Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the ciliary tip during ciliary assembly - Wikidata - wikimedia - TriplyDB

Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the ciliary tip during ciliary assembly

Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the ciliary tip during ciliary assembly

http://www.wikidata.org/entity/Q34366058

about

The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells The awesome power of dikaryons for studying flagella and basal bodies in Chlamydomonas reinhardtii Single-particle imaging reveals intraflagellar transport-independent transport and accumulation of EB1 in Chlamydomonas flagella.Basal body multipotency and axonemal remodelling are two pathways to a 9+0 flagellum.Cryo-electron tomography of motile cilia and flagella The role of the dynein light intermediate chain in retrograde IFT and flagellar function in Chlamydomonas.The nexin link and B-tubule glutamylation maintain the alignment of outer doublets in the ciliary axoneme.Clarin-1 acts as a modulator of mechanotransduction activity and presynaptic ribbon assembly.The nphp-2 and arl-13 genetic modules interact to regulate ciliogenesis and ciliary microtubule patterning in C. elegans.In vivo investigation of cilia structure and function using Xenopus Joubert Syndrome in French Canadians and Identification of Mutations in CEP104 TTBK2: a tau protein kinase beyond tau phosphorylation.Posttranslational Modifications of Tubulin and Cilia.The Ciliopathy-Associated Cep104 Protein Interacts with Tubulin and Nek1 Kinase.Biophysical and Structural Characterization of the Centriolar Protein Cep104 Interaction Network Chlamydomonas FAP265 is a tubulin polymerization promoting protein, essential for flagellar reassembly and hatching of daughter cells from the sporangium.Human DNA helicase, RuvBL1 and its Chlamydomonas homologue, CrRuvBL1 plays an important role in ciliogenesis.Dynamics of the IFT machinery at the ciliary tip.Protein diversity in discrete structures at the distal tip of the trypanosome flagellum.Drosophila PLP assembles pericentriolar clouds that promote centriole stability, cohesion and MT nucleation.Switching dynein motors on and off.Analysis of Axonemal Assembly During Ciliary Regeneration in Chlamydomonas.

P2860

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P2860

Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the ciliary tip during ciliary assembly

http://www.wikidata.org/entity/Q34366058

description

2013 nî lūn-bûn

@nan

2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年学术文章

@wuu

2013年学术文章

@zh-cn

2013年学术文章

@zh-hans

2013年学术文章

@zh-my

2013年学术文章

@zh-sg

2013年學術文章

@yue

name

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@ast

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@en

Centrosomal protein CEP104

@nl

type

label

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@ast

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@en

Centrosomal protein CEP104

@nl

prefLabel

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@ast

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@en

Centrosomal protein CEP104

@nl

P1433

Q34366058-EEFAD96E-F1BD-4C0C-AEE6-CFB0A6D39791

P1476

Q34366058-436F2AAD-11E7-455B-B1C7-1DF9AEF73F8F

P2093

Q34366058-0A9A0A94-8CE5-4042-850C-2DEFF33C1F6B

Q34366058-4463F566-BCBA-4259-B353-E83E897406E0

Q34366058-554B15D6-0901-481A-A687-5646C2969763

Q34366058-F3F7D7F5-623D-46F9-804B-EFD37EBD5B4C

P2860

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Q34366058-0CBD4983-B40C-4FCA-A97F-CF91025F8D6F

Q34366058-1135279A-2A8B-4AB2-8E63-ABDF344C1E23

Q34366058-12BA00E9-EA40-48BF-A0DC-82E48DB716FC

Q34366058-135CE00D-90E0-4BE7-9979-0EB184E329E2

Q34366058-1A4179D6-570B-4CAF-B8B3-480AD8F44C37

Q34366058-1A8196C6-E015-4EDD-A6D8-A9866EF3A146

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P304

Q34366058-931A5624-5619-49D7-848B-ADFDD4124D91

P31

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P433

Q34366058-762B0DF8-864A-4BB7-8E28-B456A4644A1E

P478

Q34366058-5E32EA7D-BEE0-493A-BBF2-EAEBEA8DE344

P577

Q34366058-21DBD8A4-0213-49CF-920D-B383D3E923E5

P5875

Q34366058-ACF3B442-1A09-4B42-B089-E01454F4FE75

P698

Q34366058-FD0F2598-75FF-4916-AAD7-7355698235DC

P921

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P932

Q34366058-5309978E-D3F7-4230-9BF1-CE13B2E2790C

P356

P1433

Journal of Cell Science

P1476

Centrosomal protein CEP104 (Ch ...... ry tip during ciliary assembly

@en

P2093

Damayanti Tammana

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

Dennis R Diener

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

Joel Rosenbaum

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

Trinadh V Satish Tammana

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

P2860

Gli2 and Gli3 localize to cilia and require the intraflagellar transport protein polaris for processing and function

The intraflagellar transport protein IFT20 is associated with the Golgi complex and is required for cilia assembly

Novel asymmetrically localizing components of human centrosomes identified by complementary proteomics methods

The spinocerebellar ataxia-associated gene Tau tubulin kinase 2 controls the initiation of ciliogenesis

Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis

The microtubule affinity regulating kinase MARK4 promotes axoneme extension during early ciliogenesis.

Cep97 and CP110 suppress a cilia assembly program

A motility in the eukaryotic flagellum unrelated to flagellar beating

Polarity of flagellar assembly in Chlamydomonas

Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons

P304

5018-5029

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

P31

scholarly article

P356

10.1242/JCS.133439

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

P407

P433

Pt 21

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

P478

126

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

P577

2013-08-22T00:00:00Z

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

P5875

256085757

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P698

23970417

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

P921

P932

3820246

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