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journal-article
Elsevier BV
Structure (78)
References
55
Referenced
152
10.1016/B978-0-12-152827-0.50011-6
/ Curr. Topics Cell Regul. / Regulation of mammalian pyruvate and branched-chain α-keto acid dehydrogenase complexes by phosphorylation–dephosphorylation by Reed (1985)10.1021/ar50074a002
/ Acc. Chem. Res. / Multienzyme complexes by Reed (1974)10.1021/bi00099a001
/ Biochemistry / Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes by Perham (1991)10.1126/science.1549782
/ Science / Atomic structure of the cubic core of the pyruvate dehydrogenase multi-enzyme complex by Mattevi (1992)10.1073/pnas.96.4.1240
/ Proc. Natl Acad. Sci. USA / Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes by Izard (1999){'key': '10.1016/S0969-2126(00)00105-2_BIB6', 'series-title': 'The Metabolic and Molecular Basis of Inherited Disease 7th edition', 'first-page': '1239', 'article-title': 'Disorders of branched-chain amino and α-ketoacid metabolism', 'author': 'Chuang', 'year': '1995'}
/ The Metabolic and Molecular Basis of Inherited Disease 7th edition / Disorders of branched-chain amino and α-ketoacid metabolism by Chuang (1995){'key': '10.1016/S0969-2126(00)00105-2_BIB7', 'series-title': 'Alpha-Keto Acid Dehydrogenase Complexes', 'first-page': '101', 'article-title': 'Structure, function and assembly of mammalian branched-chain α-ketoacid dehydrogenase complex', 'author': 'Wynn', 'year': '1996'}
/ Alpha-Keto Acid Dehydrogenase Complexes / Structure, function and assembly of mammalian branched-chain α-ketoacid dehydrogenase complex by Wynn (1996)10.1016/0003-9861(90)90645-F
/ Arch. Biochem. Biophys. / Purification and partial characterization of branched-chain α-ketoacid dehydrogenase kinase from rat liver and rat heart by Shimomura (1990){'key': '10.1016/S0969-2126(00)00105-2_BIB9', 'first-page': '109', 'article-title': 'Purification and properties of branched-chain α-keto acid dehydrogenase kinase from bovine kidney', 'volume': '2', 'author': 'Lee', 'year': '1991', 'journal-title': 'Biofactors'}
/ Biofactors / Purification and properties of branched-chain α-keto acid dehydrogenase kinase from bovine kidney by Lee (1991)10.1073/pnas.81.14.4335
/ Proc. Natl Acad. Sci. USA / Purification and properties of branched-chain α-ketoacid dehydrogenase phosphatase from bovine kidney by Damuni (1984)10.1016/S0021-9258(18)42286-7
/ J. Biol. Chem. / Chaperonins GroEL and GroES promote assembly of heterotetramers (α2β2) of mammalian mitochondrial branched-chain α-keto acid decarboxylase in E. coli by Wynn (1992)10.1074/jbc.274.15.10395
/ J. Biol. Chem. / GroEL/GroES-dependent reconsititution of α2β2, tetramers of human mitochondrial branched chain α-ketoacid decarboxylase — obligatory interaction of the chaperonins with an alpha beta dimeric intermediate by Chuang (1999)10.1016/0006-3002(60)90448-0
/ Biochim. Biophys. Acta / Metabolism of the white blood cells in maple-syrup-urine disease by Dancis (1960)10.1542/peds.14.5.462
/ Pediatrics / A new syndrome by Menkes (1954)10.1203/00006450-197801000-00018
/ Pediatr. Res. / A defect in branched-chain amino acid metabolism in a patient with congenital lactic acidosis due to dihydrolipoyl dehydrogenase deficiency by Taylor (1978)10.1038/11563
/ Nat. Struct. Biol. / Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes by Ævarsson (1999)10.1006/jmbi.1994.1299
/ J. Mol. Biol. / Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution by Nikkola (1994)10.1016/S0021-9258(20)80532-8
/ J. Biol. Chem. / Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids by Sundstrom (1993){'key': '10.1016/S0969-2126(00)00105-2_BIB19', 'first-page': '139A', 'article-title': 'Maple syrup urine disease in the old order Mennonites', 'volume': '33', 'author': 'Marshall', 'year': '1981', 'journal-title': 'Am. J. Hum. Genet.'}
/ Am. J. Hum. Genet. / Maple syrup urine disease in the old order Mennonites by Marshall (1981)10.1021/bi973047e
/ Biochemistry / The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes by Hasson (1998)10.1016/0969-2126(93)90025-C
/ Structure / A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase by Muller (1993)10.1038/5870
/ Nat. Struct. Biol. / Crystal structures of the key anaerobic enzyme pyruvate: ferredoxin oxidoreductase, free and in complex with pyruvate by Chabrière (1999)10.1126/science.275.5296.67
/ Science / How thiamine diphosphate is activated in enzymes by Kern (1997)10.1016/S0167-4838(98)00067-3
/ Biochim. Biophys. Acta / Sixty years of thiamin diphosphate biochemistry by Schellenberger (1998)10.1016/S0167-4838(98)00082-X
/ Biochim. Biophys. Acta / Crystallography and mutagenesis of transketolase by Schneider (1998)10.1016/S0021-9258(17)32349-9
/ J. Biol. Chem. / Site-directed mutagenesis of phosphorylation sites of the branched chain α-ketoacid dehydrogenase complex by Zhao (1994)10.1074/jbc.270.52.31071
/ J. Biol. Chem. / Roles of amino acid residues surrounding phosphorylation site 1 of branched-chain α-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase by Hawes (1995)10.1016/0003-9861(88)90252-4
/ Arch. Biochem. Biophys. / Monovalent cations and inorganic phosphate alter branched-chain α-ketoacid dehydrogenase-kinase activity and inhibitor sensitivity by Shimomura (1988)10.1016/0014-5793(89)81064-6
/ FEBS Lett. / A common structural motif in thiamine pyrophosphate-binding enzymes by Hawkins (1989)10.1074/jbc.273.21.13110
/ J. Biol. Chem. / Impaired assembly of E1 decarboxylase of the branched chain α-ketoacid dehydrogenase complex in type IA maple syrup urine diesase by Wynn (1998)10.1016/0006-291X(90)90723-Z
/ Biochem. Biophys. Res. Commun. / A T-to-A substitution in the E1α subunit gene of the branched-chain α-ketoacid dehydrogenase complex in two cell lines derived from Mennonite maple syrup urine disease patients by Matsuda (1990)10.1172/JCI115363
/ J. Clin. Invest. / Maple syrup urine disease in Mennonites. Evidence that the Y393N mutations in E1α impedes assembly of the E1 components of branched-chain α-keto acid dehydrogrenase complex by Fisher (1991)10.1016/S0022-3476(98)70523-2
/ J. Pediatr. / Maple syrup urine disease: it has come a long way by Chuang (1998)10.1016/S0021-9258(18)46029-2
/ J. Biol. Chem. / Cloning and expression in Escherichia coli of mature E1β subunit of bovine mitochondrial branced-chain α-ketoacid dehydrogenase complex. Mapping of the E1β-binding region on E2 by Wynn (1992)10.1021/bi961683r
/ Biochemistry / Competitive interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: kinetic analysis using surface plasmon resonance detection by Lessard (1996)10.1016/S0969-2126(96)00032-9
/ Structure / Protein–protein interactions in the pyruvate dehydrogenase multi-enzyme complex by Mande (1996){'key': '10.1016/S0969-2126(00)00105-2_BIB37', 'series-title': 'Flavoenzymes and Flavoproteins', 'first-page': '549', 'article-title': 'The three-dimensional crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution', 'author': 'Mattevi', 'year': '1990'}
/ Flavoenzymes and Flavoproteins / The three-dimensional crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution by Mattevi (1990){'key': '10.1016/S0969-2126(00)00105-2_BIB38', 'series-title': 'Alpha-Keto Acid Dehydrogenase Complexes', 'first-page': '1', 'article-title': 'Interaction of protein domains in the assembly and mechanism of 2-oxo acid dehydrogenase multienzyme complexes', 'author': 'Perham', 'year': '1996'}
/ Alpha-Keto Acid Dehydrogenase Complexes / Interaction of protein domains in the assembly and mechanism of 2-oxo acid dehydrogenase multienzyme complexes by Perham (1996){'key': '10.1016/S0969-2126(00)00105-2_BIB39', 'series-title': 'Electron Microscopy of Proteins. Vol. 2', 'first-page': '1', 'article-title': 'Multienzyme complexes', 'author': 'Oliver', 'year': '1982'}
/ Electron Microscopy of Proteins. Vol. 2 / Multienzyme complexes by Oliver (1982)10.1021/bi00066a007
/ Biochemistry / Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p) by Mattevi (1993)10.1073/pnas.95.2.621
/ Proc. Natl Acad. Sci. / The atomic model of the human protective protein/cathepsin A suggests a structural basis for galactosialidosis by Rudenko (1998){'key': '10.1016/S0969-2126(00)00105-2_BIB42', 'first-page': '429', 'article-title': 'Occurrence of a Tyr393 Asn (Y393N) mutation in the E1a gene of the branched-chain α-ketoacid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population', 'volume': '49', 'author': 'Fisher', 'year': '1991', 'journal-title': 'Am. J. Hum. Genet.'}
/ Am. J. Hum. Genet. / Occurrence of a Tyr393 Asn (Y393N) mutation in the E1a gene of the branched-chain α-ketoacid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population by Fisher (1991)10.1016/S0076-6879(88)66020-4
/ Methods Enzymol. / Enzyme assays with mutant cell lines of maple syrup urine disease by Chuang (1988)10.1107/S0108767393007597
/ Acta Crystallogr. A / AMoRe: an automated package for molecular replacement by Navaza (1994)10.1107/S0108767390010224
/ Acta Crystallogr. A / Improved methods for binding protein models in electron density maps and the location of errors in these models by Jones (1991)10.1107/S0108767390002355
/ Acta Crystallogr. A / Slow-cooling protocols for crystallographic refinement by simulated annealing by Brünger (1990)10.1107/S0907444998003254
/ Acta Crystallogr. D / Crystallography and NMR system: a new software suite for macromolecular structure determination by Brünger (1998)10.1107/S0021889891004399
/ J. Appl. Crystallogr. / MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures by Kraulis (1991)10.1107/S0907444994006396
/ Acta Crystallogr. D / Raster3D version 2.0. A program for photorealistic molecular graphics by Merritt (1994)10.1093/protein/8.2.127
/ Protein Eng. / LIGPLOT: a program to generate schematic diagrams of protein–ligand interactions by Wallace (1995)10.1002/prot.340110407
/ Proteins Struct. Funct. Gen. / Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons by Nicholls (1991)10.1016/0925-4439(93)90123-I
/ Biochim. Biophys. Acta. / Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1α and E1β subunits of the branched-chain α-keto-acid dehydrogenase multienzyme complex by Nobukuni (1993)10.1172/JCI117804
/ J. Clin. Invest. / Molecular and biochemical basis of intermediate maple syrup urine disease: occurrence of homozygous G245R and F364C mutations at the E1α locus of Hispanic-Mexican patients by Chuang (1995)10.1016/S0925-4439(97)00046-X
/ Biochim. Biophys. Acta. / Two new mutations in the human E1b subunit of branched chain α-ketoacid dehydrogenase associated with maple syrup urine disease by McConnell (1997){'key': '10.1016/S0969-2126(00)00105-2_BIB55', 'first-page': '297', 'article-title': 'Molecular basis of maple syrup urine disease: novel mutations at the E1α locus that impairs E1 (α2β2) assembly or decrease steady-state E1α mRNA levels of branched-chain α-keto acid dehydrogenase complex', 'volume': '55', 'author': 'Chuang', 'year': '1994', 'journal-title': 'Am. J. Hum. Genet.'}
/ Am. J. Hum. Genet. / Molecular basis of maple syrup urine disease: novel mutations at the E1α locus that impairs E1 (α2β2) assembly or decrease steady-state E1α mRNA levels of branched-chain α-keto acid dehydrogenase complex by Chuang (1994)
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 9:54 a.m.) |
Deposited | 2 years, 4 months ago (April 8, 2023, 6:48 p.m.) |
Indexed | 30 minutes ago (Aug. 29, 2025, 9:27 p.m.) |
Issued | 25 years, 5 months ago (March 1, 2000) |
Published | 25 years, 5 months ago (March 1, 2000) |
Published Print | 25 years, 5 months ago (March 1, 2000) |
@article{_varsson_2000, title={Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease}, volume={8}, ISSN={0969-2126}, url={http://dx.doi.org/10.1016/s0969-2126(00)00105-2}, DOI={10.1016/s0969-2126(00)00105-2}, number={3}, journal={Structure}, publisher={Elsevier BV}, author={Ævarsson, Arnthor and Chuang, Jacinta L and Max Wynn, R and Turley, Stewart and Chuang, David T and Hol, Wim GJ}, year={2000}, month=mar, pages={277–291} }