Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization. - Wikidata - awgldk - TriplyDB

Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization.

Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization.

http://www.wikidata.org/entity/Q42645529

about

VLN2 Regulates Plant Architecture by Affecting Microfilament Dynamics and Polar Auxin Transport in Rice Arabidopsis RIC1 Severs Actin Filaments at the Apex to Regulate Pollen Tube Growth Plant Actin-binding Protein SCAB1 Is Dimeric Actin Cross-linker with Atypical Pleckstrin Homology Domain A mutation in MRH2 kinesin enhances the root hair tip growth defect caused by constitutively activated ROP2 small GTPase in Arabidopsis Dynamin2 GTPase and cortactin remodel actin filaments.RNA-seq analysis of an apical meristem time series reveals a critical point in Arabidopsis thaliana flower initiation A systems-wide comparison of red rice (Oryza longistaminata) tissues identifies rhizome specific genes and proteins that are targets for cultivated rice improvement.Proteins implicated in mediating self-incompatibility-induced alterations to the actin cytoskeleton of Papaver pollen.Cotton LIM domain-containing protein GhPLIM1 is specifically expressed in anthers and participates in modulating F-actin.Bundling actin filaments from membranes: some novel players Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array.Arabidopsis CROLIN1, a novel plant actin-binding protein, functions in cross-linking and stabilizing actin filaments Swiprosin-1 modulates actin dynamics by regulating the F-actin accessibility to cofilin.Building distinct actin filament networks in a common cytoplasm.Biophysics of actin filament severing by cofilin Actin dynamics, architecture, and mechanics in cell motility.Plant villins: versatile actin regulatory proteins.CASEIN KINASE1-LIKE PROTEIN2 Regulates Actin Filament Stability and Stomatal Closure via Phosphorylation of Actin Depolymerizing Factor.The plant-specific actin binding protein SCAB1 stabilizes actin filaments and regulates stomatal movement in Arabidopsis.The Structurally Plastic CH2 Domain Is Linked to Distinct Functions of Fimbrins/Plastins.Root hairs.ACTIN BINDING PROTEIN 29 from Lilium pollen plays an important role in dynamic actin remodeling.Arabidopsis LIM proteins: a family of actin bundlers with distinct expression patterns and modes of regulation.Cucumber mosaic virus movement protein severs actin filaments to increase the plasmodesmal size exclusion limit in tobacco.LIM Proteins: A Novel Class of Actin Cytoskeleton Organizers in Plants.An Arabidopsis class II formin, AtFH19, nucleates actin assembly, binds to the barbed end of actin filaments, and antagonizes the effect of AtFH1 on actin dynamics.The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1.Phosphatidylinositol 3- and 4-phosphate modulate actin filament reorganization in guard cells of day flower.Change in the actin cytoskeleton during seismonastic movement of Mimosa pudica.Arabidopsis actin-depolymerizing factor7 severs actin filaments and regulates actin cable turnover to promote normal pollen tube growth.Tobacco WLIM1 is a novel F-actin binding protein involved in actin cytoskeleton remodeling.The Actin Cytoskeleton: Functional Arrays for Cytoplasmic Organization and Cell Shape Control.Arabidopsis VILLIN2 and VILLIN3 are required for the generation of thick actin filament bundles and for directional organ growth.GhVLN4 is involved in cell elongation via regulation of actin organization.Isolation of Actin and Actin-Binding Proteins.BENT UPPERMOST INTERNODE1 encodes the class II formin FH5 crucial for actin organization and rice development.Arabidopsis FIMBRIN5, an actin bundling factor, is required for pollen germination and pollen tube growth.14-3-3 λ protein interacts with ADF1 to regulate actin cytoskeleton dynamics in Arabidopsis.Cold stress contributes to aberrant cytokinesis during male meiosis I in a wheat thermosensitive genic male sterile line.Arabidopsis VILLIN2 and VILLIN3 act redundantly in sclerenchyma development via bundling of actin filaments

P2860

Q27318438-0F91870C-DEF8-4AFC-A409-6B75A7F0D6A4 Q27319424-180780DE-518E-41E2-AD00-BD90AC1D0340 Q27677422-0FE81CD1-7126-4EB9-844C-C3C4CDB1D26F Q28469328-3231E3DE-4E84-4077-99D3-584781E71EEC Q30434848-06D1E5A7-9295-4E43-8E15-0E45EB9467E4 Q33360947-620227D9-B9B3-4CBC-A2FD-C4856D901665 Q35093202-611BE329-56DF-4D78-A36A-5AE76F083A80 Q35205950-E878C95E-F8E5-4756-A279-47979B4D4F2B Q35311388-F5D40D52-756D-4AE8-8BA0-50214E2D37DB Q36186455-485D5425-D28D-4AE6-BAB4-EE70B76CFFEF Q37124867-C85614C6-9A9D-43A7-977E-54B78D0E690A Q37289194-9C0538EF-6B45-44A6-BCAE-BCCCDCB15F6A Q37314350-918AA09A-3E57-43AB-A063-17EA2ACA9F8C Q37904227-2EA0E81A-721C-483F-8BB9-CAD7AFD20DAB Q38080358-0BCEA67F-E073-4102-AE27-6809DB4D9E05 Q38175137-21768E17-DFEA-44D8-98E6-1FADCF709617 Q38258023-8934EFCC-BEDA-4907-8B96-8F20E0A6659C Q39628861-FDC58D14-C0F7-4C90-A53B-C2B00E57BDF3 Q39629097-2304174B-44D7-4381-8260-B7B4E31C8EE5 Q41046232-4614D576-A9B2-49C1-AC3D-3CA9D8D2ACDC Q41486874-260779DF-756A-4FA7-936D-DB5EBD910C07 Q42624358-A0356691-5E30-43EB-8B3A-8AD1EA6804C3 Q42917421-FC7D4096-5B2E-48A3-A828-D1567E4933D8 Q43076989-397509CD-293D-4028-962A-2044247FEC74 Q43190171-99DF932D-406C-4BF0-BE4C-1447AF8ADC5D Q45835791-B3E31E54-A352-4D9E-BD78-06059BBB00BB Q46581093-9D749808-7187-414E-B8CC-2718292452E8 Q46844334-AAE6F9A0-05E7-4B77-A8E9-5E82EE50BDB4 Q46952931-056EBE11-6AE7-4798-921E-9401D8A60A36 Q48037631-A5839BB3-1A48-4220-B0DC-D2E7C99CC338 Q48085379-86922B2F-F4F8-4B96-B148-0DB5160587F3 Q48207127-B6BCFA5B-478D-4923-92C1-337CF172EB54 Q50505065-70F897F5-2B7B-466B-A3FC-6BC8F95675E3 Q50925542-13DB6317-1811-49A6-A6FD-2DB140953AD5 Q51404375-12003D48-E327-4BE5-B159-37F127B91E49 Q51607599-A2075113-4FE0-41B5-8C3A-9CB385AE91F2 Q52605318-2E1168F1-4E55-44B6-BB49-A0A41A9273D2 Q52919033-1C316DC1-A993-4254-8878-BC6FE4C8DD6F Q53290438-98F5A5E1-6F36-44C6-B796-C56D6942393C Q58944184-66C0D383-FD9D-4047-8ACA-65387082B404

P2860

Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization.

http://www.wikidata.org/entity/Q42645529

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@en

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@nl

type

label

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@en

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@nl

prefLabel

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@en

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@nl

P1433

Q42645529-31BD306D-9734-4AA7-A878-C6AC103F4346

P1476

Q42645529-F485C7C5-D9A2-42B6-9D91-7407F7C98D86

P2093

Q42645529-37EB096C-F1FB-4BBA-BD1A-D9950525885C

Q42645529-46A69B2D-61F5-4284-AC82-6FC6F4FE53E2

Q42645529-AC7709B0-8F41-4614-B7BB-405760301D11

Q42645529-E32EC6E1-CFE6-449C-ABF9-9E9A33A71076

Q42645529-FF1F1AEE-E3FA-471F-92EC-E2AD8C08133E

P2860

Q42645529-01B36C4C-F089-48B3-B4E3-47FB9A237DB4

Q42645529-053ED108-605D-4A4C-93A5-C3E78917F1C1

Q42645529-0581AB59-7DBF-4555-86B1-8ECA154C9021

Q42645529-084FFE3A-D631-4ADF-9A11-AECD671085F7

Q42645529-136D4898-0986-4A96-9FC2-72524267C5B9

Q42645529-16FF68B5-881A-4232-8A4C-F5CDD7258C50

Q42645529-1C69F888-027E-484F-A720-FA3EF711D66B

Q42645529-2737633C-9FD6-4391-BF13-236C8186CC8D

Q42645529-2D5A95D7-EED3-4D25-8B0F-57152060803A

Q42645529-2DC271D6-8198-42FE-A246-200B9AE3AB30

P304

Q42645529-87D5F079-3CF2-4DB5-ACEB-65533DEC8ED2

P31

Q42645529-AA2B6BCB-CA89-46C9-B7B2-A8CA60AF13E0

P356

Q42645529-98765994-888B-4404-9D57-C93CE7603B61

P433

Q42645529-6FC7A217-8B2B-4ACC-AFA9-B9E178E03B95

P478

Q42645529-3E04348E-819C-40DE-8708-3831E8BBEB18

P50

Q42645529-A65036B3-76F3-41A2-8DA0-620A8422600B

Q42645529-C1F12A8C-2944-4B6C-8579-4B364C5BAEE0

P577

Q42645529-B7029090-DB3A-4569-936F-981C2B30BE31

P5875

Q42645529-945C41C9-E08A-4D62-AAA8-4DE024C1DCDC

P698

Q42645529-344B2AF6-AEE9-41C8-BE1A-29B977A4C9F3

P921

Q42645529-389C04F9-1F1F-4F77-BB15-5E0915E3D32C

P932

Q42645529-D0D6CBD0-E84C-4E80-929C-B045C856532C

P356

P1433

P1476

Arabidopsis VILLIN1 generates ...... resistant to depolymerization.

@en

P2093

Arnaud Brunet

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

Christopher J Staiger

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

Lisa Y Gao

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

Shanjin Huang

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

Tracie Matsumoto

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

P2860

Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity

Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin

The ADF/cofilin family: actin-remodeling proteins.

Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis

Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF

Villin sequence and peptide map identify six homologous domains

Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility

The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex

The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation

Villin function in the organization of the actin cytoskeleton. Correlation of in vivo effects to its biochemical activities in vitro

P304

486-501

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

P31

scholarly article

P356

10.1105/TPC.104.028555

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

P433

2

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

P478

17

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

P50

Robert C Robinson

Laurent Blanchoin

P577

2005-01-19T00:00:00Z

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

P5875

8071082

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

P698

15659626

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

P921

P932

548821

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