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first study describing features of human triosephosphate isomerase S-nitrosylation
Disease-associated variants change well-conserved residues in the protein's sequence and affect protein stability.
A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease has been presented. (Review)
Results revealed that TPI expression might be considered as a novel prognostic factor to evaluate gastric cancer patients' survival
TPI1 functions as a tumor suppressor in hepatocellular carcinoma and might serve as a potential therapeutic target for the treatment of HCC
our findings are the first to identify, to our knowledge, a functional synaptic defect in TPI deficiency derived from molecular changes in the TPI dimer interface.
Polyvinylpyrrolidone stabilised silver nanoparticles (60 nM; 2-6 nm diameter) selectively inhibited PfTIM with a 7-fold decrease in enzyme catalytic efficiency (K(cat)/K(m)) over hTIM.
results suggest amyloid-beta oligomers induce neuronal death by triggering methylglyoxal(MG) production; increased release of MG is a direct consequence of triosephosphate isomerase nitrotyrosination due to amyloid-beta peptide action at the 2 tyrosines associated with the catalytic center
TPI-PEP co-crystal structure, demonstrating that PEP directly binds into the catalytic pocket of TPI.
E104D mutant is highly susceptible to proteolysis, which in all likelihood contributes to the pathogenesis of enzymopathy. In addition, the proteolysis data on wild type HsTIM illustrate an asymmetric conduct of the two monomers.
Data suggest that exchange reactions during gluconeogenesis catalyzed by triose-phosphate isomerase and transaldolase do not differ between subjects with type 2 diabetes and control subjects under fasting or hyperglycemic conditions.
we review the relationship between modified TPI and Alzheimer disease (AD), highlighting the relevance of this protein in AD pathology
study found promoter SNPs of CKB and TPI1 were weakly associated with schizophrenia;in addition, IFNG polymorphisms were associated with schizophrenia; results suggest that IFNG and proteins affected by IFNG may play a role in the pathogenesis of schizophrenia
[Review] The activity of glycolytic enzyme TPI reveals a mechanistic link between energy metabolism and age-related proteostatic dysfunction which can suppress generation of altered proteins that characterize the aged phenotype in cells and tissues.
A patient with triosephosphate isomerase-deficiency was found to be homozygous for a Val231Met mutation.
A proteomic approach for identification and localization of the pericellular components of chondrocytes.
structural changes rather than abnormal catalysis may play an important role in the clinical manifestations of TPI deficiency; the postulated high aggregation ability of the unstable Glu104Asp mutant would lead to more serious symptoms
TPI1 were up-regulated with the malignancy of prostate cancer cell lines and have their potential as serum biomarkers for indicating the developmental stage of prostate cancer.
of two previously undescribed mutations: c.722 T>C (Phe240Ser) and c.28 insG; each of the two unrelated patients showed the new mutation in compound heterozygosity with the most common variant Glu104Asp, resulting in a very severe clinical pattern.
This protein has been found differentially expressed in thalami from patients with schizophrenia.
TPI interacts with Tau protein in a normal, nondisease state as well as in a neurodegenerative state.
Triosephosphate isomerase activity-deficient mice show haemolytic anaemia in homozygous condition
data indicate that Tipin/Tim1/And1 form a complex that links stabilization of replication fork and establishment of sister chromatid cohesion
Sperm TPI content and amounts of GPX5 in seminal plasma may be used as quality markers of boar sperm.
TPI sugarkill can be genetically complemented by TPI encoding a catalytically inactive enzyme.
Mutation of wasted away, a recessive, hypomorphic mutation of triosephosphate isomerase (Tpi), highlights the essential protective role of triosephosphate isomerase.
This gene encodes an enzyme, consisting of two identical proteins, which catalyzes the isomerization of glyceraldehydes 3-phosphate (G3P) and dihydroxy-acetone phosphate (DHAP) in glycolysis and gluconeogenesis. Mutations in this gene are associated with triosephosphate isomerase deficiency. Pseudogenes have been identified on chromosomes 1, 4, 6 and 7. Alternative splicing results in multiple transcript variants.
, triosephosphate isomerase
, Triose-phosphate isomerase
, triosephosphate isomerase 1
, triosephosphate isomerase (TIM, D-glyceraldehyde 3-phosphate ketol-isomerase)
, triosephoshpate isomerase
, neurodegeneration 14
, triose phosphate isomerase
, wasted away
, triose-phosphate isomerase A
, triosephosphate isomerase A