Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
about
Ascospore formation in the yeast Saccharomyces cerevisiae.Ady4p and Spo74p are components of the meiotic spindle pole body that promote growth of the prospore membrane in Saccharomyces cerevisiae.Differential requirement for phospholipase D/Spo14 and its novel interactor Sma1 for regulation of exocytotic vesicle fusion in yeast meiosis.SSP2 and OSW1, two sporulation-specific genes involved in spore morphogenesis in Saccharomyces cerevisiae.SPO71 mediates prospore membrane size and maturation in Saccharomyces cerevisiae.Molecular interactions position Mso1p, a novel PTB domain homologue, in the interface of the exocyst complex and the exocytic SNARE machinery in yeast.The SpoMBe pathway drives membrane bending necessary for cytokinesis and spore formation in yeast meiosis.Protein phosphatase type 1-interacting protein Ysw1 is involved in proper septin organization and prospore membrane formation during sporulationSPO71 encodes a developmental stage-specific partner for Vps13 in Saccharomyces cerevisiae.Genetic evidence for a SPO1-dependent signaling pathway controlling meiotic progression in yeast.Alternative modes of organellar segregation during sporulation in Saccharomyces cerevisiaeDtrlp, a multidrug resistance transporter of the major facilitator superfamily, plays an essential role in spore wall maturation in Saccharomyces cerevisiae.Ady3p links spindle pole body function to spore wall synthesis in Saccharomyces cerevisiae.Timely Closure of the Prospore Membrane Requires SPS1 and SPO77 in Saccharomyces cerevisiaeVesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae.The Dysferlin Domain-Only Protein, Spo73, Is Required for Prospore Membrane Extension in Saccharomyces cerevisiaeSpore number control and breeding inSaccharomyces cerevisiaeCytokinesis in yeast meiosis depends on the regulated removal of Ssp1p from the prospore membraneLive observation of forespore membrane formation in fission yeastThe anaphase promoting complex targeting subunit Ama1 links meiotic exit to cytokinesis during sporulation in Saccharomyces cerevisiaeRole of septins in the orientation of forespore membrane extension during sporulation in fission yeast.Mug28, a meiosis-specific protein of Schizosaccharomyces pombe, regulates spore wall formationThe Arf-GTPase-activating protein Gcs1p is essential for sporulation and regulates the phospholipase D Spo14p.The fission yeast pleckstrin homology domain protein Spo7 is essential for initiation of forespore membrane assembly and spore morphogenesisSporulation in the budding yeast Saccharomyces cerevisiae.Roles of septins in prospore membrane morphogenesis and spore wall assembly in Saccharomyces cerevisiaeThe Genomes of Three Uneven Siblings: Footprints of the Lifestyles of Three Trichoderma Species.Reduction of ribosome level triggers flocculation of fission yeast cells.Sorting signals within the Saccharomyces cerevisiae sporulation-specific dityrosine transporter, Dtr1p, C terminus promote Golgi-to-prospore membrane transport.Lipid droplet dynamics during Schizosaccharomyces pombe sporulation and their role in spore survival.Lipid droplets are central organelles for meiosis II progression during yeast sporulation.A visual screen of protein localization during sporulation identifies new components of prospore membrane-associated complexes in budding yeast.Spo5/Mug12, a putative meiosis-specific RNA-binding protein, is essential for meiotic progression and forms Mei2 dot-like nuclear fociDevelopmental Coordination of Gamete Differentiation with Programmed Cell Death in Sporulating Yeast.Dynamic localization of a yeast development-specific PP1 complex during prospore membrane formation is dependent on multiple localization signals and complex formation.The Mitotic Exit Network Regulates Spindle Pole Body Selection During Sporulation of Saccharomyces cerevisiae.
P2860
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P248
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P2860
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@ast
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@en
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@nl
type
label
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@ast
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@en
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@nl
prefLabel
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@ast
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@en
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@nl
P2093
P2860
P356
P1433
P1476
Prospore membrane formation linked to the leading edge protein (LEP) coat assembly.
@en
P2093
A C Moreno-Borchart
A Shevchenko
K Strasser
M G Finkbeiner
P2860
P304
P356
10.1093/EMBOJ/20.24.6946
P407
P577
2001-12-17T00:00:00Z