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The pyruvate dehydrogenase (PDH) complex is located in the mitochondrial matrix and catalyzes the conversion of pyruvate to acetyl coenzyme A. De plus, nous expédions Pyruvate Dehydrogenase Complex, Component X Protéines (9) et et beaucoup plus de produits pour cette protéine.
Showing 10 out of 66 products:
Human Polyclonal PDHX Primary Antibody pour IHC (p), ELISA - ABIN547434
Roche, Baker, Yan, Hiromasa, Gong, Peng, Dong, Turkan, Kasten: Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms. dans Progress in nucleic acid research and molecular biology 2001
Human Polyclonal PDHX Primary Antibody pour IHC (p), ELISA - ABIN544818
Ling, McEachern, Seyda, MacKay, Scherer, Bratinova, Beatty, Giovannucci-Uzielli, Robinson: Detection of a homozygous four base pair deletion in the protein X gene in a case of pyruvate dehydrogenase complex deficiency. dans Human molecular genetics 1998
Show all 3 Pubmed References
Human Polyclonal PDHX Primary Antibody pour IHC (p), IHC - ABIN250349
Schild, Ruhs, Beiter, Zügel, Hudemann, Reimer, Krumholz-Wagner, Wagner, Keller, Eder, Krüger, Krüger, Braun, Nieß, Steinacker, Mooren: Basal and exercise induced label-free quantitative protein profiling of m. vastus lateralis in trained and untrained individuals. dans Journal of proteomics 2015
We propose testing for the R446* mutation in PDHX as a rapid first screening in Roma infants with metabolic acidosis.
MiR-26a regulates glucose metabolism of colorectal cancer cells by direct targeting PDHX.
New mutation in PDHX gene found in two unrelated patients with Pyruvate dehydrogenase deficiency.
genetic association with systemic lupus erythematosus to a haplotype between PDHX and CD44 was established.
determination that PDH and complex III exist at a steady-state ratio of 1:100, 1:128 and 1:202 in HeLa cell extracts, fibroblast mitochondria and heart tissue mitochondria, respectively
model of the pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and binding of the E1 and E3 components
specificity of pairing for human E3BP with E3 from its subcomplex structure to be most likely due to conformational rigidity of the binding fragment of the E3-binding domain of E3BP and its exquisite amino acid match with the E3 target interface
A cluster of disease-causing E3 mutations located near the center of the E3BD/E3 interface prevents the efficient recruitment of these E3 variants by E3BP into the PDC, leading to the dysfunction of the PDC catalytic machine.
These data provide an additional case of E3BP deficiency with a unique and previously unreported deletion in the PDHX gene.
Despite the presence of antibodies reactive with PDC-E3BP in the majority of primary biliary cirrhosis (PBC) patients this self-protein is not a dominant T-cell autoantigen in PBC.
PDHX-assisted photosensitization with rose Bengal induces structural and functional alteration of mitochondria in HeLa cells.
T1a/podoplanin is first expressed in prox 1-positive lymphatic progenitor cells, with predominant localization in the luminal plasma membrane of lymphatic endothelial cells during later development.
In islet cells both fat and glucose regulate PDK gene and protein expression and indicate that hyperglycemia and hyperlipidemia contribute to the decline in diabetic islet PDH activity by increasing mRNA and protein expression of PDK.
This study showed that the recombinant and bovine E2/E3BP cores bind E3s with a 2:1 stoichiometry, and propose that mammalian PDC comprises a heterogeneous population of assemblies incorporating a network of E3 cross-bridges above the core surface.
The pyruvate dehydrogenase (PDH) complex is located in the mitochondrial matrix and catalyzes the conversion of pyruvate to acetyl coenzyme A. The PDH complex thereby links glycolysis to Krebs cycle. The PDH complex contains three catalytic subunits, E1, E2, and E3, two regulatory subunits, E1 kinase and E1 phosphatase, and a non-catalytic subunit, E3 binding protein (E3BP). This gene encodes the E3 binding protein subunit\; also known as component X of the pyruvate dehydrogenase complex. This protein tethers E3 dimers to the E2 core of the PDH complex. Defects in this gene are a cause of pyruvate dehydrogenase deficiency which results in neurological dysfunction and lactic acidosis in infancy and early childhood. This protein is also a minor antigen for antimitochondrial antibodies. These autoantibodies are present in nearly 95% of patients with the autoimmune liver disease primary biliary cirrhosis (PBC). In PBC, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed. PBC eventually leads to cirrhosis and liver failure. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
pyruvate dehydrogenase complex, component X
, pyruvate dehydrogenase protein X component, mitochondrial-like
, dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
, lipoyl-containing pyruvate dehydrogenase complex component X
, pyruvate dehydrogenase complex, E3-binding protein subunit
, pyruvate dehydrogenase complex, lipoyl-containing component X
, pyruvate dehydrogenase protein X component, mitochondrial
, dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex (E3-binding protein) (proX)
, E3-binding protein
, pyruvate dehydrogenase protein X component