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The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and carbon dioxide, and provides the primary link between glycolysis and the tricarboxylic acid. Additionally we are shipping Pyruvate Dehydrogenase beta Proteins (20) and Pyruvate Dehydrogenase beta Kits (18) and many more products for this protein.
Showing 10 out of 58 products:
Human Polyclonal PDHB Primary Antibody for IF (p), IHC (p) - ABIN752833
Xing, Yuan, Xu, Gu, Liang, Lu: Proteomic identification of mitochondrial targets involved in andrographolide sodium bisulfite-induced nephrotoxicity in a rat model. in Environmental toxicology and pharmacology 2015
Human Monoclonal PDHB Primary Antibody for IHC (p), ELISA - ABIN562157
Coupland, Vorum, Mandal, Kalirai, Honoré, Urbak, Lake, Dopierala, Damato: Proteomics of uveal melanomas suggests HSP-27 as a possible surrogate marker of chromosome 3 loss. in Investigative ophthalmology & visual science 2010
Cow (Bovine) Polyclonal PDHB Primary Antibody for IHC, WB - ABIN2783247
Okajima, Korotchkina, Prasad, Rupar, Phillips, Ficicioglu, Hertecant, Patel, Kerr: Mutations of the E1beta subunit gene (PDHB) in four families with pyruvate dehydrogenase deficiency. in Molecular genetics and metabolism 2008
PDHB was downregulated in nasopharyngeal carcinoma cells. Forced expression of PDHB in NPC (show NPC1 Antibodies) cells inhibited cell growth and migration, while knocking down the expression of PDHB promoted the growth, migration, and tumorigenesis of NPC (show NPC1 Antibodies) cells. PDHB inhibited ERK (show EPHB2 Antibodies) signaling and cell growth driven by RasV12.
Data indicate that (pro)renin receptor (show ATP6AP2 Antibodies) ATP6PA2 interacts with the E1 beta subunit (show POLG Antibodies) of pyruvate dehydrogenase (show PDP Antibodies) and controlling its protein stability
PHD3 (show EGLN3 Antibodies) depletion did not affect the expression of the PDH (show PDP Antibodies)-E1alpha, E1beta, and E2 subunits, or the phosphorylation status of E1alpha, but destabilized the PDH (show PDP Antibodies) complex (PDC (show PNKD Antibodies)), resulting in less functional PDC (show PNKD Antibodies).
Sequencing of PDHB reveals a homozygous point mutation (c.302T>C), causing a predicted amino acid change in patient 1. Patient 2 is compound heterozygote for mutations c.301A>G (p.M101V) and c.313G>A (p.R105Q).
Data indicate that PDH (show PDP Antibodies) deficiency in our patient involves a post-translational modification in which EGFR (show EGFR Antibodies)-PTK-mediated tyrosine phosphorylation of the E1beta protein leads to enhanced ubiquitination followed by proteasome-mediated degradation.
clinical findings are similar to those of PDHA1 (show PDHA1 Antibodies) deficiency, except that ataxia (show USP14 Antibodies) was more frequent in PDHA1 (show PDHA1 Antibodies) cases and consanguinity was found only in PDHB families.
Species specificity in the interaction between hE1beta and hE2 (show SPAG11B Antibodies) in pyruvate dehydrogenase (show PDP Antibodies) complex.
Data indicate the pyruvate dehydrogenase (show PDP Antibodies)-E1 beta core promoter to be located 490bp upstream from the transcription initiation site (+1).
Polymorphisms in promoter regions of PDHB, SORBS1 (show SORBS1 Antibodies), and EDG1 (show S1PR1 Antibodies) genes showing marbling-associated expression changes.
PHD3 (show EGLN3 Antibodies) depletion did not affect the expression of the PDH (show PDP Antibodies)-E1alpha, E1beta, and E2 subunits, or the phosphorylation status of E1alpha, but destabilized the PDH (show PDP Antibodies) complex (PDC (show PDC Antibodies)), resulting in less functional PDC (show PDC Antibodies).
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and carbon dioxide, and provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle. The PDH complex is composed of multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). The E1 enzyme is a heterotetramer of two alpha and two beta subunits. This gene encodes the E1 beta subunit. Mutations in this gene are associated with pyruvate dehydrogenase E1-beta deficiency. Alternatively spliced transcript variants have been found for this gene.
, pyruvate dehydrogenase E1beta subunit
, pyruvate dehydrogenase E1 component subunit beta, mitochondrial
, pyruvate dehydrogenase, E1 beta polypeptide