Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
about
Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenaseCrystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complexPyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activityStructural 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 radicicolCloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenaseNovel therapeutic targets of tumor metabolismThe pyruvate dehydrogenase complex of Saccharomyces cerevisiae is regulated by phosphorylation.YIL042c and YOR090c encode the kinase and phosphatase of the Saccharomyces cerevisiae pyruvate dehydrogenase complex.Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferaseRecent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKsThe 2-oxo acid dehydrogenase complexes: recent advancesInactivation of pyruvate dehydrogenase kinase 2 by mitochondrial reactive oxygen speciesMutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulationPDH activation during in vitro muscle contractions in PDH kinase 2 knockout mice: effect of PDH kinase 1 compensationThe phosphorylation of subunits of complex I from bovine heart mitochondria.Identification and analysis of the genes coding for the putative pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii.Regulation of pyruvate metabolism and human diseaseProbing the mechanism of inactivation of human pyruvate dehydrogenase by phosphorylation of three sites.Three genes for enzymes of the pyruvate dehydrogenase complex map to human chromosomes 3, 7, and X.Structural 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.Chronic inhibition of pyruvate dehydrogenase in heart triggers an adaptive metabolic response.A comprehensive proteomic approach to identifying capacitation related proteins in boar spermatozoa.Genome-Wide Profiling of TRACK Kidneys Shows Similarity to the Human ccRCC Transcriptome.Molecular cloning of cDNAs for alpha and beta subunits of human pyruvate dehydrogenase.Role of mitochondrial Ca2+ in the regulation of cellular energeticsDrug Signature-based Finding of Additional Clinical Use of LC28-0126 for Neutrophilic Bronchial Asthma.Phosphoprotein network analysis of white adipose tissues unveils deregulated pathways in response to high-fat diet.Monitoring phosphorylation of the pyruvate dehydrogenase complex.Quantitative mitochondrial phosphoproteomics using iTRAQ on an LTQ-Orbitrap with high energy collision dissociation.Essential regulation of cell bioenergetics in Trypanosoma brucei by the mitochondrial calcium uniporter.The 2-oxoacid dehydrogenase complexes in mitochondria can produce superoxide/hydrogen peroxide at much higher rates than complex IRegulation of muscle pyruvate dehydrogenase complex in insulin resistance: effects of exercise and dichloroacetateQuantitative cardiac phosphoproteomics profiling during ischemia-reperfusion in an immature swine model.High-dose vitamin B1 reduces proliferation in cancer cell lines analogous to dichloroacetate.Integrative proteomics and biochemical analyses define Ptc6p as the Saccharomyces cerevisiae pyruvate dehydrogenase phosphatase.Biochemical and molecular genetic aspects of pyruvate dehydrogenase complex from Saccharomyces cerevisiae.Regulation of the pyruvate dehydrogenase complexes in plants.
P2860
Q24291531-839E8FE3-85A1-434A-821B-DA4F84CD667AQ24301004-97D4F367-1A84-4581-8413-2546084569D0Q24317423-6B06FE83-F846-407C-8206-7DC2DCC0A0E6Q24329273-DF3EB81E-4EB3-46EA-A03D-F7A72090A883Q24336339-D86D97BA-5B81-49F5-90C2-D4ECB4430A1DQ24336876-12266B86-ED5C-469F-8DD9-4FC1A71BAC1FQ24657108-29AEA794-49D2-41CC-A1D1-34F08791D33FQ27005930-F82E2CFE-1B31-4CBA-BFE1-65880507F04AQ27932009-62A94C69-A858-4F90-886F-2433E7510C59Q27932952-765D0D90-0F95-4EA7-8B41-02E944B07C8BQ28180567-E6F113E7-EF04-488E-8DE5-D945C0E783FBQ28188766-33F56260-B00E-4060-A6A7-4A8DC4DA7534Q28268939-B05229C9-B720-403F-B13D-8E486DBB8CEBQ28273438-1CC2B393-79E6-4632-A0F1-BA8F050E9151Q28303294-CB109866-9BE5-4A5D-9D12-E5E971AA8231Q28307470-BABDD740-53F5-4E6A-94D3-79CBD77E92E6Q33200678-E5488494-255A-4318-8204-4539C4B69EEEQ33278375-10F0DFC2-DB13-4732-A48E-5C4DE8626C48Q33764544-96A3366C-65FE-47C6-9CD8-51516A467C13Q33926252-8140014B-5FF2-49AE-9978-8AA1B9C8E275Q34018938-B3E542DF-ABD7-4F7A-9BE3-393A2B550566Q34548748-FF06E279-4180-4C0D-8163-F055E0E8BAD5Q34572847-FFA922D9-5CB7-4499-BD62-C48D3CDE1D4DQ34719537-CE715334-BC00-427B-ABD4-49EB97D9AE68Q34871037-78993C88-B529-477E-A94C-EB605B4460E8Q35567752-7CFF8E08-D0CC-49D3-891C-C856B9521A37Q35765512-B9206E2F-B682-45AC-AEEF-4B8ABA01057FQ35903712-0C4A75A6-808A-41C6-AC76-EC9E8CBC2A82Q36340148-1DBA45CC-1348-4D80-9D54-549E82338BC6Q36903098-EB5DF5D8-5374-4CB6-B972-F891CF46379DQ37269832-EC65EC39-4773-457E-B699-B74D72D1AD6EQ37400627-DA360788-41B1-478B-8670-6E98F1EC46CEQ37404480-0BC22852-2ED8-4E31-BD09-BE2F4C73089BQ37653268-4B410322-79F8-4BF3-89AA-D6BCF53F4D0BQ38160493-CD2540FC-1510-4EB6-ACFC-4CB4BF5EB023Q38377369-63435F67-842E-43EC-9F44-C90A570BC73FQ38420969-61A913E2-F1E7-4CA1-B61F-6E8FB476E6D9Q38766497-3F7A077C-1BF0-41EA-A365-726FB9F54F27Q38781240-74EA2EBA-157C-44E1-944D-377F79B8FDC6Q38781243-A0A98891-F342-455F-A262-E4D720845205
P2860
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
description
1978 nî lūn-bûn
@nan
1978 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1978 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1978年の論文
@ja
1978年論文
@yue
1978年論文
@zh-hant
1978年論文
@zh-hk
1978年論文
@zh-mo
1978年論文
@zh-tw
1978年论文
@wuu
name
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@ast
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@en
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@nl
type
label
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@ast
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@en
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@nl
prefLabel
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@ast
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@en
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@nl
P2093
P356
P1433
P1476
Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart.
@en
P2093
Hutcheson ET
P304
P356
10.1021/BI00605A017
P407
P577
1978-06-01T00:00:00Z