Sequential and Multistep Substrate Interrogation Provides the Scaffold for Specificity in Human Flap Endonuclease 1
Human flap endonuclease 1 (FEN1), one of the structure-specific 5′ nucleases, is integral in replication, repair, and recombination of cellular DNA. The 5′ nucleases share significant unifying features yet cleave diverse substrates at similar positions relative to 5′ end junctions. Using single-mole...
Main Authors: | Mohamed A. Sobhy, Luay I. Joudeh, Xiaojuan Huang, Masateru Takahashi, Samir M. Hamdan |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2013-06-01
|
Series: | Cell Reports |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124713002180 |
Similar Items
-
Single-molecule FRET unveils induced-fit mechanism for substrate selectivity in flap endonuclease 1
by: Fahad Rashid, et al.
Published: (2017-02-01) -
Implementing fluorescence enhancement, quenching, and FRET for investigating flap endonuclease 1 enzymatic reaction at the single-molecule level
by: Mohamed A. Sobhy, et al.
Published: (2021-01-01) -
Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9.
by: Keeble, A, et al.
Published: (2002) -
Phosphate steering by Flap Endonuclease 1 promotes 5′-flap specificity and incision to prevent genome instability
by: Susan E. Tsutakawa, et al.
Published: (2017-06-01) -
Identification of Flap Endonuclease 1 With Diagnostic and Prognostic Value in Breast Cancer
by: Min Wu, et al.
Published: (2021-06-01)