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induced pluripotent stem cells (iPSCs) from the umbilical cord and peripheral blood of two lissencephaly patients with different clinical severities carrying alpha tubulin (zeige TUBA4A Proteine) (TUBA1A) missense mutations, were generated.
Long intergenic non-coding RNA APOC1P1-3 inhibits apoptosis by decreasing alpha-tubulin (zeige TUBA4A Proteine) 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 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
Data show that tubulin (zeige TUBB Proteine) phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
Data show that plasma membrane Ca(2+)-ATPase (zeige ATP2B2 Proteine) (PMCA) was associated with tubulin (zeige TUBB Proteine) in normotensive and hypertensive erythrocytes.
Data suggest that tubulin (zeige TUBB Proteine) functionally interact with the vimentin (zeige VIM Proteine) network in a cell-type specific manner.
Studies indicate that alpha-tubulin (zeige TUBA4A Proteine) acetylation and microtubule level is mainly governed by opposing actions of alpha-tubulin acetyltransferase 1 (ATAT1 (zeige C6orf134 Proteine)) and histone deacetylase 6 (HDAC6 (zeige HDAC6 Proteine)).
Data from studies using peptide fragment of alpha-tubulin (zeige TUBA4A Proteine) (residues 31-49) suggest that Ser38 is crucial for substrate recognition by alpha-tubulin (zeige TUBA4A Proteine) acetylase 1 (ATAT1 (zeige C6orf134 Proteine)); Asp39, Ile42, the glycine stretch (residues 43-45), and Asp46 are also involved.
Lysine 40 acetylation of alpha-tubulin (zeige TUBA4A Proteine) does not result in significant changes in kinesin-1's landing rate or motility parameters.
Here the authors demonstrate that mice lacking the alpha-tubulin (zeige TUBA4A Proteine) acetyltransferase Atat1 (zeige C6orf134 Proteine) in sensory neurons display profound deficits in their ability to detect mechanical stimuli.
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 (zeige HDAC6 Proteine)) levels and thus increasing acetylation of alpha-tubulin (zeige TUBA4A Proteine) 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 (zeige HDAC6 Proteine) knockout mice allowed to identify six new deacetylation sites possibly mediated by HDAC6 (zeige HDAC6 Proteine).
These results give new insights into the functions of Tuba1a, mechanisms for regulating tubulin (zeige TUBB Proteine) proteostasis, and how compromising these may lead to neural defects.
Data indicate that alpha 1a tubulin (zeige TUBB Proteine) (Tuba1a) showed the least variability in expression among the different stages of lung development.
Tubulin-tyrosine ligase (TTL (zeige TTL Proteine)) is required to increase the levels of tyrosinated alpha-tubulin (zeige TUBA4A Proteine) at the axon injury site and plays an important role in injury signaling.
Data suggest a mechanistic link between tubulin (zeige TUBB Proteine) hyperacetylation and autophagy induction.
TFIIB (zeige GTF2B Proteine) co-localizes and interacts with alpha-tubulin (zeige TUBA4A Proteine) during oocyte meiosis in the mouse and depletion of TFIIB (zeige GTF2B Proteine) causes arrest of subsequent embryo development.
Acetylation of alpha-tubulin (zeige TUBA4A Proteine) is under the control of the acetyltransferase MEC-17 (zeige C6orf134 Proteine) and deacetylases SIRT2 (Sirtuin 2 (zeige SIRT2 Proteine)) and HDAC6 (histone deacetylase 6 (zeige HDAC6 Proteine)). Adipocyte development is inhibited in MEC-17 (zeige C6orf134 Proteine)-knockdown cells, but enhanced in MEC-17 (zeige C6orf134 Proteine)-overexpressing cells.
Lys40 of alpha-tubulin (zeige TUBA4A Proteine) acetylation directly weakens inter-protofilament interactions.
the role of the human TBCE and TBCB (zeige TBCB Proteine) chaperones in alpha-tubulin (zeige TUBA4A Proteine)-beta-tubulin (zeige TUBB Proteine) dissociation, was investigated.
Data suggest presence of unstructured C-terminal tubulin (zeige TUBB Proteine) tail in Vdac1 (zeige VDAC1 Proteine) pore (voltage-dependent anion channel 1 (zeige VDAC1 Proteine)) decreases pore's conductance and switches pore's selectivity from anionic to cationic rendering ATP transport virtually impossible.
TTL (zeige TTL Proteine) has specifically evolved to recognize and modify tubulin (zeige TUBB Proteine).
VDAC phosphorylation is an important determinant of its interaction with dimeric tubulin (zeige TUBB Proteine).
LRRK2 (zeige LRRK2 Proteine) plays an important role as a physiological regulator for phosphorylation-mediated dissociation of tau from microtubules.
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins. The genes encoding these microtubule constituents belong to the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes, which are highly conserved among species. This gene encodes alpha tubulin and is highly similar to the mouse and rat Tuba1 genes. Northern blotting studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells. This gene is one of three alpha-tubulin genes in a cluster on chromosome 12q. Mutations in this gene cause lissencephaly type 3 (LIS3) - a neurological condition characterized by microcephaly, mental retardation, and early-onset epilepsy and caused by defective neuronal migration. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, tubulin alpha-1 chain
, tubulin alpha-1A chain
, tubulin, alpha 1
, tubulin B-alpha-1
, tubulin alpha-3 chain
, tubulin, alpha, brain-specific
, alpha-tubulin 3
, tubulin, alpha 3
, Talpha1 alpha-tubulin
, alpha-tubulin isotype M-alpha-1
, alpha-tubulin ubiquitous
, tubulin K-alpha-1
, tubulin alpha-1B chain
, tubulin alpha-ubiquitous chain
, tubulin, alpha 1a
, tubulin alpha-1A chain-like
, Alpha-tubulin 1
, Tubulin alpha-1 chain
, tubulin alpha 3
, Alpha-tubulin 2
, Alpha-tubulin II
, Tubulin alpha-2 chain
, alpha-tubulin II
, tubulin alpha 1a L homeolog