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The motility of axonemal dynein is regulated by the tubulin code.
scientific article published on December 2014
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4808650
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29 February 2020
title
The motility of axonemal dynein is regulated by the tubulin code
(English)
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4808650
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29 February 2020
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Jonathon Howard
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4
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4808650
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29 February 2020
Joshua Alper
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1
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4808650
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29 February 2020
author name string
Franziska Decker
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2
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29 February 2020
Bernice Agana
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3
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29 February 2020
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1 December 2014
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4808650
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29 February 2020
published in
Biophysical Journal
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4808650
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29 February 2020
volume
107
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29 February 2020
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12
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29 February 2020
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2872-2880
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4808650
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29 February 2020
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cites work
Effects of α-tubulin K40 acetylation and detyrosination on kinesin-1 motility in a purified system
1 reference
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PubMed Central
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Loss of MEC-17 leads to microtubule instability and axonal degeneration
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Displacement-weighted velocity analysis of gliding assays reveals that Chlamydomonas axonemal dynein preferentially moves conspecific microtubules
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Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro
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Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions
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Cryo-electron tomography reveals conserved features of doublet microtubules in flagella
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The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensation
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MEC-17 is an alpha-tubulin acetyltransferase
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PubMed Central
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Tubulin glutamylation regulates ciliary motility by altering inner dynein arm activity.
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Posttranslational modifications of tubulin and the polarized transport of kinesin-1 in neurons.
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Single molecule imaging reveals differences in microtubule track selection between Kinesin motors
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Lysine acetylation targets protein complexes and co-regulates major cellular functions
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The tubulin code
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PubMed Central
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Direct involvement of the isotype-specific C-terminus of beta tubulin in ciliary beating
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The E-hook of tubulin interacts with kinesin's head to increase processivity and speed
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Tubulin polyglutamylase enzymes are members of the TTL domain protein family
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Modulation of kinesin binding by the C-termini of tubulin
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The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
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The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
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Mechanochemical aspects of axonemal dynein activity studied by in vitro microtubule translocation
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Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardi
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Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms
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Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
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Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila
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Bending patterns of Chlamydomonas flagella: IV. Mutants with defects in inner and outer dynein arms indicate differences in dynein arm function
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Purification of tubulin from porcine brain.
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Tubulin polyglutamylation regulates axonemal motility by modulating activities of inner-arm dyneins.
1 reference
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21 August 2018
Systematic comparison of in vitro motile properties between Chlamydomonas wild-type and mutant outer arm dyneins each lacking one of the three heavy chains.
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21 August 2018
The C-termini of tubulin and the specific geometry of tubulin substrates influence the depolymerization activity of MCAK.
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21 August 2018
A targeted multienzyme mechanism for selective microtubule polyglutamylation
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21 August 2018
Tubulin polyglutamylation regulates flagellar motility by controlling a specific inner-arm dynein that interacts with the dynein regulatory complex
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/25658008
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Reconstitution of flagellar sliding
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/25658008
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/25658008
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Isolation of Chlamydomonas flagella and flagellar axonemes
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/25658008
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
High level expression of nonacetylatable alpha-tubulin in Chlamydomonas reinhardtii
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/25658008
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1016/J.BPJ.2014.10.061
1 reference
stated in
Europe PubMed Central
PMC publication ID
4808650
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25658008%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 February 2020
PMC publication ID
4808650
1 reference
stated in
Europe PubMed Central
PMC publication ID
4808650
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25658008%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 February 2020
PubMed publication ID
25658008
1 reference
stated in
Europe PubMed Central
PMC publication ID
4808650
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25658008%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 February 2020
ResearchGate publication ID
270217954
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