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Observation of unpaired substrate DNA in the flap endonuclease-1 active site.

Finger LD, Patel N, Beddows A, Ma L, Exell JC, Jardine E, Jones AC, Grasby JA.

Nucleic Acids Res. 2013 Nov;41(21):9839-47. doi: 10.1093/nar/gkt737. Epub 2013 Aug 23.


Proline scanning mutagenesis reveals a role for the flap endonuclease-1 helical cap in substrate unpairing.

Patel N, Exell JC, Jardine E, Ombler B, Finger LD, Ciani B, Grasby JA.

J Biol Chem. 2013 Nov 22;288(47):34239-48. doi: 10.1074/jbc.M113.509489. Epub 2013 Oct 14.


DNA and Protein Requirements for Substrate Conformational Changes Necessary for Human Flap Endonuclease-1-catalyzed Reaction.

Algasaier SI, Exell JC, Bennet IA, Thompson MJ, Gotham VJ, Shaw SJ, Craggs TD, Finger LD, Grasby JA.

J Biol Chem. 2016 Apr 8;291(15):8258-68. doi: 10.1074/jbc.M115.698993. Epub 2016 Feb 16.


Human flap endonuclease structures, DNA double-base flipping, and a unified understanding of the FEN1 superfamily.

Tsutakawa SE, Classen S, Chapados BR, Arvai AS, Finger LD, Guenther G, Tomlinson CG, Thompson P, Sarker AH, Shen B, Cooper PK, Grasby JA, Tainer JA.

Cell. 2011 Apr 15;145(2):198-211. doi: 10.1016/j.cell.2011.03.004.


Double strand binding-single strand incision mechanism for human flap endonuclease: implications for the superfamily.

Tsutakawa SE, Tainer JA.

Mech Ageing Dev. 2012 Apr;133(4):195-202. doi: 10.1016/j.mad.2011.11.009. Epub 2012 Jan 8. Review.


Sequential and multistep substrate interrogation provides the scaffold for specificity in human flap endonuclease 1.

Sobhy MA, Joudeh LI, Huang X, Takahashi M, Hamdan SM.

Cell Rep. 2013 Jun 27;3(6):1785-94. doi: 10.1016/j.celrep.2013.05.001. Epub 2013 Jun 6.


Triplet repeat expansion generated by DNA slippage is suppressed by human flap endonuclease 1.

Ruggiero BL, Topal MD.

J Biol Chem. 2004 May 28;279(22):23088-97. Epub 2004 Mar 22.


Flap endonuclease 1.

Balakrishnan L, Bambara RA.

Annu Rev Biochem. 2013;82:119-38. doi: 10.1146/annurev-biochem-072511-122603. Epub 2013 Feb 28. Review.


Single-molecule characterization of Fen1 and Fen1/PCNA complexes acting on flap substrates.

Craggs TD, Hutton RD, Brenlla A, White MF, Penedo JC.

Nucleic Acids Res. 2014 Feb;42(3):1857-72. doi: 10.1093/nar/gkt1116. Epub 2013 Nov 13.


Flap endonuclease 1: a central component of DNA metabolism.

Liu Y, Kao HI, Bambara RA.

Annu Rev Biochem. 2004;73:589-615. Review.


Crystal structure of bacteriophage T4 5' nuclease in complex with a branched DNA reveals how flap endonuclease-1 family nucleases bind their substrates.

Devos JM, Tomanicek SJ, Jones CE, Nossal NG, Mueser TC.

J Biol Chem. 2007 Oct 26;282(43):31713-24. Epub 2007 Aug 9.


The wonders of flap endonucleases: structure, function, mechanism and regulation.

Finger LD, Atack JM, Tsutakawa S, Classen S, Tainer J, Grasby J, Shen B.

Subcell Biochem. 2012;62:301-26. doi: 10.1007/978-94-007-4572-8_16. Review.


Unpairing and gating: sequence-independent substrate recognition by FEN superfamily nucleases.

Grasby JA, Finger LD, Tsutakawa SE, Atack JM, Tainer JA.

Trends Biochem Sci. 2012 Feb;37(2):74-84. doi: 10.1016/j.tibs.2011.10.003. Epub 2011 Nov 24. Review.


Cellularly active N-hydroxyurea FEN1 inhibitors block substrate entry to the active site.

Exell JC, Thompson MJ, Finger LD, Shaw SJ, Debreczeni J, Ward TA, McWhirter C, Siöberg CL, Martinez Molina D, Abbott WM, Jones CD, Nissink JW, Durant ST, Grasby JA.

Nat Chem Biol. 2016 Oct;12(10):815-21. doi: 10.1038/nchembio.2148. Epub 2016 Aug 15.


Comparison of the catalytic parameters and reaction specificities of a phage and an archaeal flap endonuclease.

Williams R, Sengerová B, Osborne S, Syson K, Ault S, Kilgour A, Chapados BR, Tainer JA, Sayers JR, Grasby JA.

J Mol Biol. 2007 Aug 3;371(1):34-48. Epub 2007 May 1.


Rate-determining Step of Flap Endonuclease 1 (FEN1) Reflects a Kinetic Bias against Long Flaps and Trinucleotide Repeat Sequences.

Tarantino ME, Bilotti K, Huang J, Delaney S.

J Biol Chem. 2015 Aug 21;290(34):21154-62. doi: 10.1074/jbc.M115.666438. Epub 2015 Jul 9.


FANCD2-associated nuclease 1, but not exonuclease 1 or flap endonuclease 1, is able to unhook DNA interstrand cross-links in vitro.

Pizzolato J, Mukherjee S, Schärer OD, Jiricny J.

J Biol Chem. 2015 Sep 11;290(37):22602-11. doi: 10.1074/jbc.M115.663666. Epub 2015 Jul 28.


Substrate recognition and catalysis by flap endonucleases and related enzymes.

Tomlinson CG, Atack JM, Chapados B, Tainer JA, Grasby JA.

Biochem Soc Trans. 2010 Apr;38(2):433-7. doi: 10.1042/BST0380433. Review.


Positioning the 5'-flap junction in the active site controls the rate of flap endonuclease-1-catalyzed DNA cleavage.

Song B, Hamdan SM, Hingorani MM.

J Biol Chem. 2018 Mar 30;293(13):4792-4804. doi: 10.1074/jbc.RA117.001137. Epub 2018 Feb 9.


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