Phosphatase complex Pph3/Psy2 is involved in regulation of efficient non-homologous end-joining pathway in the yeast Saccharomyces cerevisiae.
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Regulatory roles of phosphorylation in model and pathogenic fungiThe genome of an Encephalitozoon cuniculi type III strain reveals insights into the genetic diversity and mode of reproduction of a ubiquitous vertebrate pathogenThe sensitivity of the yeast, Saccharomyces cerevisiae, to acetic acid is influenced by DOM34 and RPL36A.Mapping and identification of a potential candidate gene for a novel maturity locus, E10, in soybean.Heavy metal sensitivities of gene deletion strains for ITT1 and RPS1A connect their activities to the expression of URE2, a key gene involved in metal detoxification in yeast
P2860
Phosphatase complex Pph3/Psy2 is involved in regulation of efficient non-homologous end-joining pathway in the yeast Saccharomyces cerevisiae.
description
2014 nî lūn-bûn
@nan
2014 թուականին հրատարակուած գիտական յօդուած
@hyw
2014 թվականին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@ast
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@en
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@nl
type
label
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@ast
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@en
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@nl
prefLabel
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@ast
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@en
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@nl
P2093
P2860
P1433
P1476
Phosphatase complex Pph3/Psy2 ...... east Saccharomyces cerevisiae.
@en
P2093
Andrew Schoenrock
Ashkan Golshani
Bahram Samanfar
Daniel Burnside
Jianhua Xu
Katayoun Omidi
Matthew Jessulat
Megan Sanders
Mohan Babu
Mohsen Hooshyar
P2860
P304
P356
10.1371/JOURNAL.PONE.0087248
P407
P577
2014-01-01T00:00:00Z