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Long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by decreasing alpha-tubulin (show TUBA4A Proteins) acetylation in breast cancer.
Results show that Tuba1a plays an essential, noncompensated role in neuronal saltatory migration in vivo and highlight the importance of microtubule flexibility in nucleus-centrosome coupling and neuronal-branching regulation during neuronal migration.
Data show that retinal endothelial cells (HREC) treated with low molecular weight fraction of commercial 5% human serum albumin (show ALB Proteins) (LMWF5A) exhibit a rapid increase in the amount and distribution of acetylated alpha-tubulin (show TUBA4A Proteins).
The C-terminal tail from the tubulin beta (show TUBB Proteins) I isotype, but not the beta III isotype, formed contacts in the putative binding site of a recently discovered antineoplastic peptide that disrupts microtubule formation in glioma cells.
TUBA1B (show TUBA1B Proteins)/ESR1 (show ESR1 Proteins) gene interaction might play pivotal roles in the occurrence and development of Postmenopausal Osteoporosis.
data suggest that the TUBA1A mutations disrupting lateral interactions have pronounced dominant-negative effects on microtubule dynamics that are associated with the severe end of the lissencephaly spectrum
Taken together our data provide valuable information regarding the interaction of CK1delta and a-tubulin (show TUBB Proteins) and a novel approach for the development of pharmacological tools to inhibit proliferation of cancer cells.
Data show that tubulin (show TUBB Proteins) phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
Data show that plasma membrane Ca(2+)-ATPase (show ATP2B2 Proteins) (PMCA) was associated with tubulin (show TUBB Proteins) in normotensive and hypertensive erythrocytes.
Data suggest that tubulin (show TUBB Proteins) functionally interact with the vimentin (show VIM Proteins) network in a cell-type specific manner.
Collectively, these findings suggest that Smo and primary cilia-dependent noncanonical Hh signaling leads to post-translational regulation of microtubules and may be important for modulating cell behaviors.
Further PS treatment resulted in recovery of axonal outgrowth and enhanced retrograde axonal transport by decreasing histone deacetylase 6 (HDAC6 (show HDAC6 Proteins)) levels and thus increasing acetylation of alpha-tubulin (show TUBA4A Proteins) levels. Thus, we have identified the molecular pathway that leads to neurodegeneration in FD and have demonstrated that phosphatidylserine treatment has the potential to slow progression of neurodegeneration
mass spectrometry-based quantitative comparison of acetylated peptides from wild-type vs HDAC6 (show HDAC6 Proteins) knockout mice allowed to identify six new deacetylation sites possibly mediated by HDAC6 (show HDAC6 Proteins).
These results give new insights into the functions of Tuba1a, mechanisms for regulating tubulin (show TUBB Proteins) proteostasis, and how compromising these may lead to neural defects.
Data indicate that alpha 1a tubulin (show TUBB Proteins) (Tuba1a) showed the least variability in expression among the different stages of lung development.
Tubulin-tyrosine ligase (TTL (show TTL Proteins)) is required to increase the levels of tyrosinated alpha-tubulin (show TUBA4A Proteins) at the axon injury site and plays an important role in injury signaling.
Data suggest a mechanistic link between tubulin (show TUBB Proteins) hyperacetylation and autophagy induction.
TFIIB (show GTF2B Proteins) co-localizes and interacts with alpha-tubulin (show TUBA4A Proteins) during oocyte meiosis in the mouse and depletion of TFIIB (show GTF2B Proteins) causes arrest of subsequent embryo development.
Acetylation of alpha-tubulin (show TUBA4A Proteins) is under the control of the acetyltransferase MEC-17 (show C6orf134 Proteins) and deacetylases SIRT2 (Sirtuin 2 (show SIRT2 Proteins)) and HDAC6 (histone deacetylase 6 (show HDAC6 Proteins)). Adipocyte development is inhibited in MEC-17 (show C6orf134 Proteins)-knockdown cells, but enhanced in MEC-17 (show C6orf134 Proteins)-overexpressing cells.
Unambiguous identification of novel glutamylation sites E441 and E443 in mouse brain Tuba1a and Tuba1b (show TUBA1B Proteins).
TTL (show TTL Proteins) has specifically evolved to recognize and modify tubulin (show TUBB Proteins).
LRRK2 (show LRRK2 Proteins) plays an important role as a physiological regulator for phosphorylation-mediated dissociation of tau from microtubules.
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain.
tubulin, alpha 1a
, tubulin alpha-1A chain-like
, alpha tubulin1
, tubulin alpha-3 chain
, tubulin, alpha 3d
, tubulin, alpha 3e
, tubulin B-alpha-1
, tubulin alpha-1A chain
, tubulin, alpha, brain-specific
, Talpha1 alpha-tubulin
, alpha-tubulin 1
, alpha-tubulin isotype M-alpha-1
, tubulin alpha-1 chain
, tubulin, alpha 1
, alpha-tubulin 3
, tubulin, alpha 3
, alpha tubulin
, alpha-tubulin ubiquitous
, tubulin K-alpha-1
, tubulin alpha-1B chain
, tubulin alpha-ubiquitous chain
, tubulin, alpha, ubiquitous
, tubulin, alpha 1 (testis specific)
, tubulin, alpha 6
, alpha-tubulin 3/7
, alpha-tubulin isotype M-alpha-3/7
, tubulin alpha-3/alpha-7 chain
, tubulin, alpha 7
, tubulin, alpha 3B
, tubulin alpha-8 chain
, tubulin, alpha 2