α-Tubulin acetylation from the inside out

scientific article

α-Tubulin acetylation from the inside out is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2012PNAS..10919515A
P356DOI10.1073/PNAS.1217594109
P932PMC publication ID3511746
P698PubMed publication ID23150594
P5875ResearchGate publication ID233412164

P50authorKevin D CorbettQ38327382
P2093author name stringJawdat Al-Bassam
P2860cites workMEC-17 is an alpha-tubulin acetyltransferaseQ24299301
Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylationQ24300995
A BBSome subunit links ciliogenesis, microtubule stability, and acetylationQ24336047
The conserved Bardet-Biedl syndrome proteins assemble a coat that traffics membrane proteins to ciliaQ24337528
The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediateQ27639749
Structural Basis for Histone and Phosphohistone Binding by the GCN5 Histone AcetyltransferaseQ27642329
Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBPQ27650912
Atomic resolution structure of human  -tubulin acetyltransferase bound to acetyl-CoAQ27674573
Lysine acetylation targets protein complexes and co-regulates major cellular functionsQ27860589
The major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensationQ28000035
Post-translational regulation of the microtubule cytoskeleton: mechanisms and functionsQ34232911
Genetically separable functions of the MEC-17 tubulin acetyltransferase affect microtubule organizationQ36055162
Posttranslational acetylation of α-tubulin constrains protofilament number in native microtubulesQ36894917
Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and functionQ37290564
Ciliary and flagellar structure and function--their regulations by posttranslational modifications of axonemal tubulinQ37988055
MEC-17 deficiency leads to reduced α-tubulin acetylation and impaired migration of cortical neurons.Q48379537
Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysineQ69940175
P433issue48
P407language of work or nameEnglishQ1860
P304page(s)19515-19516
P577publication date2012-11-13
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleα-Tubulin acetylation from the inside out
P478volume109

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cites work (P2860)
Q39297835Activation of AMP-activated Protein Kinase by Metformin Induces Protein Acetylation in Prostate and Ovarian Cancer Cells
Q28662026Independent localization of plasma membrane and chloroplast components during eyespot assembly
Q26753208Post-translational modification-regulated leukocyte adhesion and migration
Q90350244Posttranslational modification of plant microtubules
Q90759990RTN4 Knockdown Dysregulates the AKT Pathway, Destabilizes the Cytoskeleton, and Enhances Paclitaxel-Induced Cytotoxicity in Cancers
Q38874926Role of the Tau N-terminal region in microtubule stabilization revealed by new endogenous truncated forms
Q28834427TgATAT-Mediated α-Tubulin Acetylation Is Required for Division of the Protozoan Parasite Toxoplasma gondii
Q38135829The diversity of histone versus nonhistone sirtuin substrates.

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