Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
about
Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complexAssembly and full functionality of recombinantly expressed dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complexThe remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexesCrystal structures of murine carnitine acetyltransferase in ternary complexes with its substratesCatalytic domain of PDC-E2 contains epitopes recognized by antimitochondrial antibodies in primary biliary cirrhosisPrinciples of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexesEscherichia coli redox mutants as microbial cell factories for the synthesis of reduced biochemicals.Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains.The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivityExpression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferaseStructure of human carnitine acetyltransferase. Molecular basis for fatty acyl transferStructural and mutational studies of anthocyanin malonyltransferases establish the features of BAHD enzyme catalysisDihydroorotase from the Hyperthermophile Aquifiex aeolicus Is Activated by Stoichiometric Association with Aspartate Transcarbamoylase and Forms a One-Pot Reactor for Pyrimidine Biosynthesis † ‡The catalytic core of an archaeal 2-oxoacid dehydrogenase multienzyme complex is a 42-mer protein assemblyInsight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural ApproachesWhy are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complexOn the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complexBiochemical and structural characterization of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparumHow dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complexCrystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivityCrystal structure of vinorine synthase, the first representative of the BAHD superfamily.Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images.Production and characterization of murine models of classic and intermediate maple syrup urine diseaseKinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a precatalytic complex with 2-oxoglutarate.Lipoic acid metabolism in microbial pathogens.Mammalian sprouty proteins assemble into large monodisperse particles having the properties of intracellular nanobatteries.Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex: a multifunctional catalytic machineQuantitative proteomics reveals the temperature-dependent proteins encoded by a series of cluster genes in thermoanaerobacter tengcongensis.A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complexThe dihydrolipoyl acyltransferase (BCE2) subunit of the plant branched-chain alpha-ketoacid dehydrogenase complex forms a 24-mer core with octagonal symmetryEvaluation of a symmetry-based strategy for assembling protein complexes.Modeling mitochondrial function.Characterization of a highly flexible self-assembling protein system designed to form nanocages.Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.Cloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex.Interchain acetyl transfer in the E2 component of bacterial pyruvate dehydrogenase suggests a model with different roles for each chain in a trimer of the homooligomeric component.c-di-AMP modulates Listeria monocytogenes central metabolism to regulate growth, antibiotic resistance and osmoregulation.O-Acetyltransferases for chloramphenicol and other natural products.mgpS, a complex regulatory locus involved in the transcriptional control of the puc and puf operons in Rhodobacter sphaeroides 2.4.1.Sequences and expression of pyruvate dehydrogenase genes from Pseudomonas aeruginosa.
P2860
Q24292283-97F698CD-5967-4D25-B61E-3C48A589CA53Q24322055-C27AF1E0-9287-4EE6-AD3A-E1377D89B5DFQ24555057-90675DDF-E4BD-47A3-9534-1D436F3FD431Q24607519-A129B918-A148-42A8-80AC-A0F06EA28B99Q24642160-3F48B6F5-56F0-4851-9A8F-3E5B9587E27CQ24676255-1856425B-72D0-400F-A3F7-BDE5A740B6A3Q27004040-4D170F06-F141-45E2-A2A7-D466F93F2E2FQ27303634-D7ECDFC4-36E7-47A4-A598-EBB0C579AAA1Q27617940-FC3FB109-421A-42D7-8D5B-14455689BBEDQ27621927-8D50A745-D6FE-49DD-B6FF-5B8BAE127C6AQ27640412-AE5F8AB3-2FCF-48C0-9B16-49F3177B8164Q27644220-4C214CA0-5252-4D66-B069-70465AC6BB34Q27653358-D490FA2F-2AC7-46FD-A634-4D43A2F89B19Q27676346-1ED1C11B-863C-4FA2-91DC-DA7FD5F10F94Q27677341-86219007-487F-4D87-8924-C2F5CB0F4A32Q27694710-6085D413-810B-4FAB-BA25-5B469DBAA6DCQ27935381-23375B93-FD20-48AD-BABE-04E632D56A3FQ27973614-B3FC0C28-2F11-42E2-B52E-897AC15AB8A4Q28279943-922EAD9B-9E52-4470-A903-C97E49D1EF7EQ28513264-F9D3F02F-8E57-48C7-A048-CE2F9BC5B226Q30350026-61B094F1-B43C-4D2B-A549-35D5FB9BBAC2Q31145684-EA4DD775-6AB5-47CC-AA53-0A3382760777Q33238292-16EB491D-6043-4FBB-BED4-7A795FB14E30Q33905272-09602A35-7BF7-4FFD-AB47-F6725004D681Q33909117-7B98658E-9F3B-4590-97E2-DD31208DFAD8Q34000526-AF5532C2-4F5C-48DC-B897-05D030D31EC4Q34206769-F75E53B1-BBA9-4782-91C9-552AC5F38159Q34715701-24B778A2-87E4-46CB-866C-C90A6103CC28Q35222236-44713A86-63EC-4294-A940-6E458CEF106FQ36282139-BA5D3D5D-5063-45A2-B5C8-8838FD64DFF0Q36507250-7B01D9BD-8E30-4264-B0E1-AAE189535921Q36593123-8F5C798F-BC5E-44F9-9CFC-CFCCAD794BC1Q37588970-5B23C67A-64E7-488A-8F89-9A005E82638BQ38146650-757F6D1D-71D0-4063-A998-5A1F46F8F7B7Q38312361-487A8543-A306-45AA-9CDC-E49710AA4CA0Q38326917-B83363AB-31F8-47EB-9B26-56D1D2D7ABBCQ39015536-16E97227-EF23-4313-9FBE-80737E09C934Q39783388-B37B988A-EE54-4DBE-BA1C-1E0D1A31E947Q39839652-56B32AB0-7D73-4B79-8F3F-1B2F2275ACB8Q39845909-C8A158CA-88DE-4AD3-86C6-96655800D80A
P2860
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
description
1992 nî lūn-bûn
@nan
1992 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի մարտին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@ast
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@en
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@nl
type
label
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@ast
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@en
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@nl
prefLabel
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@ast
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@en
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@nl
P2093
P356
P1433
P1476
Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
@en
P2093
A H Westphal
G Obmolova
P304
P356
10.1126/SCIENCE.1549782
P407
P577
1992-03-20T00:00:00Z