She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae. - Wikidata - wikimedia - TriplyDB

She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae.

She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q39890714

about

Myosin chaperones UCS protein Rng3p is essential for myosin-II motor activity during cytokinesis in fission yeast UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster The Myosin Chaperone UNC-45 Is Organized in Tandem Modules to Support Myofilament Formation in C. elegans Cytokinesis depends on the motor domains of myosin-II in fission yeast but not in budding yeast.Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway.Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast.Initial polarized bud growth by endocytic recycling in the absence of actin cable-dependent vesicle transport in yeast.Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast.A quantitative imaging-based screen reveals the exocyst as a network hub connecting endocytosis and exocytosis.Triangle network motifs predict complexes by complementing high-error interactomes with structural information.Getting folded: chaperone proteins in muscle development, maintenance and disease.Transformation of Saccharomyces cerevisiae and other fungi: methods and possible underlying mechanism.The UNC-45 myosin chaperone: from worms to flies to vertebrates.Drosophila UNC-45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability.RNA asymmetric distribution and daughter/mother differentiation in yeast Daughter-specific repression of Saccharomyces cerevisiae HO: Ash1 is the commander.Tracking UNC-45 chaperone-myosin interaction with a titin mechanical reporter.Motor protein Myo5p is required to maintain the regulatory circuit controlling WOR1 expression in Candida albicans RNA localization in yeast: moving towards a mechanism.Dual function of the UNC-45b chaperone with myosin and GATA4 in cardiac development UCS protein Rng3p activates actin filament gliding by fission yeast myosin-II.Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril Yeast UCS proteins promote actomyosin interactions and limit myosin turnover in cells.Classifying transcription factor targets and discovering relevant biological features.The myosin-binding UCS domain but not the Hsp90-binding TPR domain of the UNC-45 chaperone is essential for function in Caenorhabditis elegans Septin ring assembly requires concerted action of polarisome components, a PAK kinase Cla4p, and the actin cytoskeleton in Saccharomyces cerevisiae.Principles of mRNA transport in yeast.Here, there, everywhere. mRNA localization in budding yeast Of social molecules: The interactive assembly of ASH1 mRNA-transport complexes in yeast.Essential role of the NH2-terminal region of Cdc24 guanine nucleotide exchange factor in its initial polarized localization in Saccharomyces cerevisiae.Mutation of the Ser18 phosphorylation site on the sole Saccharomyces cerevisiae UCS protein, She4, can compromise high-temperature survival.Rng3, a member of the UCS family of myosin co-chaperones, associates with myosin heavy chains cotranslationally.Structural insight into the UNC-45-myosin complex.UCS protein function is partially restored in the Saccharomyces cerevisiae she4 mutant with expression of the human UNC45-GC, but not UNC45-SM.Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast.UNC-45a promotes myosin folding and stress fiber assembly.

P2860

Q26863588-8E9900F6-8978-42F4-84F4-9E44D95CAB02 Q27302780-7E3C4A1E-60A7-43FF-88CF-913DD06D9777 Q27666105-0A5A69E5-17C0-4C18-9E58-15348DD42D81 Q27667259-FC42D1D4-F2E7-4730-BFB4-841B53386F40 Q27675937-3C8DF70C-D766-4FD6-B3E0-4F4BF06C8553 Q27933611-F48FA0DE-526F-4203-BA11-ED4D5F296226 Q27933703-DF5E66D3-9DF0-4A0A-8873-BAE068F7C14B Q27939959-A8ED5F0E-5B76-49D7-AC17-99CA3827F2C0 Q27940028-10149102-7B4B-443C-977E-0EE80655DACE Q30435835-2275B81F-51E6-4636-B5C5-926451F2F746 Q30528962-C4660333-C443-442D-9747-0DA3E176B6D7 Q30664635-63BD811C-A775-45C7-9DDF-89CD65E8D6FD Q33475174-0E0840AE-729F-471B-A888-27B1F3864D54 Q34055646-D9786452-94A0-45C6-B6B9-965EDA619540 Q34176111-CFD27C0E-88E0-4AF0-9145-24CD82CE48E5 Q34477894-5F0D0C01-2D32-4114-AFFE-A51504CFF58D Q34574189-BF03FD67-445B-4BFE-8C70-7D89F59192BC Q35602957-2C628243-C79E-471E-B9F8-4E7F198E59C2 Q35906140-FA774138-4066-4E3A-82E0-928205B13ED9 Q35926209-C06240E9-E11E-4779-B471-23D9DBC5E311 Q35941030-DC46E251-82D0-46EA-9244-A13ED5B11869 Q35985189-753061AB-772F-4565-B383-FEBD669AD170 Q36290852-5062A7F0-E386-4425-8C58-96AE92781A30 Q36322706-09A40625-1379-4303-89AC-71BF84BE332D Q36534622-2207C42D-04A1-4B33-AA87-66D8855ED7B7 Q36725660-E81B587B-703A-4AB0-9597-F59ECA33060A Q36739744-DE9725FA-2418-4D29-8D33-D2A27A0D1B25 Q36995989-463F95AE-8315-4A79-9A58-C0499A293F16 Q37657258-00050C6D-66AA-4F5B-8C1C-8C518E7DDD5D Q37967198-D1B3E080-761F-4F3E-B24C-7CF6D597161C Q38284523-2B94E5BF-A457-4372-A7D7-C6A8E3CC6692 Q38284527-07DA0747-5830-4102-8D26-8721065A3C93 Q40322541-88F65B89-3FBD-494E-9494-E47CD53282F8 Q41176499-9C4EFA12-329F-418A-ADE1-8D0E733E69A5 Q41839057-A48973B2-9807-4B2B-9761-2D90BFDDCFA4 Q45223476-85D9910E-314E-4933-94AE-78B4B2C976BF Q47243892-498E0061-363B-42EB-8EFC-CF7CEA2AFCA2 Q47359029-8D27DB9A-C2B1-4EE9-9CE6-9FAA2E7EBAF3 Q47621531-A057F32A-DBC8-4C91-A2CA-F854259A042C

P2860

She4p/Dim1p interacts with the motor domain of unconventional myosins in the budding yeast, Saccharomyces cerevisiae.

http://www.wikidata.org/entity/Q39890714

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh

2003年學術文章

@zh-hant

name

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@en

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@nl

type

label

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@en

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@nl

prefLabel

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@en

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@nl

P1433

Q39890714-26315C38-74C5-41B2-8596-065807D9D8AE

P1476

Q39890714-F2669616-E451-426E-B4FE-75E9F03C91CF

P2093

Q39890714-3A59336E-C571-41FF-BD01-68B9472A743B

Q39890714-7A3ABCFD-A967-4A41-ABBD-DA935DC0B456

Q39890714-85FA5FD1-5E1C-4AE3-B314-151AFC9205B4

Q39890714-A5FD2EE1-F3BC-44E3-8E19-FBEAE4180311

Q39890714-CC48374C-1C11-450E-81AC-E7531E5D28DF

Q39890714-F96B2F23-F44D-46C9-9F9D-464A9868986D

P2860

Q39890714-0A56AFF1-040B-4E1F-9A17-BF12AB4478F2

Q39890714-0E4EB863-E6FC-4389-9FDD-1456CAFB3D39

Q39890714-215ACAD6-F992-4EC4-8093-61E19D6CB52A

Q39890714-241CD859-BE05-481F-9E29-7361E07D05E5

Q39890714-24778F39-BD4C-40FD-8C8B-8C7CA9640CC6

Q39890714-24BECE37-D6C9-4BDC-950C-0B015FFCFE19

Q39890714-2837F561-07D1-454B-ADED-1347D4425841

Q39890714-2BFC3508-7DEF-442E-A4ED-32BCF0ACC442

Q39890714-2D8E3D96-50C8-45AB-B0D8-395FAFACC65D

Q39890714-30569FA0-F813-4B34-9608-0C42B921472E

P304

Q39890714-40894EF1-2A51-4412-AE4A-8C328CFFFFE8

P31

Q39890714-77F0C594-DFBA-4F0A-8158-8B4C1B909108

P356

Q39890714-FFB0C2E2-5238-4717-832D-DC93D82C9BDB

P433

Q39890714-1A16C5F3-68D8-4BDB-9263-DB72FB83BE09

P478

Q39890714-13A8948E-DEFD-4FAF-9423-692C3B1169BD

P577

Q39890714-D5553DF1-D621-42FE-98A7-B2DD5D577AAE

P698

Q39890714-7FB42CA3-A4F4-4CEA-AD5C-22686EA35643

P921

Q39890714-F118CCF1-B49F-489E-8E03-06EAF503D9CC

P932

Q39890714-37F74E49-8177-45D3-8975-DC8F1F437FEF

P356

MBC.E02-09-0616

P1433

Molecular Biology of the Cell

P1476

She4p/Dim1p interacts with the ...... ast, Saccharomyces cerevisiae.

@en

P2093

Hirofumi Toi

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

Kazuma Tanaka

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

Kenji Irie

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

Konomi Fujimura-Kamada

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

Satoru Todo

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

Yoshimi Takai

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

P2860

Crystal structure of the motor domain of a class-I myosin.

Three-dimensional structure of myosin subfragment-1: a molecular motor

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

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

A generic protein purification method for protein complex characterization and proteome exploration

Identification of asymmetrically localized determinant, Ash1p, required for lineage-specific transcription of the yeast HO gene.

Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA.

The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae

Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae.

Polarization of cell growth in yeast. I. Establishment and maintenance of polarity states.

P304

2237-2249

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

P31

scholarly article

P356

10.1091/MBC.E02-09-0616

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

P433

6

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

P478

14

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

P577

2003-02-06T00:00:00Z

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

P698

12808026

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

P921

Saccharomyces cerevisiae

P932

194874

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