IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending - Wikidata - wikimedia - TriplyDB

IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending

IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending

http://www.wikidata.org/entity/Q28770082

about

Whole-exome capture and sequencing identifies HEATR2 mutation as a cause of primary ciliary dyskinesia Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella.Loss of ASP but not ROPN1 reduces mammalian ciliary motility Disruption of the A-kinase anchoring domain in flagellar radial spoke protein 3 results in unregulated axonemal cAMP-dependent protein kinase activity and abnormal flagellar motility Identification of a novel region of the cytoplasmic Dynein intermediate chain important for dimerization in the absence of the light chains.The flagellar motility of Chlamydomonas pf25 mutant lacking an AKAP-binding protein is overtly sensitive to medium conditions.IC138 defines a subdomain at the base of the I1 dynein that regulates microtubule sliding and flagellar motility Distinct roles of 1alpha and 1beta heavy chains of the inner arm dynein I1 of Chlamydomonas flagella.bop5 Mutations reveal new roles for the IC138 phosphoprotein in the regulation of flagellar motility and asymmetric waveforms Application of phosphoproteomics to find targets of casein kinase 1 in the flagellum of chlamydomonas.The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility.Mechanosignaling between central apparatus and radial spokes controls axonemal dynein activity Molecular architecture of inner dynein arms in situ in Chlamydomonas reinhardtii flagella.Slow axonemal dynein e facilitates the motility of faster dynein c.Drosophila Dynein intermediate chain gene, Dic61B, is required for spermatogenesis.Differential light chain assembly influences outer arm dynein motor function.The eukaryotic flagellum makes the day: novel and unforeseen roles uncovered after post-genomics and proteomics data.A novel ankyrin-repeat protein interacts with the regulatory proteins of inner arm dynein f (I1) of Chlamydomonas reinhardtii Regulation of ciliary motility: conserved protein kinases and phosphatases are targeted and anchored in the ciliary axoneme An axonemal PP2A B-subunit is required for PP2A localization and flagellar motility.Building blocks of the nexin-dynein regulatory complex in Chlamydomonas flagella.The Pcdp1 complex coordinates the activity of dynein isoforms to produce wild-type ciliary motility Whole-Genome Sequencing to Identify Mutants and Polymorphisms in Chlamydomonas reinhardtii.Knockdown of Inner Arm Protein IC138 in Trypanosoma brucei Causes Defective Motility and Flagellar Detachment.The ciliary inner dynein arm, I1 dynein, is assembled in the cytoplasm and transported by IFT before axonemal docking.A conserved CaM- and radial spoke associated complex mediates regulation of flagellar dynein activity Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.Three members of the LC8/DYNLL family are required for outer arm dynein motor function IC97 is a novel intermediate chain of I1 dynein that interacts with tubulin and regulates interdoublet sliding.Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii.Regulation of dynein-driven microtubule sliding by the axonemal protein kinase CK1 in Chlamydomonas flagella Novel LC8 mutations have disparate effects on the assembly and stability of flagellar complexes.The Chlamydomonas mutant pf27 reveals novel features of ciliary radial spoke assembly.Sperm flagella: comparative and phylogenetic perspectives of protein components.Discrete PIH proteins function in the cytoplasmic preassembly of different subsets of axonemal dyneins.Dyneins across eukaryotes: a comparative genomic analysis.Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways.Targeted copy number screening highlights an intragenic deletion of WDR63 as the likely cause of human occipital encephalocele and abnormal CNS development in zebrafish.Novel Mutations in CFAP44 and CFAP43 Cause Multiple Morphological Abnormalities of the Sperm Flagella (MMAF).

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IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending

http://www.wikidata.org/entity/Q28770082

description

2004 nî lūn-bûn

@nan

2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

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IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

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type

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IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

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IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

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IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

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IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

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MBC.E04-08-0694

P1433

Molecular Biology of the Cell

P1476

IC138 is a WD-repeat dynein in ...... egulation of flagellar bending

@en

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Catherine A Perrone

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

Joshua Mueller

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

Kristin Wuichet

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

Mary E Porter

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Paul Griffin

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Pinfen Yang

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

Triscia W Hendrickson

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Winfield S Sale

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P2860

Loss-of-function mutations in a human gene related to Chlamydomonas reinhardtii dynein IC78 result in primary ciliary dyskinesia.

The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility

Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes

The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2

The 2.0 A crystal structure of a heterotrimeric G protein

Crystal structure of a G-protein beta gamma dimer at 2.1A resolution

1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin

The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif

The WD repeat: a common architecture for diverse functions

The ancient regulatory-protein family of WD-repeat proteins

P304

5431-42

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scholarly article

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10.1091/MBC.E04-08-0694

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12

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15

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2004-12-01T00:00:00Z

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8245723

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15469982

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532023

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