A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins.
about
Evolutionary families of peptidase inhibitorsBiochemical analysis of the yeast proteinase inhibitor (IC) homolog ICh and its comparison with IC.Tfs1p, a member of the PEBP family, inhibits the Ira2p but not the Ira1p Ras GTPase-activating protein in Saccharomyces cerevisiaeThe phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitorsThe stress-induced Tfs1p requires NatB-mediated acetylation to inhibit carboxypeptidase Y and to regulate the protein kinase A pathway.A proteomic approach for the analysis of instantly released wound and immune proteins in Drosophila melanogaster hemolymph.Transcriptional regulation by protein kinase A in Cryptococcus neoformans.A single amino acid converts a repressor to an activator of flowering.Learning gene networks under SNP perturbations using eQTL datasets.Raf kinase inhibitory protein knockout mice: expression in the brain and olfaction deficitImproved production of fatty acids by Saccharomyces cerevisiae through screening a cDNA library from the oleaginous yeast Yarrowia lipolytica.Modulation of the MAP kinase signaling cascade by Raf kinase inhibitory protein.Genome-wide transcriptional profiling of the cyclic AMP-dependent signaling pathway during morphogenic transitions of Candida albicansPhosphatidylenthanolamine Binding Protein aka Raf Kinase Inhibitor Protein: A Brief History of Its Discovery and the Remarkable Diversity of Biological Functions.RKIP: much more than Raf kinase inhibitory protein.A DNA microarray-based approach to elucidate the effects of the immunosuppressant SR31747A on gene expression in Saccharomyces cerevisiae.Some properties and possible biological role of peptidase inhibitors from the entomopathogenic fungus Tolypocladium cylindrosporum.A divergent external loop confers antagonistic activity on floral regulators FT and TFL1.N-terminal acetyl group is essential for the inhibitory function of carboxypeptidase Y inhibitor (I(C)).The multiple site binding of carboxypeptidase Y inhibitor (IC) to the cognate proteinase. Implications for the biological roles of the phosphatidylethanolamine-binding protein.The hippocampal cholinergic neurostimulating peptide, the N-terminal fragment of the secreted phosphatidylethanolamine-binding protein, possesses a new biological activity on cardiac physiology.MrpL35, a mitospecific component of mitoribosomes, plays a key role in cytochrome c oxidase assembly.
P2860
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P2860
A high-affinity inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins.
description
1998 nî lūn-bûn
@nan
1998 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի մարտին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@ast
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@en
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@nl
type
label
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@ast
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@en
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@nl
prefLabel
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@ast
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@en
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@nl
P2093
P356
P1433
P1476
A high-affinity inhibitor of y ...... ily of lipid binding proteins.
@en
P2093
I Svendsen
J R Winther
M C Kielland-Brandt
S O Sørensen
P304
P356
10.1021/BI971286W
P407
P577
1998-03-10T00:00:00Z