Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p. - Wikidata - wikimedia - TriplyDB

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

http://www.wikidata.org/entity/Q36381135

about

Septin function in yeast model systems and pathogenic fungi.Analysis of mammalian septin expression in human malignant brain tumors The yeast actin cytoskeleton: from cellular function to biochemical mechanism The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast Unique spatiotemporal activation pattern of Cdc42 by Gef1 and Scd1 promotes different events during cytokinesis.Rho1- and Pkc1-dependent phosphorylation of the F-BAR protein Syp1 contributes to septin ring assembly.The small GTP-binding proteins AgRho2 and AgRho5 regulate tip-branching, maintenance of the growth axis and actin-ring-integrity in the filamentous fungus Ashbya gossypii Septins from the phytopathogenic fungus Ustilago maydis are required for proper morphogenesis but dispensable for virulence Phosphorylation of Bem2p and Bem3p may contribute to local activation of Cdc42p at bud emergence.Activation of the Cdc42p GTPase by cyclin-dependent protein kinases in budding yeast.Pxl1p, a paxillin-like protein in Saccharomyces cerevisiae, may coordinate Cdc42p and Rho1p functions during polarized growth.The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast.Bud3 activates Cdc42 to establish a proper growth site in budding yeast.Daughter cell identity emerges from the interplay of Cdc42, septins, and exocytosis Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle.Septin collar formation in budding yeast requires GTP binding and direct phosphorylation by the PAK, Cla4.Role of a Cdc42p effector pathway in recruitment of the yeast septins to the presumptive bud site.Cdc42p and Fus2p act together late in yeast cell fusion.Adjacent positioning of cellular structures enabled by a Cdc42 GTPase-activating protein-mediated zone of inhibition.A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous growth pathway in yeast.The identification of Pcl1-interacting proteins that genetically interact with Cla4 may indicate a link between G1 progression and mitotic exit Shs1 plays separable roles in septin organization and cytokinesis in Saccharomyces cerevisiae.Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae.Role of the septin ring in the asymmetric localization of proteins at the mother-bud neck in Saccharomyces cerevisiae.The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms.Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast.Distinct roles of Rho1, Cdc42, and Cyk3 in septum formation and abscission during yeast cytokinesis.A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast Septin Organization and Functions in Budding Yeast Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments Here come the septins: novel polymers that coordinate intracellular functions and organization Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins.Hob3p, the fission yeast ortholog of human BIN3, localizes Cdc42p to the division site and regulates cytokinesis.Role of nucleotide binding in septin-septin interactions and septin localization in Saccharomyces cerevisiae The yeast endocytic protein Epsin 2 functions in a cell-division signaling pathway.Dynamics of septin ring and collar formation in Saccharomyces cerevisiae.Inhibition of Cdc42 during mitotic exit is required for cytokinesis.Septin assemblies form by diffusion-driven annealing on membranes Pkc1 acts through Zds1 and Gic1 to suppress growth and cell polarity defects of a yeast eIF5A mutant

P2860

Q24533502-BB95D0FA-BDB9-469B-A70D-52339397E73C Q24550903-7972EE23-B12E-4008-ADF0-6371A8C0257C Q24669945-E33B98FF-6F5D-47C6-8286-A8D9CEE8A1A7 Q26753023-3FCD145B-F6B0-41D2-B036-4CD925D9BF2D Q26778771-C179ECB4-6DCC-4F88-B7F2-523C721086C8 Q27304958-8B75CBD7-C4CA-494A-9958-2F6D3C0CE605 Q27305424-B9D279A1-1745-468D-9922-A03932E1B7BB Q27313505-292A91F1-1AE5-419E-B4D0-41FC982529E8 Q27319443-AA217EC2-F016-40C8-8B10-0BC2127BA77F Q27932112-8C282D06-821B-4E41-98A1-C2FBD2CD125A Q27932231-6468FCB3-CB34-4FBB-A58A-8E03DC2A058E Q27933264-781FFC54-1413-4E76-A05A-91C379AFE95A Q27933947-8C82432D-6902-4761-A6BC-94746EDD2014 Q27933962-350A12BC-4754-4FFE-9C0C-B50CF155336F Q27934066-47447562-4DD9-481C-A6B2-0293823E9885 Q27935008-F1376345-2E6E-4B70-9E7A-76C7655757D6 Q27935649-C73476B1-F8FE-4FCA-98FA-F903F650BCFE Q27936436-88FBC1A8-9C53-4508-82D5-6A8D47C90201 Q27937292-D7819CB2-593F-4E38-AC9C-008AEF54FE88 Q27937709-A2FA36DF-AC25-4E3B-BBB6-DA538EE2B81A Q27938083-81B0331A-654E-4AF3-B1F6-569B4471A943 Q27938470-DC263D90-1277-4793-9C57-571CCF1D5B4C Q27938523-35981FF8-39E3-4753-A032-2FD89F203DA6 Q27938690-0D2E3502-395F-4581-AC2B-E9FC47025505 Q27939421-AAB137A5-D27F-4CCE-960D-24B26891935A Q27939498-9AD73FD8-4B2B-4A2A-8535-E551EECAE2B9 Q27939574-582D516B-1B35-4147-BDC1-E170D0AB935D Q27939851-E46BEBC6-B61A-40BB-8257-4F616EEB3534 Q27940239-06125723-6D0B-4649-9788-19A88C4D5FEA Q28071347-2131253C-C666-4757-9D4E-DF66AE5AD528 Q28215790-DE5ED69B-95EA-4253-BB35-1FB40EBD58DD Q28510832-132F5204-B359-4ABD-92C0-031154D1AEB2 Q30445918-C64D5C00-0CEC-4664-A37D-8A22BEBF1CEC Q30479235-35931B95-C299-4535-86CE-365CBC185CB1 Q30483185-17CEDC6F-95E7-4EF6-A377-0FDEB01A501A Q30488557-C97330DC-E0DB-40C5-B267-82C65FC1306D Q30539580-3F7B485F-9762-45AA-950B-A73618AEE483 Q30541691-3A69195B-6698-4BA4-9900-F89B0516CB8F Q30571994-A4689E45-DCEC-433F-ABBD-30275AAD0F2F Q33223205-FA59AB11-9F2E-421E-ADA6-EBD7F0EAEFAC

P2860

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

http://www.wikidata.org/entity/Q36381135

description

2002 nî lūn-bûn

@nan

2002年の論文

@ja

2002年学术文章

@wuu

2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

2002年學術文章

@zh

2002年學術文章

@zh-hant

name

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@ast

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@en

type

label

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@ast

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@en

prefLabel

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@ast

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@en

P1433

Q36381135-A01BEC8E-55B1-4097-A383-767B3F626B13

P1476

Q36381135-99B708C4-E361-4252-A4D1-D06DFDBF9286

P2093

Q36381135-0BF598ED-2E22-4D69-9622-66CB2496D2F4

Q36381135-2C955CDE-FCB0-4FE8-B096-6E32C5D38147

Q36381135-B5CDD733-FEF1-42EF-A327-BCF2A4013A00

Q36381135-D289FD02-DD98-4AFF-ACFB-2D0DCDA76529

Q36381135-DAD3D815-C17A-43B3-ABEB-97754A55A66A

P2860

Q36381135-01A0E317-B187-46A2-BEA7-894C2BE61AC2

Q36381135-03303A33-EAA4-47C0-B128-A43F0B0331BE

Q36381135-0379CD9D-5933-4D18-99F5-CA5DFB3883D8

Q36381135-10640A20-3D9D-48E0-B8D1-77A19B27A449

Q36381135-12BD2AA1-EAB1-4AC3-8E48-AD689D4544F8

Q36381135-1D4A2300-0635-4264-A157-6F34A3A56630

Q36381135-2330D2F3-47E9-404D-9429-03176858DF8A

Q36381135-234BEC33-73FD-4CBA-B1A5-BD2B59B51084

Q36381135-2EAA358F-23B3-4F87-9A5E-AD0FFE93BC69

Q36381135-41641C25-00E9-48E8-BC53-8339DEDF1C4D

P304

Q36381135-EB6D0A0B-7F23-4276-8F55-87B02B511761

P31

Q36381135-A634743A-3ECF-4C9D-AF06-3B20B48ACBA9

P356

Q36381135-4367A9A7-094B-4C2F-A314-2E09961963B8

P407

Q36381135-6A1B172D-5FF2-4A1B-BAB4-4BD7C31EA32C

P433

Q36381135-5E542F97-350F-452B-942D-CA5957797DFE

P478

Q36381135-6A69D48C-5D9D-46DC-9CDA-FB642D6914C3

P577

Q36381135-0704076D-B766-4FB6-9093-7A4E4F2FF755

P5875

Q36381135-29B82BCF-FA15-4E63-A59A-947D3236D409

P698

Q36381135-9C100FF9-F9D7-47D2-84F2-50749E1B38D4

P932

Q36381135-7659800B-BA3B-4713-882D-52C1007C514B

P356

P1433

Journal of Cell Biology

P1476

Septin ring assembly involves cycles of GTP loading and hydrolysis by Cdc42p.

@en

P2093

Amy S Gladfelter

http://www.w3.org/2001/XMLSchema#string

Daniel J Lew

http://www.w3.org/2001/XMLSchema#string

Elaine S G Bardes

http://www.w3.org/2001/XMLSchema#string

Indrani Bose

http://www.w3.org/2001/XMLSchema#string

Trevin R Zyla

http://www.w3.org/2001/XMLSchema#string

P2860

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

Ras2 signals via the Cdc42/Ste20/mitogen-activated protein kinase module to induce filamentous growth in Saccharomyces cerevisiae

A morphogenesis checkpoint monitors the actin cytoskeleton in yeast

Identification of novel, evolutionarily conserved Cdc42p-interacting proteins and of redundant pathways linking Cdc24p and Cdc42p to actin polarization in yeast

Mutation of RGA1, which encodes a putative GTPase-activating protein for the polarity-establishment protein Cdc42p, activates the pheromone-response pathway in the yeast Saccharomyces cerevisiae.

Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis.

Assembly of scaffold-mediated complexes containing Cdc42p, the exchange factor Cdc24p, and the effector Cla4p required for cell cycle-regulated phosphorylation of Cdc24p.

Cdc28 tyrosine phosphorylation and the morphogenesis checkpoint in budding yeast.

Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function.

The septins: roles in cytokinesis and other processes

P304

315-326

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1083/JCB.200109062

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

156

http://www.w3.org/2001/XMLSchema#string

P577

2002-01-21T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11552317

http://www.w3.org/2001/XMLSchema#string

P698

11807094

http://www.w3.org/2001/XMLSchema#string

P932

2199227

http://www.w3.org/2001/XMLSchema#string