Eukaryotic Lagging Strand DNA Replication Employs a Multi-pathway Mechanism That Protects Genome Integrity

Flap Endonuclease 1 Mechanism Analysis Indicates Flap Base Binding Prior to Threading

(2010) Jason W. Gloor et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

An Alternative Pathway for Okazaki Fragment Processing

(2010) Jason E. Pike et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Components of the Secondary Pathway Stimulate the Primary Pathway of Eukaryotic Okazaki Fragment Processing

(2010) Ryan A. Henry et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding

(2010) Zhigang Guo et al.   Nature Chemical Biology

Mechanism of polymerase collision release from sliding clamps on the lagging strand

(2009) Roxana E Georgescu et al.   EMBO JOURNAL

Acetylation of Dna2 Endonuclease/Helicase and Flap Endonuclease 1 by p300 Promotes DNA Stability by Creating Long Flap Intermediates

(2009) Lata Balakrishnan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Coordinating DNA replication by means of priming loop and differential synthesis rate

(2009) Manjula Pandey et al.   NATURE

Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions

(2009) C. Choudhary et al.   SCIENCE

Dynamic Removal of Replication Protein A by Dna2 Facilitates Primer Cleavage during Okazaki Fragment Processing inSaccharomyces cerevisiae

(2008) Jason A. Stewart et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Pif1 Helicase Directs Eukaryotic Okazaki Fragments toward the Two-nuclease Cleavage Pathway for Primer Removal

(2008) Marie L. Rossi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Polymerase Dynamics at the Eukaryotic DNA Replication Fork

(2008) Peter M. J. Burgers   JOURNAL OF BIOLOGICAL CHEMISTRY

Human DNA2 Is a Mitochondrial Nuclease/Helicase for Efficient Processing of DNA Replication and Repair Intermediates

(2008) Li Zheng et al.   MOLECULAR CELL

Acetylation Regulates WRN Catalytic Activities and Affects Base Excision DNA Repair

(2008) Meltem Muftuoglu et al.   PLoS One