient Cellular dNTP Utilization by Reverse Transcriptase*
- Tracy L. Diamond, M. Roshal, Baek Kim
- BiologyJournal of Biological Chemistry
- 3 December 2004
The results suggest that the ability of HIV-1 to infect macrophages depends, at least in part, on enzymatic adaptation ofAIDS-1 RT to efficiently catalyze DNA synthesis in limited cellular dNTP substrate environments.
Enzymatic completion of mammalian lagging-strand DNA replication.
- J. Turchi, L. Huang, R. Murante, Y. Kim, R. Bambara
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 11 October 1994
Using purified proteins from calf and a synthetic substrate, the enzymatic reactions required for mammalian Okazaki fragment processing in vitro are reconstituted and strongly suggest that they perform the same reactions in vivo.
Okazaki fragment metabolism.
- Lata Balakrishnan, R. Bambara
- BiologyCold Spring Harbor Perspectives in Biology
- 1 February 2013
Genetic analyses and reconstitution experiments identified proteins and multiple pathways responsible for maturation of the lagging strand, which involves many enzymes, possibly three pathways, and regulation that can shift from high efficiency to high fidelity.
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