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PIF1 is a 5-prime-to-3-prime DNA helicase that negatively regulates telomerase (see TERT\; MIM 187270), a reverse transcriptase that maintains telomere length (Zhang et al., 2006 [PubMed 16522649]).[supplied by OMIM, Mar 2008].. Additionally we are shipping PIF1 5'-To-3' DNA Helicase Homolog (S. Cerevisiae) Antibodies (30) and and many more products for this protein.
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Structural and functional characterization of the unwinding mechanism of Bacteroides and human Pif1 helicases has been reported.
Authors characterised a functional role for human PIF1 in DNA replication that becomes important for cell growth under oncogenic stress.
Pif1 readily unfolds a parallel quadruplex DNA substrate in a multiturnover reaction and also generates some product under single cycle conditions
A minimum of 10 oligonucleotide bases are required for PIF1 binding and the hydrolysis of ATP.
the yeast ortholog of Pif1 appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP.
Evidence that the PIF1 N-terminal (PINT) domain as crucial functions in PIF1 helicase.
when expressed in yeast, human PIF1 suppressed both G-quadruplex-associated DNA damage and telomere lengthening
PIF1 variant L319P was identified in three breast cancer families
Findings suggest roles for PIF1 in S-phase entry and progression that are essential to protect human tumor cells from apoptosis.
Human Pif1 could have a role in processing G4 structures that arise in the single-stranded nucleic acid intermediates formed during DNA replication and gene expression.
hPif1 may regulate telomere elongation by decreasing telomerase processivity, possibly via a mechanism that involves the unwinding of telomerase RNA from telomeric DNA by hPif1.
Human PIF, like S. cerevisiae Pif1p, plays a role in telomerase regulation.
hPif1 in the nucleus may be involved in chromosome maintenance in association with DNA replication
hPif1 specifically recognizes and unwinds DNA structures resembling putative stalled replication forks.
pif1-/- animals develop a mitochondrial myopathy with respiratory chain deficiency.
murine cells have evolved mechanisms to ensure the functional redundancy of Pif1 or Nbs1 in the regulation of chromosome healing.
Murine telomere homeostasis or genetic stability does not depend on mPif1.
PIF1 is a 5-prime-to-3-prime DNA helicase that negatively regulates telomerase (see TERT\; MIM 187270), a reverse transcriptase that maintains telomere length (Zhang et al., 2006
ATP-dependent DNA helicase PIF1
, DNA helicase PIF1
, DNA helicase homolog PIF1
, PIF1 5'-to-3' DNA helicase homolog
, PIF1 DNA helicase
, PIF1/RRM3 DNA helicase-like protein
, petite integration frequency 1
, Pif1/Rrm3 DNA-helicase-like protein
, DNA helicase-like protein
, PIF1 homolog
, Pif1/Rrm3 DNA helicase-like protein