Pif1 helicases are a multifunctional family of DNA helicases that are important for many aspects of genomic stability in the nucleus and mitochondria. Pif1 helicases are conserved from bacteria to humans. Pif1 helicases play multiple roles at the replication fork, including promoting replication through many barriers such as G-quadruplex DNA, the rDNA replication fork barrier, tRNA genes, and R-loops. Pif1 helicases also regulate telomerase and promote replication termination, Okazaki fragment maturation, and break-induced replication. This review highlights many of the roles and regulations of Pif1 at the replication fork that promote cellular health and viability
ScPif1 DNA helicase is the prototypical member of a 5′-to-3 ′ helicase superfamily conserved from ba...
Summary: DNA breaks are complex lesions that can be repaired either by non-homologous end joining (N...
Summary: The S. cerevisiae Pif1 helicase functions with DNA polymerase (Pol) δ in DNA synthesis duri...
The Pif1p family of DNA helicases is conserved from yeast to humans. To date, four members of this f...
SummaryThe conserved PIF helicase family appears to function in replication to ensure termination an...
Approximately, 1% of the genes in eukaryotic genomes encode for helicases, which make the number of ...
Pif-1 proteins are 5′→3′ superfamily 1 (SF1) helicases that in yeast have roles in the maintenance o...
Unwinding duplex DNA is a critical processing step during replication, repair and transcription. Pif...
Pif1, an evolutionarily conserved helicase, negatively regulates telomere length by removing telomer...
The Saccharomyces cerevisiae Pif1 helicase is the prototypical member of the Pif1 DNA helicase famil...
Pif-1 proteins are 50!30 superfamily 1 (SF1) helicases that in yeast have roles in the mainte-nance ...
Bidirectionally moving DNA replication forks merge at termination sites composed of accidental or pr...
DNA breaks are complex lesions that can be repaired either by non-homologous end joining (NHEJ) or b...
The precise machineries required for two aspects of eukaryotic DNA replication, Okazaki fragment pro...
The precise machineries required for two aspects of eukaryotic DNA replication, Okazaki fragment pro...
ScPif1 DNA helicase is the prototypical member of a 5′-to-3 ′ helicase superfamily conserved from ba...
Summary: DNA breaks are complex lesions that can be repaired either by non-homologous end joining (N...
Summary: The S. cerevisiae Pif1 helicase functions with DNA polymerase (Pol) δ in DNA synthesis duri...
The Pif1p family of DNA helicases is conserved from yeast to humans. To date, four members of this f...
SummaryThe conserved PIF helicase family appears to function in replication to ensure termination an...
Approximately, 1% of the genes in eukaryotic genomes encode for helicases, which make the number of ...
Pif-1 proteins are 5′→3′ superfamily 1 (SF1) helicases that in yeast have roles in the maintenance o...
Unwinding duplex DNA is a critical processing step during replication, repair and transcription. Pif...
Pif1, an evolutionarily conserved helicase, negatively regulates telomere length by removing telomer...
The Saccharomyces cerevisiae Pif1 helicase is the prototypical member of the Pif1 DNA helicase famil...
Pif-1 proteins are 50!30 superfamily 1 (SF1) helicases that in yeast have roles in the mainte-nance ...
Bidirectionally moving DNA replication forks merge at termination sites composed of accidental or pr...
DNA breaks are complex lesions that can be repaired either by non-homologous end joining (NHEJ) or b...
The precise machineries required for two aspects of eukaryotic DNA replication, Okazaki fragment pro...
The precise machineries required for two aspects of eukaryotic DNA replication, Okazaki fragment pro...
ScPif1 DNA helicase is the prototypical member of a 5′-to-3 ′ helicase superfamily conserved from ba...
Summary: DNA breaks are complex lesions that can be repaired either by non-homologous end joining (N...
Summary: The S. cerevisiae Pif1 helicase functions with DNA polymerase (Pol) δ in DNA synthesis duri...