Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.
about
One of the nine doublet microtubules of eukaryotic flagella exhibits unique and partially conserved structuresThe neomuran revolution and phagotrophic origin of eukaryotes and cilia in the light of intracellular coevolution and a revised tree of lifeThe N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes.The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility.Conserved structural motifs in the central pair complex of eukaryotic flagella.Cryo-electron tomography of motile cilia and flagellaFAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein cThe nexin link and B-tubule glutamylation maintain the alignment of outer doublets in the ciliary axoneme.Slow axonemal dynein e facilitates the motility of faster dynein c.Role of cryo-ET in membrane bioenergetics research.Visualization of ATP synthase dimers in mitochondria by electron cryo-tomography.X-Ray Fiber Diffraction Recordings from Oriented Demembranated Chlamydomonas Flagellar AxonemesKnockdown 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.The CSC connects three major axonemal complexes involved in dynein regulationA Structural Basis for How Motile Cilia BeatProtein tagging reveals new insights into signaling in flagella.Big steps toward understanding dynein.Axoneme Structure from Motile Cilia.Genetic and genomic approaches to identify genes involved in flagellar assembly in Chlamydomonas reinhardtii.Chlamydomonas DYX1C1/PF23 is essential for axonemal assembly and proper morphology of inner dynein arms.Dynein-deficient flagella respond to increased viscosity with contrasting changes in power and recovery strokes.DRC2/CCDC65 is a central hub for assembly of the nexin-dynein regulatory complex and other regulators of ciliary and flagellar motility.A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1).The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility.Ciliary Motility: Regulation of Axonemal Dynein Motors.Fifty years of microtubule sliding in cilia.Four-dimensional analysis by high-speed holographic imaging reveals a chiral memory of sperm flagella.The IDA3 adapter, required for intraflagellar transport of I1 dynein, is regulated by ciliary length.
P2860
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P2860
Cryoelectron tomography reveals doublet-specific structures and unique interactions in the I1 dynein.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Cryoelectron tomography reveal ...... interactions in the I1 dynein.
@ast
Cryoelectron tomography reveal ...... interactions in the I1 dynein.
@en
type
label
Cryoelectron tomography reveal ...... interactions in the I1 dynein.
@ast
Cryoelectron tomography reveal ...... interactions in the I1 dynein.
@en
prefLabel
Cryoelectron tomography reveal ...... interactions in the I1 dynein.
@ast
Cryoelectron tomography reveal ...... interactions in the I1 dynein.
@en
P2093
P2860
P356
P1476
Cryoelectron tomography reveal ...... interactions in the I1 dynein
@en
P2093
Cynthia F Barber
Daniela Nicastro
Jeremy Krell
Mary E Porter
Matthew Rebesco
P2860
P304
P356
10.1073/PNAS.1120690109
P407
P577
2012-06-25T00:00:00Z