The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes - Wikidata - awgldk - TriplyDB

The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes

The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes

http://www.wikidata.org/entity/Q24555057

about

Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex activity Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex Molecular structure of a 9-MDa icosahedral pyruvate dehydrogenase subcomplex containing the E2 and E3 enzymes using cryoelectron microscopy Targeting Cancer Metabolism - Revisiting the Warburg Effects Parts plus pipes: synthetic biology approaches to metabolic engineering Chemistry and biochemistry of 13C hyperpolarized magnetic resonance using dynamic nuclear polarization Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains.The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism 3D electron microscopy reveals the variable deposition and protein dynamics of the peripheral pyruvate dehydrogenase component about the core.Cryo-electron Microscopy Analysis of Structurally Heterogeneous Macromolecular Complexes Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components Quantitative proteomics: the copy number of pyruvate dehydrogenase is more than 10(2)-fold lower than that of complex III in human mitochondria Qualitative and Quantitative Protein Complex Prediction Through Proteome-Wide Simulations Reciprocal regulation of protein synthesis and carbon metabolism for thylakoid membrane biogenesis Biochemistry and evolution of anaerobic energy metabolism in eukaryotes Tropical infectious diseases: metabolic maps and functions of the Plasmodium falciparum apicoplast Does mtDNA nucleoid organization impact aging?Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex: a multifunctional catalytic machine Mechanisms underlying regulation of the expression and activities of the mammalian pyruvate dehydrogenase kinases.Phase 1 trial of dichloroacetate (DCA) in adults with recurrent malignant brain tumors.Mitochondrial Dihydrolipoamide Dehydrogenase is Upregulated in Response to Intermittent Hypoxic Preconditioning.A metabolic signature for long life in the Caenorhabditis elegans Mit mutants.Nicotine Dehydrogenase Complexed with 6-Hydroxypseudooxynicotine Oxidase Involved in the Hybrid Nicotine-Degrading Pathway in Agrobacterium tumefaciens S33 Computational Study on New Natural Compound Inhibitors of Pyruvate Dehydrogenase Kinases.Flexible, symmetry-directed approach to assembling protein cages.Monitoring phosphorylation of the pyruvate dehydrogenase complex.A zebrafish model for pyruvate dehydrogenase deficiency: rescue of neurological dysfunction and embryonic lethality using a ketogenic diet.Kinetic flux profiling elucidates two independent acetyl-CoA biosynthetic pathways in Plasmodium falciparum.Exploring conformational modes of macromolecular assemblies by multiparticle cryo-EM.Comparative Phosphoproteomic Analysis under High-Nitrogen Fertilizer Reveals Central Phosphoproteins Promoting Wheat Grain Starch and Protein Synthesis.The pyruvate dehydrogenase complex as a therapeutic target for age-related diseases.A new level of architectural complexity in the human pyruvate dehydrogenase complex.Connecting Salt Stress Signalling Pathways with Salinity Induced Changes in Mitochondrial Metabolic Processes in C3 Plants.Substrate channelling as an approach to cascade reactions.Spatial Organization of Metabolic Enzyme Complexes in Cells.Involvement of Candida albicans pyruvate dehydrogenase complex protein X (Pdx1) in filamentation Mitochondrial Dihydrolipoyl Dehydrogenase Activity Shapes Photosynthesis and Photorespiration of Arabidopsis thaliana.Solution structure and characterisation of the human pyruvate dehydrogenase complex core assembly.Extreme anoxia tolerance in crucian carp and goldfish through neofunctionalization of duplicated genes creating a new ethanol-producing pyruvate decarboxylase pathway.

P2860

Q24302051-49485890-843D-4C96-82E3-41046E8B5EFB Q24310540-79E53D0E-C897-49EA-8643-DF638F6A8B41 Q24534337-A7A13AFC-9A40-419C-873E-A24090F48CEA Q24669729-6F25FED0-A134-4BC1-B7A2-5AE693B6C84F Q26738876-80292172-140C-4D0A-ABEC-39AEB9BA4F8A Q27000122-FD753987-5EE5-40FF-B19F-5D79DCCECBE0 Q27023363-CD3D4D71-09E5-4D24-B1E1-3A1BA34331AE Q27303634-D210616D-233A-4F8A-A6A8-06B03A1779E2 Q27643936-E9910FEB-B8D6-4BC6-98AC-388CD2602E85 Q27935277-551B8814-2E36-433F-B07F-50AB7635CD1F Q28077127-5BD11AEF-46CB-4424-9EBD-3FFA2F50EE06 Q28187388-FC1F05B9-D3E0-4AAC-9D14-F29D112B9766 Q28206298-0D85D665-07A8-4DA0-BDC3-D00027095E14 Q28550460-039803D4-20F6-4877-A415-F0D69359D1C1 Q28709005-A0396201-2818-48A0-BB0E-1FE9EB0E6B48 Q28728648-80DF3E7A-7D15-4505-8728-435A99003DB5 Q30080014-E355C31D-DF33-4305-8E58-790752D60574 Q33889067-B66D1118-84FF-425F-9F5A-185C222DF7D3 Q34206769-B9994AE9-6CBC-4704-8800-474C45764CD0 Q34572847-762FD3AC-ACC6-42C2-BAE7-2B48213460B1 Q35684292-B5569003-896A-4FBF-8780-36EB01C0A312 Q35739510-D48BA95D-FB00-44F1-9DD9-F3477B36784C Q36553737-31B05041-D3DD-46C2-8E52-1BCA5412E071 Q36667305-D31AE8E1-0209-46E7-B504-1FB608809212 Q36743618-C3B2D99C-E105-46D9-BEF3-9E2BC3D29515 Q37161506-1087D248-04C7-440C-93A9-0F5F7529BDD3 Q37269832-CA930522-320A-43EC-874A-1C56258E3324 Q37358186-DD475ACF-995D-4D2F-892C-5929F71DBB78 Q37404986-8D9E5934-D872-4417-9A74-51BEFD571863 Q37600488-5A842BAF-9A30-498B-86CA-0B745B0AE716 Q37611791-2E6D84C2-ADA9-4576-9068-BE0BA3708444 Q37982890-40C47872-E9D1-42FD-AB80-4F277785510F Q38274657-D666FB62-D185-4E65-B6B5-CD7F4C7C7307 Q38652166-4D8F729E-71CC-4FC6-9F50-C981A76B91CF Q38784351-AEE1CA4C-AA11-4747-A4C9-77CE2AA020B6 Q39350533-356BD51E-14B9-428D-94AF-5AE6A9643B66 Q39694921-FFD52443-2E24-48BD-A165-50CD85BBA40B Q40791504-C958A142-C4CE-4C3B-AD2C-05DCA6F9F521 Q40884689-AEEA3DC7-4D6C-48AD-BC2B-3C9861E99457 Q41367711-F94B68E5-4386-4AC7-9A8A-1B0E6D59D0F3

P2860

The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes

http://www.wikidata.org/entity/Q24555057

description

2001 nî lūn-bûn

@nan

2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի դեկտեմբերին 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

The remarkable structural and ...... ruvate dehydrogenase complexes

@ast

The remarkable structural and ...... ruvate dehydrogenase complexes

@en

The remarkable structural and ...... ruvate dehydrogenase complexes

@nl

type

label

The remarkable structural and ...... ruvate dehydrogenase complexes

@ast

The remarkable structural and ...... ruvate dehydrogenase complexes

@en

The remarkable structural and ...... ruvate dehydrogenase complexes

@nl

prefLabel

The remarkable structural and ...... ruvate dehydrogenase complexes

@ast

The remarkable structural and ...... ruvate dehydrogenase complexes

@en

The remarkable structural and ...... ruvate dehydrogenase complexes

@nl

P1433

Q24555057-0A8BE32B-D2C3-4296-8712-55DD612B65B7

P1476

Q24555057-5A3A0CD1-F403-45C4-88B5-9DB408A51B73

P2093

Q24555057-2D11D157-B876-4B91-99A0-327FCE1C43E5

Q24555057-369C726A-30CD-48E8-8ED3-FAB28761E60C

Q24555057-C36BD4DA-3893-47AE-BF5D-BAF067CFCAFB

Q24555057-D19EED34-897B-46D7-942B-37A5C38C82E9

Q24555057-D8A086CB-7DD4-43C3-864C-063FBE60088A

P2860

Q24555057-0EF1C52C-4779-4573-8A00-DA6994079668

Q24555057-0FD61CC1-C776-4E9E-8414-C110A68EEE5A

Q24555057-12882CE1-BFF1-4F42-A7B1-FC800C7AF212

Q24555057-1C92A18D-FCB7-4E95-82BF-2069E0FDA414

Q24555057-2C656507-9A66-40FD-AFC2-159C4C8CF45B

Q24555057-42B9653B-B1F5-4978-83FA-62E46FA5B546

Q24555057-59AB398F-5F7D-4CC9-A60D-D23B59711D3C

Q24555057-5E39091D-F942-46EE-B5FF-9CF302B8BFE1

Q24555057-5F18CDE9-5918-4B7F-AC6A-C82437744850

Q24555057-823C382F-B548-4D6B-AB73-E0AA8871E32C

P304

Q24555057-7836BB3D-3AB8-4982-BF9D-503D532EC961

P31

Q24555057-26F51609-152E-4C07-B5D7-72359239E444

P3181

Q24555057-E6F64303-D5A9-4A2A-8739-AFB42E9F126E

P356

Q24555057-5BB34639-E60A-458F-8785-78B26B6C8C9D

P407

Q24555057-19F8DBEA-086D-42BB-B357-C9B42D2F9BD4

P433

Q24555057-D298A119-19B6-4623-9DB5-39A7AA51B080

P478

Q24555057-599C3185-9721-42BC-A4C1-7E1ACD99A01B

P577

Q24555057-163F2006-9A95-4CA3-85A0-6412F308D0C7

P5875

Q24555057-936B7EAF-6267-4B5E-9CCD-BCDF54B39F84

P698

Q24555057-BAFB6F78-B35E-4E3A-BBBD-F85F3C3CFE6C

P932

Q24555057-223CA629-D027-4BD0-ACF4-4AE5A08137D7

P3181

P356

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

The remarkable structural and ...... ruvate dehydrogenase complexes

@en

P2093

C M O'Connor

http://www.w3.org/2001/XMLSchema#string

D B McCarthy

http://www.w3.org/2001/XMLSchema#string

J K Stoops

http://www.w3.org/2001/XMLSchema#string

L J Reed

http://www.w3.org/2001/XMLSchema#string

Z H Zhou

http://www.w3.org/2001/XMLSchema#string

P2860

Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes

Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes

Three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex

Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex

Expression, purification, and characterization of the dihydrolipoamide dehydrogenase-binding protein of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae.

On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex

Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex.

Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions

Structure-function relationships in dihydrolipoamide acyltransferases

Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex

P304

14802-7

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2967434

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.011597698

http://www.w3.org/2001/XMLSchema#string

P407

P433

26

http://www.w3.org/2001/XMLSchema#string

P478

98

http://www.w3.org/2001/XMLSchema#string

P577

2001-12-18T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

235613533

http://www.w3.org/2001/XMLSchema#string

P698

11752427

http://www.w3.org/2001/XMLSchema#string

P932

64939

http://www.w3.org/2001/XMLSchema#string