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Thiamin pyrophosphokinase 1

Thiamin Pyrophosphokinase, thiamine pyrophosphokinase, TPKI
This gene encodes a protein, that exists as a homodimer, which catalyzes the conversion of thiamine to thiamine pyrophosphate. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, ACID, transketolase, AML1, STEP
Papers on Thiamin Pyrophosphokinase
Examination of the effects of thiamine and thiamine pyrophosphate on Doxorubicin-induced experimental cardiotoxicity.
Akcay et al., Erzurum, Turkey. In J Cardiovasc Pharmacol Ther, Mar 2015
BACKGROUND AND PURPOSE: To investigate the effect of thiamine and thiamine pyrophosphate on doxorubicin-induced cardiotoxicity biochemically and histopathologically and to examine whether doxorubicin cardiotoxicity is related to the conversion of thiamine into thiamine pyrophosphate and inhibition of thiamine pyrophosphokinase (TPK) enzyme.
Bioinformatic and metabolomic analysis reveals miR-155 regulates thiamine level in breast cancer.
Chang et al., Seoul, South Korea. In Cancer Lett, Mar 2015
The results showed the expression of two thiamine transporter genes (SLC19A2, SLC25A19) as well as thiamine pyrophosphokinase-1 (TPK1) were decreased in both RNA and protein level in miR-155 dependent manner.
Characterization of Thiamin Phosphate Kinase in the Hyperthermophilic Archaeon Pyrobaculum calidifontis.
Nosaka et al., In J Nutr Sci Vitaminol (tokyo), 2014
Many eubacterial cells directly synthesize thiamin pyrophosphate by the phosphorylation of thiamin phosphate by thiamin phosphate kinase (ThiL), whereas this final step occurs in two stages in eukaryotic cells and some eubacterial cells: hydrolysis of thiamin phosphate to free thiamin and its pyrophosphorylation by thiamin pyrophosphokinase.
Chronic Nicotine Exposure In Vivo and In Vitro Inhibits Vitamin B1 (Thiamin) Uptake by Pancreatic Acinar Cells.
Said et al., West Haven, United States. In Plos One, 2014
Furthermore, expression of the important thiamin-metabolizing enzyme, thiamin pyrophosphokinase (TPKase), was significantly reduced in PAC of mice exposed to nicotine.
Expanding the clinical and molecular spectrum of thiamine pyrophosphokinase deficiency: a treatable neurological disorder caused by TPK1 mutations.
Mayr et al., Manchester, United Kingdom. In Mol Genet Metab, 2014
Thiamine pyrophosphokinase (TPK) produces thiamine pyrophosphate, a cofactor for a number of enzymes, including pyruvate dehydrogenase and 2-ketoglutarate dehydrogenase.
Up-regulation of vitamin B1 homeostasis genes in breast cancer.
Govindarajan et al., Athens, United States. In J Nutr Biochem, 2013
Intracellular availability of thiamine is facilitated by the activity of thiamine transporters and thiamine pyrophosphokinase-1 (TPK-1).
Chemical and genetic validation of thiamine utilization as an antimalarial drug target.
Saliba et al., Canberra, Australia. In Nat Commun, 2012
Overexpression of thiamine pyrophosphokinase (the enzyme that converts thiamine into its active form, thiamine pyrophosphate) hypersensitizes parasites to oxythiamine by up to 1,700-fold, consistent with oxythiamine being a substrate for thiamine pyrophosphokinase and its conversion into an antimetabolite.
Identification of the thiamin pyrophosphokinase gene in rainbow trout: characteristic structure and expression of seven splice variants in tissues and cell lines and during embryo development.
Li et al., East Lansing, United States. In Comp Biochem Physiol B Biochem Mol Biol, 2012
Thiamin pyrophosphokinase (TPK) converts thiamin to its active form, thiamin diphosphate.
Thiamine pyrophosphokinase deficiency in encephalopathic children with defects in the pyruvate oxidation pathway.
Sperl et al., Salzburg, Austria. In Am J Hum Genet, 2012
Mutation analysis of TPK1 uncovered three missense, one splice-site, and one frameshift mutation resulting in decreased TPK protein levels
Assembly and sorting of the tonoplast potassium channel AtTPK1 and its turnover by internalization into the vacuole.
Vitale et al., Milano, Italy. In Plant Physiol, 2011
TPK1 must assemble correctly to pass endoplasmic reticulum quality control.
The biochemical study on the etiology of Alzheimer's disease.
Imahori, Tokyo, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2009
Then we have proved that TPKI is upregulated in AD brain but not in control brain.
Thiamin diphosphate in biological chemistry: new aspects of thiamin metabolism, especially triphosphate derivatives acting other than as cofactors.
Wins et al., Liège, Belgium. In Febs J, 2009
Among the proteins involved in thiamin metabolism, thiamin transporters, thiamin pyrophosphokinase and a soluble 25-kDa thiamin triphosphatase have been characterized at the molecular level, in contrast to thiamin mono- and diphosphatases whose specificities remain to be proven.
TPK1, a Ca(2+)-regulated Arabidopsis vacuole two-pore K(+) channel is activated by 14-3-3 proteins.
Hedrich et al., Würzburg, Germany. In Plant J, 2007
findings show that AtTPK1 (KCO1), interacts with 14-3-3 proteins (general regulating factors, GRFs; TPK1 seems to provide for a Ca(2+)- and 14-3-3-sensitive mechanism capable of controlling cytoplasmic potassium homeostasis in plants
Three common intronic variants in the maternal and fetal thiamine pyrophosphokinase gene (TPK1) are associated with birth weight.
Bougneres et al., Paris, France. In Ann Hum Genet, 2007
Genomic variations in either the fetal or maternal TPK1 gene could contribute to variability of birth weight in normal humans.
The two-pore channel TPK1 gene encodes the vacuolar K+ conductance and plays a role in K+ homeostasis.
Maathuis et al., York, United Kingdom. In Proc Natl Acad Sci U S A, 2007
The two-pore channel TPK1 gene encodes the vacuolar K+ conductance and plays a role in K+ homeostasis.
GSK-3 is essential in the pathogenesis of Alzheimer's disease.
Takashima, Wako, Japan. In J Alzheimers Dis, 2005
GSK-3beta has exactly the same oligonucleotide sequence as tau-protein kinase I (TPKI), which was first purified from the microtubule fraction of bovine brain.
Possible role of tau protein kinases in pathogenesis of Alzheimer's disease.
Uchida et al., Machida, Japan. In Neurobiol Aging, 1998
Immunostaining with anti-TPKI antibody indicated that this kinase is up-regulated in AD brain.
Physiology and pathology of tau protein kinases in relation to Alzheimer's disease.
Uchida et al., Machida, Japan. In J Biochem, 1997
Since prior phosphorylation of tau by TPKII strongly enhanced the action of TPKI, it was thought that TPKII was involved in the formation of PHF-tau in concert with TPKI.
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