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alphaTAT1 has a conserved function as the major alpha-tubulin acetyltransferase in ciliated organisms and has an important role in regulating subcellular specialization of subsets of microtubules.
Data indicate that alpha-tubulin acetyltransferase 1 Atat1 (zeige C6orf134 ELISA Kits) is not required for survival and development but may regulate more advanced functions.
Acetylation of alpha-tubulin (zeige TUBA4A ELISA Kits) is under the control of the acetyltransferase MEC-17 (zeige C6orf134 ELISA Kits) and deacetylases SIRT2 (Sirtuin 2 (zeige SIRT2 ELISA Kits)) and HDAC6 (histone deacetylase 6 (zeige HDAC6 ELISA Kits)). Adipocyte development is inhibited in MEC-17 (zeige C6orf134 ELISA Kits)-knockdown cells, but enhanced in MEC-17 (zeige C6orf134 ELISA Kits)-overexpressing cells.
Tat-DJ-1 protein (zeige PARK7 ELISA Kits) protects against dopaminergic neuronal cell death in 1-methyl-4-phenyl-1,2,3,6,-tetrahydropyridine (MPTP (zeige PTPN2 ELISA Kits))-induced PD mouse models.
Sequencing of TAT indicated two new homozygous mutations p.L312P (c.935T>C) and p.T408M (c.1223C>T) for the proband and his asymptomatic sister.
Two known mutations and one novel mutation was found in the TAT gene of Tunesian Richner-Hanhart syndrome patients. The geographical distribution of RHS mutations shows regional specificities.
The high potential application of Tat and its entrapment in elastic cationic niosomes for development of a transdermal gene delivery system are described.
A paternal inherited frameshift mutation c.1213delCinsAG at codon 405 causing a premature stop codon, and a maternally inherited deletion of 193kb encompassing the complete TAT gene yield the first complete TAT deletion in tyrosinaemia type II described.
tumor suppressive mechanism of TAT was associated with its proapoptotic role in a mitochondrial-dependent manner by promoting cytochrome-c (zeige CYCS ELISA Kits) release and activating caspase-9 (zeige CASP9 ELISA Kits) and PARP (zeige COL11A2 ELISA Kits).
a silent exonic transversion in TAT causes complete missplicing by exon 11 skipping in oculocutaneous tyrosinaemia type II
Genetically modified adenoviral vector with the protein transduction domain of Tat improves gene transfer to CAR-deficient cells.
This nuclear gene encodes a mitochondrial protein tyrosine aminotransferase which is present in the liver and catalyzes the conversion of L-tyrosine into p-hydroxyphenylpyruvate. Mutations in this gene cause tyrosinemia (type II, Richner-Hanhart syndrome), a disorder accompanied by major skin and corneal lesions, with possible mental retardation. A regulator gene for tyrosine aminotransferase is X-linked.
Novel DUF738 containing protein (2610110G12Rik)
, acetyltransferase mec-17 homolog
, alpha-tubulin N-acetyltransferase
, tyrosine aminotransferase
, tyrosine aminotransferase-like
, L-tyrosine:2-oxoglutarate aminotransferase
, tyrosine aminotransferase, cytosolic
, tyrosine transaminase