Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sarah D. Aubert"'
Autor:
Karen M Chisholm, Sarah D Aubert, Krister P Freese, Virginia A Zakian, Mary-Claire King, Piri L Welcsh
Publikováno v:
PLoS ONE, Vol 7, Iss 2, p e30748 (2012)
Alu-mediated rearrangement of tumor suppressor genes occurs frequently during carcinogenesis. In breast cancer, this mechanism contributes to loss of the wild-type BRCA1 allele in inherited disease and to loss of heterozygosity in sporadic cancer. To
Externí odkaz:
https://doaj.org/article/123ea2d018064e7cbd047d4a35226e0f
Publikováno v:
Molecular and Cellular Biology. 28:6594-6608
Schizosaccharomyces pombe Pfh1p is an essential member of the Pif family of 5'-3' DNA helicases. The two Saccharomyces cerevisiae homologs, Pif1p and Rrm3p, function in nuclear DNA replication, telomere length regulation, and mitochondrial genome int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0188a9660788f4f13d81d1d197785875
https://doi.org/10.1128/mcb.00191-08
https://doi.org/10.1128/mcb.00191-08
Autor:
Krister P. Freese, Virginia A. Zakian, Piri Welcsh, Sarah D. Aubert, Karen M. Chisholm, Mary Claire King
Publikováno v:
PLoS ONE
PLoS ONE, Vol 7, Iss 2, p e30748 (2012)
PLoS ONE, Vol 7, Iss 2, p e30748 (2012)
Alu-mediated rearrangement of tumor suppressor genes occurs frequently during carcinogenesis. In breast cancer, this mechanism contributes to loss of the wild-type BRCA1 allele in inherited disease and to loss of heterozygosity in sporadic cancer. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34e64d86f86eed5ed93189b3a1176c9c
http://europepmc.org/articles/PMC3276492
http://europepmc.org/articles/PMC3276492
Publikováno v:
Journal of the American Chemical Society. 126(29)
The bacterial phosphotriesterase has been shown to catalyze the stereoselective hydrolysis of phosphinate esters. The wild-type enzyme preferentially hydrolyzes the SP-enantiomers of methyl phenyl p-X-phenylphosphinate esters by 3 orders of magnitude
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aceae200f60956e9f83c6785bfc5aeb1
https://pubmed.ncbi.nlm.nih.gov/15264807
https://pubmed.ncbi.nlm.nih.gov/15264807
Publikováno v:
Biochemistry. 43(19)
Phosphotriesterase (PTE) from Pseudomonas diminuta is a zinc metalloenzyme that hydrolyzes a variety of organophosphorus compounds. The kinetic parameters of Zn/Zn PTE, Cd/Cd PTE, and a mixed-metal Zn/Cd hybrid PTE were obtained with a variety of sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97e8e8f1564b63bb3fe02cc05a83b006
https://pubmed.ncbi.nlm.nih.gov/15134445
https://pubmed.ncbi.nlm.nih.gov/15134445
Publikováno v:
Journal of the American Chemical Society. 125(25)
The wild-type bacterial phosphotriesterase catalyzes the stereoselective hydrolysis of racemic pairs of organophosphorus compounds. The enzymatic stereoselectivity can be substantially enhanced via systematic alteration of the pKa for the leaving gro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::165ec3a6ed8f168fee8cee6774632f0a
https://pubmed.ncbi.nlm.nih.gov/12812487
https://pubmed.ncbi.nlm.nih.gov/12812487