Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase
about
Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complexCharacterization of testis-specific isoenzyme of human pyruvate dehydrogenaseStructural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loopsPivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetateDistinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicolMetabolic aspects of low carbohydrate diets and exerciseThe two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanismInhibitor-bound structures of human pyruvate dehydrogenase kinase 4Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases.Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKsAllosteric coupling in pyruvate dehydrogenase kinase 2PDH activation during in vitro muscle contractions in PDH kinase 2 knockout mice: effect of PDH kinase 1 compensationIdentification of rare DNA sequence variants in high-risk autism families and their prevalence in a large case/control populationA new locus for X-linked dominant Charcot-Marie-Tooth disease (CMTX6) is caused by mutations in the pyruvate dehydrogenase kinase isoenzyme 3 (PDK3) gene.PGC-1α and fasting-induced PDH regulation in mouse skeletal muscleThe pyruvate dehydrogenase complexes: structure-based function and regulation.Regulation of pyruvate metabolism and human diseaseMICU1 drives glycolysis and chemoresistance in ovarian cancer.Phenylbutyrate therapy for pyruvate dehydrogenase complex deficiency and lactic acidosis.Characterization of interactions of dihydrolipoamide dehydrogenase with its binding protein in the human pyruvate dehydrogenase complex.Pyruvate dehydrogenase kinase 1 controls mitochondrial metabolism and insulin secretion in INS-1 832/13 clonal beta-cells.Linking vitamin B1 with cancer cell metabolismStructural determinants for cross-talk between pyruvate dehydrogenase kinase 3 and lipoyl domain 2 of the human pyruvate dehydrogenase complex.Mechanisms underlying regulation of the expression and activities of the mammalian pyruvate dehydrogenase kinases.Elucidation of the interaction loci of the human pyruvate dehydrogenase complex E2·E3BP core with pyruvate dehydrogenase kinase 1 and kinase 2 by H/D exchange mass spectrometry and nuclear magnetic resonanceEssential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1.Metabolic programming and PDHK1 control CD4+ T cell subsets and inflammationTumor cell metabolism: an integral view.Differing roles of pyruvate dehydrogenase kinases during mouse oocyte maturation.Differential inhibition of PDKs by phenylbutyrate and enhancement of pyruvate dehydrogenase complex activity by combination with dichloroacetateLack of Skeletal Muscle IL-6 Affects Pyruvate Dehydrogenase Activity at Rest and during Prolonged Exercise.Malate dehydrogenase-2 inhibitor LW6 promotes metabolic adaptations and reduces proliferation and apoptosis in activated human T-cells.Anticancer agents that counteract tumor glycolysis.Pyruvate Dehydrogenase Kinases in the Nervous System: Their Principal Functions in Neuronal-glial Metabolic Interaction and Neuro-metabolic Disorders.Metabolic preconditioning of mammalian cells: mimetic agents for hypoxia lack fidelity in promoting phosphorylation of pyruvate dehydrogenaseMetabolomic profiling of lung and prostate tumor tissues by capillary electrophoresis time-of-flight mass spectrometry.Applying a targeted label-free approach using LC-MS AMT tags to evaluate changes in protein phosphorylation following phosphatase inhibition.The ERK signaling target RNF126 regulates anoikis resistance in cancer cells by changing the mitochondrial metabolic flux.Age-related impairments in skeletal muscle PDH phosphorylation and plasma lactate are indicative of metabolic inflexibility and the effects of exercise training.Hypoxic repression of pyruvate dehydrogenase activity is necessary for metabolic reprogramming and growth of model tumours.
P2860
Q24301004-F0543D0B-DD16-461A-B440-E13B029ED2E0Q24302051-D1A7405B-C6AF-4FA8-8696-7430C1196E76Q24329273-50F028F7-8996-45E3-9DB8-E5CCA43C0998Q24336339-EF0DAB97-8761-4132-847C-880CE47A74CAQ24336876-E677831F-D868-488A-AA83-EE8D84FBD2AFQ24804364-B9763E2D-17CA-47C5-A5BD-E7BB1C3456F1Q27643936-4BF7E4AC-6A29-482B-B4CA-6DF57DC1E5DAQ27673456-10929C48-BFC7-4D7F-9F87-B5C6D5D0DAE0Q27930852-07259172-3ADE-446E-AC10-4796A8917915Q28188766-95477313-AC1B-40B0-82B6-45F84EC3A810Q28287166-85B1F82D-85EA-4F90-A420-A20F64F50F17Q28307470-B5DD0711-698E-4ABC-9929-576552BC5BD6Q28655709-183456AB-C482-4C91-9A5D-B0F2BF6BB5B2Q30537559-6CF9B7B3-66CA-438A-A09C-7F238711566AQ33567491-378A41DF-1D2F-4C21-A529-3C043AADA2F4Q33761130-D45749E1-4187-4935-B124-6BE5BBEA4DB8Q33764544-275BD5BD-376B-4E05-9B1F-C22D3F0FC395Q33815720-58F6E619-4CA6-4789-B2EE-42BF03369DFFQ33918023-22209D73-AE88-4407-B740-789B7D203B8FQ34082484-EF4B11EE-54FD-4AAC-9E66-4778E289CC3EQ34111818-CC1F14A2-1530-4A9F-871D-794182F42744Q34258898-90F37CA6-7B4E-4A6F-A6B9-229B073A9B6BQ34548748-91EA1269-97C7-410F-83AA-890998019E69Q34572847-A7FD04B5-CF07-428A-BF7E-00B4AA3F34F8Q34972253-12BCB875-4010-46A7-92EE-3A3F56E6175DQ35083660-71DE0FF4-9338-4F63-9E11-B0656D7A4913Q35242438-9614D2BD-8E3F-400A-B038-375E7ADB8CB6Q35760954-EA57A29C-2EA7-4AC1-91C5-2BA3B4C87A49Q35878096-512865EE-43FA-4D60-A1A7-67F0833CC630Q36001522-05B54B20-721A-49BB-8356-52F4B62DF923Q36057621-9B621ACB-D5C8-423A-AFF6-E71E9EFC8FFEQ36334286-C521FB0E-2A82-4B82-B812-CF05C07967A9Q36452381-224B4FC8-AA20-4A49-94D6-21200A7E615DQ36460635-31448F97-9E8B-496F-A60F-E8A0C1713FA4Q36511184-18951623-C748-474A-91AC-C0EF67FD9ECBQ36718418-C6010D97-CBB9-45B7-8B94-FB4F125B58F1Q36837717-B6BBEEE8-8690-4A30-9105-47F967DEBF8DQ37125226-B8F0D915-0604-4A49-855E-C9F3E30A495AQ37139419-CE3370D9-4F4B-4E6F-B2E6-4C4DBA75EB0CQ37157453-4E8268D6-1E25-46C7-8BD5-5BE44D225E8A
P2860
Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@ast
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en-gb
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@nl
type
label
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@ast
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en-gb
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@nl
prefLabel
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@ast
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en-gb
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@nl
P2860
P921
P3181
P356
P1476
Site specificity of four pyruv ...... f human pyruvate dehydrogenase
@en
P2093
L G Korotchkina
P2860
P304
P3181
P356
10.1074/JBC.M103069200
P407
P577
2001-10-05T00:00:00Z