Mutational analysis of STE5 in the yeast Saccharomyces cerevisiae: application of a differential interaction trap assay for examining protein-protein interactions.
about
MAP kinase pathways in the yeast Saccharomyces cerevisiaeInteraction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3Function of the MAPK scaffold protein, Ste5, requires a cryptic PH domainScaffold proteins: hubs for controlling the flow of cellular informationThe Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activationA novel 14-kilodalton protein interacts with the mitogen-activated protein kinase scaffold mp1 on a late endosomal/lysosomal compartmentConformational Control of the Ste5 Scaffold Protein Insulates Against MAP Kinase MisactivationAdy4p and Spo74p are components of the meiotic spindle pole body that promote growth of the prospore membrane in Saccharomyces cerevisiae.Hsl7 localizes to a septin ring and serves as an adapter in a regulatory pathway that relieves tyrosine phosphorylation of Cdc28 protein kinase in Saccharomyces cerevisiae.Dynamic localization of the Swe1 regulator Hsl7 during the Saccharomyces cerevisiae cell cycleAdy3p links spindle pole body function to spore wall synthesis in Saccharomyces cerevisiae.A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmissionMutations in the YRB1 gene encoding yeast ran-binding-protein-1 that impair nucleocytoplasmic transport and suppress yeast mating defects'Edgetic' perturbation of a C. elegans BCL2 ortholog.Mitogen-activated protein kinases with distinct requirements for Ste5 scaffolding influence signaling specificity in Saccharomyces cerevisiaeComplex formation by the Drosophila MSL proteins: role of the MSL2 RING finger in protein complex assembly.Using the two-hybrid screen in the classroom laboratory.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Evolutionary reshaping of fungal mating pathway scaffold proteinsMutational analysis suggests that activation of the yeast pheromone response mitogen-activated protein kinase pathway involves conformational changes in the Ste5 scaffold protein.Recruitment interactions can override catalytic interactions in determining the functional identity of a protein kinase.Nuclear export and plasma membrane recruitment of the Ste5 scaffold are coordinated with oligomerization and association with signal transduction components.Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiaeStructurally unique interaction of RBD-like and PH domains is crucial for yeast pheromone signalingThe regulation of filamentous growth in yeast.A framework for mapping, visualisation and automatic model creation of signal-transduction networks.Nucleus-specific and cell cycle-regulated degradation of mitogen-activated protein kinase scaffold protein Ste5 contributes to the control of signaling competence.Analysis of the thresholds for transcriptional activation by the yeast MAP kinases Fus3 and Kss1.Negative Feedback Phosphorylation of Gγ Subunit Ste18 and the Ste5 Scaffold Synergistically Regulates MAPK Activation in Yeast.
P2860
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P2860
Mutational analysis of STE5 in the yeast Saccharomyces cerevisiae: application of a differential interaction trap assay for examining protein-protein interactions.
description
1997 nî lūn-bûn
@nan
1997 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Mutational analysis of STE5 in ...... protein-protein interactions.
@ast
Mutational analysis of STE5 in ...... protein-protein interactions.
@en
Mutational analysis of STE5 in ...... protein-protein interactions.
@nl
type
label
Mutational analysis of STE5 in ...... protein-protein interactions.
@ast
Mutational analysis of STE5 in ...... protein-protein interactions.
@en
Mutational analysis of STE5 in ...... protein-protein interactions.
@nl
prefLabel
Mutational analysis of STE5 in ...... protein-protein interactions.
@ast
Mutational analysis of STE5 in ...... protein-protein interactions.
@en
Mutational analysis of STE5 in ...... protein-protein interactions.
@nl
P2093
P2860
P1433
P1476
Mutational analysis of STE5 in ...... g protein-protein interactions
@en
P2093
P2860
P304
P407
P577
1997-10-01T00:00:00Z