about
Role of secretory carrier membrane protein SCAMP2 in granule exocytosis.The BAR domain proteins: molding membranes in fission, fusion, and phagyA walk-through of the yeast mating pheromone response pathwayA role for a complex between activated G protein-coupled receptors in yeast cellular matingRegulation of mating and filamentation genes by two distinct Ste12 complexes in Saccharomyces cerevisiaeA mechanism for the coordination of proliferation and differentiation by spatial regulation of Fus2p in budding yeast.Prm1 prevents contact-dependent lysis of yeast mating pairs.Maintenance of mating cell integrity requires the adhesin Fig2pAntagonistic regulation of Fus2p nuclear localization by pheromone signaling and the cell cycleDynamic localization of yeast Fus2p to an expanding ring at the cell fusion junction during matingFunctional coupling of a nematode chemoreceptor to the yeast pheromone response pathwayFUS1 regulates the opening and expansion of fusion pores between mating yeast.The plasma membrane proteins Prm1 and Fig1 ascertain fidelity of membrane fusion during yeast mating.The so locus is required for vegetative cell fusion and postfertilization events in Neurospora crassaErgosterol promotes pheromone signaling and plasma membrane fusion in mating yeast.The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract.The Chlamydomonas Fus1 protein is present on the mating type plus fusion organelle and required for a critical membrane adhesion event during fusion with minus gametesNuclear fusion during yeast mating occurs by a three-step pathwayBiogenesis of the Saccharomyces cerevisiae pheromone a-factor, from yeast mating to human disease.Cell fusion and plasticity.An Amphiphysin-Like Domain in Fus2p Is Required for Rvs161p Interaction and Cortical Localization.Quantification of mutation-derived bias for alternate mating functionalities of the Saccharomyces cerevisiae Ste2p pheromone receptorMembrane lysis during biological membrane fusion: collateral damage by misregulated fusion machines.Membrane organization and cell fusion during mating in fission yeast requires multipass membrane protein Prm1Profiling a killer, the development of Cryptococcus neoformans.The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast matingSpecific protein targeting during cell differentiation: polarized localization of Fus1p during mating depends on Chs5p in Saccharomyces cerevisiae.Quantitation of yeast cell-cell fusion using multicolor flow cytometry.Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.Identification and characterization of LFD1, a novel protein involved in membrane merger during cell fusion in Neurospora crassa.The ancient claudin Dni2 facilitates yeast cell fusion by compartmentalizing Dni1 into a membrane subdomain.Endocytosis is essential for pathogenic development in the corn smut fungus Ustilago maydis.
P2860
Q24541551-851784B2-F66F-4C5C-AB17-D59F79BD7FC6Q24544126-298CA06E-B6B8-4290-87B1-E76ECD10786BQ24603343-B16FF605-DD80-4BDE-9A13-F9EC83F28085Q27478197-DC6534CD-1954-4756-B21C-A95A2013F8EEQ27932174-22DF6F89-80D0-4951-A0D6-D31579E310FEQ27933058-8F71F3C6-29E5-4EFC-8C7C-677B02D8EEC7Q27933298-318C89A1-6C0F-4DE3-87F0-177DEE1C3A17Q27933548-2DB193B9-252F-4CA8-AB5B-4A5C6EFD7E08Q27939695-8B35A829-DCBB-4910-9575-25DCD1D8AA46Q27939873-DE83D28E-B89B-417E-9E62-87111F0242B7Q28545110-89CE40D7-7C71-4153-8C50-29147074F5B5Q30477169-27AA4F71-28C5-4B5F-8047-0CBD25DB594AQ30478914-5EE1CAAB-9B40-4628-AB3C-A2C89971AC89Q33835964-E1690882-9238-48C7-9D24-61971DE4E59AQ34588776-5DD20124-2C3B-4D83-B0F3-46ABDEB1FFB8Q35144556-6754669D-B18A-4E83-B0A6-C25A5A2E003DQ35941507-E67BF066-8AFD-47A3-B46B-CE0C863ADBD4Q36149303-179EF587-DF55-4CD7-9E28-B20EA772E9BBQ36194945-2F15B080-3B35-4F89-9CF1-BE7D5C87B788Q36304585-3FC64686-8CBD-4AFB-BBAD-EB625506BD17Q36574539-1E752353-B9BC-4870-995B-BA69B456B316Q36941643-30313DAD-6CD4-4FFF-9F22-7E7F22A9E487Q37292928-CE5B27B2-6016-4606-B17E-0462BAAF594BQ37696337-2D9511A1-EE0C-4AC1-83FD-3DD8A773532AQ37887048-8AFAAF5C-9DBF-4557-95AE-8083B6B0ACEBQ39731297-2BCB811C-86E0-409D-914A-7EE14B3DA632Q39842673-8150A7EC-6334-4704-9F31-B8E0DAAE8DE6Q40879459-DD263E41-0CA2-4B8D-9403-75CC092725D7Q45234630-E7A0CB03-E407-42FC-9406-7CA8DAF085D3Q46455136-2B0518A8-8583-4C2A-AC6F-894BA149FFD9Q47183822-ED43B4FF-926C-4109-8E44-F9AFB8C57939Q48086500-053A7ABF-2103-4DDD-8AD1-2B9FBD930E0F
P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Yeast mating: getting close to membrane merger.
@ast
Yeast mating: getting close to membrane merger.
@en
type
label
Yeast mating: getting close to membrane merger.
@ast
Yeast mating: getting close to membrane merger.
@en
prefLabel
Yeast mating: getting close to membrane merger.
@ast
Yeast mating: getting close to membrane merger.
@en
P1433
P1476
Yeast mating: getting close to membrane merger
@en
P2093
P304
P356
10.1016/S0960-9822(00)00036-1
P407
P50
P577
2001-01-01T00:00:00Z