AAAAAA

   
Results: 1-25 | 26-42
Results: 1-25/42
COPPER AMINE OXIDASE FROM HANSENULA-POLYMORPHA - THE CRYSTAL-STRUCTURE DETERMINED AT 2.4-ANGSTROM RESOLUTION REVEALS THE ACTIVE CONFORMATION
Authors: LI RB KLINMAN JP MATHEWS FS
Citation: Rb. Li et al., COPPER AMINE OXIDASE FROM HANSENULA-POLYMORPHA - THE CRYSTAL-STRUCTURE DETERMINED AT 2.4-ANGSTROM RESOLUTION REVEALS THE ACTIVE CONFORMATION, Structure, 6(3), 1998, pp. 293-307
CRYSTALLOGRAPHIC STUDY OF AZURIN FROM PSEUDOMONAS-PUTIDA
Authors: CHEN ZW BARBER MJ MCINTIRE WS MATHEWS FS
Citation: Zw. Chen et al., CRYSTALLOGRAPHIC STUDY OF AZURIN FROM PSEUDOMONAS-PUTIDA, Acta crystallographica. Section D, Biological crystallography, 54, 1998, pp. 253-268
REFINED CRYSTAL-STRUCTURE OF METHYLAMINE DEHYDROGENASE FROM PARACOCCUS-DENITRIFICANS AT 1.75 ANGSTROM RESOLUTION
Authors: CHEN LY DOI N DURLEY RCE CHISTOSERDOV AY LIDSTROM ME DAVIDSON VL MATHEWS FS
Citation: Ly. Chen et al., REFINED CRYSTAL-STRUCTURE OF METHYLAMINE DEHYDROGENASE FROM PARACOCCUS-DENITRIFICANS AT 1.75 ANGSTROM RESOLUTION, Journal of Molecular Biology, 276(1), 1998, pp. 131-149
CRYSTALLOGRAPHIC AND SPECTROSCOPIC STUDIES OF NATIVE, AMINOQUINOL, AND MONOVALENT CATION-BOUND FORMS OF METHYLAMINE DEHYDROGENASE FROM METHYLOBACTERIUM-EXTORQUENS AM1
Authors: LABESSE I FERRARI D CHEN ZW ROSSI GL KUUSK V MCINTIRE WS MATHEWS FS
Citation: I. Labesse et al., CRYSTALLOGRAPHIC AND SPECTROSCOPIC STUDIES OF NATIVE, AMINOQUINOL, AND MONOVALENT CATION-BOUND FORMS OF METHYLAMINE DEHYDROGENASE FROM METHYLOBACTERIUM-EXTORQUENS AM1, The Journal of biological chemistry, 273(40), 1998, pp. 25703-25712
HAH1 IS A COPPER-BINDING PROTEIN WITH DISTINCT AMINO-ACID-RESIDUES MEDIATING COPPER HOMEOSTASIS AND ANTIOXIDANT DEFENSE
Authors: HUNG IH CASARENO RLB LABESSE G MATHEWS FS GITLIN JD
Citation: Ih. Hung et al., HAH1 IS A COPPER-BINDING PROTEIN WITH DISTINCT AMINO-ACID-RESIDUES MEDIATING COPPER HOMEOSTASIS AND ANTIOXIDANT DEFENSE, The Journal of biological chemistry, 273(3), 1998, pp. 1749-1754
CRYSTALLOGRAPHIC STUDY OF YEAST COPPER AMINE OXIDASE
Authors: LI RB CHEN LY CAI DY KLINMAN JP MATHEWS FS
Citation: Rb. Li et al., CRYSTALLOGRAPHIC STUDY OF YEAST COPPER AMINE OXIDASE, Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 364-370
SELECTIVE MODIFICATION OF ALKYLAMMONIUM ION SPECIFICITY IN TRIMETHYLAMINE DEHYDROGENASE BY THE RATIONAL ENGINEERING OF CATION-PI BONDING
Authors: BASRAN J MEWIES M MATHEWS FS SCRUTTON NS
Citation: J. Basran et al., SELECTIVE MODIFICATION OF ALKYLAMMONIUM ION SPECIFICITY IN TRIMETHYLAMINE DEHYDROGENASE BY THE RATIONAL ENGINEERING OF CATION-PI BONDING, Biochemistry, 36(8), 1997, pp. 1989-1998
FACTORS WHICH STABILIZE THE METHYLAMINE DEHYDROGENASE-AMICYANIN ELECTRON-TRANSFER PROTEIN COMPLEX REVEALED BY SITE-DIRECTED MUTAGENESIS
Authors: DAVIDSON VL JONES LH GRAICHEN ME MATHEWS FS HOSLER JP
Citation: Vl. Davidson et al., FACTORS WHICH STABILIZE THE METHYLAMINE DEHYDROGENASE-AMICYANIN ELECTRON-TRANSFER PROTEIN COMPLEX REVEALED BY SITE-DIRECTED MUTAGENESIS, Biochemistry, 36(42), 1997, pp. 12733-12738
AN EXPOSED TYROSINE ON THE SURFACE OF TRIMETHYLAMINE DEHYDROGENASE FACILITATES ELECTRON-TRANSFER TO ELECTRON TRANSFERRING FLAVOPROTEIN - KINETICS OF TRANSFER IN WILD-TYPE AND MUTANT COMPLEXES
Authors: WILSON EK HUANG LX SUTCLIFFE MJ MATHEWS FS HILLE R SCRUTTON NS
Citation: Ek. Wilson et al., AN EXPOSED TYROSINE ON THE SURFACE OF TRIMETHYLAMINE DEHYDROGENASE FACILITATES ELECTRON-TRANSFER TO ELECTRON TRANSFERRING FLAVOPROTEIN - KINETICS OF TRANSFER IN WILD-TYPE AND MUTANT COMPLEXES, Biochemistry, 36(1), 1997, pp. 41-48
STRUCTURE OF HUMAN BETA-GLUCURONIDASE REVEALS CANDIDATE LYSOSOMAL TARGETING AND ACTIVE-SITE MOTIFS
Authors: JAIN S DRENDEL WB CHEN ZW MATHEWS FS SLY WS GRUBB JH
Citation: S. Jain et al., STRUCTURE OF HUMAN BETA-GLUCURONIDASE REVEALS CANDIDATE LYSOSOMAL TARGETING AND ACTIVE-SITE MOTIFS, Nature structural biology, 3(4), 1996, pp. 375-381
COVALENT STRUCTURE OF THE FLAVOPROTEIN SUBUNIT OF THE FLAVOCYTOCHROME-C - SULFIDE DEHYDROGENASE FROM THE PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM-VINOSUM
Authors: VANDRIESSCHE G KOH M CHEN ZW MATHEWS FS MEYER TE BARTSCH RG CUSANOVICH MA VANBEEUMEN JJ
Citation: G. Vandriessche et al., COVALENT STRUCTURE OF THE FLAVOPROTEIN SUBUNIT OF THE FLAVOCYTOCHROME-C - SULFIDE DEHYDROGENASE FROM THE PURPLE PHOTOTROPHIC BACTERIUM CHROMATIUM-VINOSUM, Protein science, 5(9), 1996, pp. 1753-1764
X-RAY STRUCTURE OF THE CUPREDOXIN AMICYANIN, FROM PARACOCCUS-DENITRIFICANS, REFINED AT 1.31-ANGSTROM RESOLUTION
Authors: CUNANE LM CHEN ZW DURLEY RCE MATHEWS FS
Citation: Lm. Cunane et al., X-RAY STRUCTURE OF THE CUPREDOXIN AMICYANIN, FROM PARACOCCUS-DENITRIFICANS, REFINED AT 1.31-ANGSTROM RESOLUTION, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 676-686
REFINEMENT AND STRUCTURAL-ANALYSIS OF BOVINE CYTOCHROME B(5) AT 1.5 ANGSTROM RESOLUTION
Authors: DURLEY RCE MATHEWS FS
Citation: Rce. Durley et Fs. Mathews, REFINEMENT AND STRUCTURAL-ANALYSIS OF BOVINE CYTOCHROME B(5) AT 1.5 ANGSTROM RESOLUTION, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 65-76
ELECTRON-TRANSFER IN TRIMETHYLAMINE DEHYDROGENASE - DIRECTED MUTAGENESIS OF A POTENTIAL TUNNELING PATHWAY
Authors: WILSON EK HUANG LX HILLE R MATHEWS FS SCRUTTON NS
Citation: Ek. Wilson et al., ELECTRON-TRANSFER IN TRIMETHYLAMINE DEHYDROGENASE - DIRECTED MUTAGENESIS OF A POTENTIAL TUNNELING PATHWAY, Biochemical Society transactions, 24(3), 1996, pp. 456-456
FLAVINYLATION IN WILD-TYPE TRIMETHYLAMINE DEHYDROGENASE AND DIFFERENTIALLY CHARGED MUTANT ENZYMES - A STUDY OF THE PROTEIN ENVIRONMENT AROUND THE N1 OF THE FLAVIN ISOALLOXAZINE
Authors: MEWIES M PACKMAN LC MATHEWS FS SCRUTTON NS
Citation: M. Mewies et al., FLAVINYLATION IN WILD-TYPE TRIMETHYLAMINE DEHYDROGENASE AND DIFFERENTIALLY CHARGED MUTANT ENZYMES - A STUDY OF THE PROTEIN ENVIRONMENT AROUND THE N1 OF THE FLAVIN ISOALLOXAZINE, Biochemical journal, 317, 1996, pp. 267-272
DETERMINATION OF THE GENE SEQUENCE AND THE 3-DIMENSIONAL STRUCTURE AT2.4-ANGSTROM RESOLUTION OF METHANOL DEHYDROGENASE FROM METHYLOPHILUS W3A1
Authors: XIA ZX DAI WW ZHANG YF WHITE SA BOYD GD MATHEWS FS
Citation: Zx. Xia et al., DETERMINATION OF THE GENE SEQUENCE AND THE 3-DIMENSIONAL STRUCTURE AT2.4-ANGSTROM RESOLUTION OF METHANOL DEHYDROGENASE FROM METHYLOPHILUS W3A1, Journal of Molecular Biology, 259(3), 1996, pp. 480-501
ENZYMATIC AND ELECTRON-TRANSFER ACTIVITIES IN CRYSTALLINE PROTEIN COMPLEXES
Authors: MERLI A BRODERSEN DE MORINI B CHEN ZW DURLEY RCE MATHEWS FS DAVIDSON VL ROSSI GL
Citation: A. Merli et al., ENZYMATIC AND ELECTRON-TRANSFER ACTIVITIES IN CRYSTALLINE PROTEIN COMPLEXES, The Journal of biological chemistry, 271(16), 1996, pp. 9177-9180
ON THE LACK OF COORDINATION BETWEEN PROTEIN-FOLDING AND FLAVIN INSERTION IN ESCHERICHIA-COLI FOR FLAVOCYTOCHROME B-2 MUTANT FORMS Y254L ANDD282N
Authors: GONDRY M LE KHD MANSON FDC CHAPMAN SK MATHEWS FS REID GA LEDERER F
Citation: M. Gondry et al., ON THE LACK OF COORDINATION BETWEEN PROTEIN-FOLDING AND FLAVIN INSERTION IN ESCHERICHIA-COLI FOR FLAVOCYTOCHROME B-2 MUTANT FORMS Y254L ANDD282N, Protein science, 4(5), 1995, pp. 925-935
PROTEIN RECOGNITION OF AMMONIUM CATIONS USING SIDE-CHAIN AROMATICS - A STRUCTURAL VARIATION FOR SECONDARY AMMONIUM LIGANDS
Authors: RAINE ARC YANG CC PACKMAN LC WHITE SA MATHEWS FS SCRUTTON NS
Citation: Arc. Raine et al., PROTEIN RECOGNITION OF AMMONIUM CATIONS USING SIDE-CHAIN AROMATICS - A STRUCTURAL VARIATION FOR SECONDARY AMMONIUM LIGANDS, Protein science, 4(12), 1995, pp. 2625-2628
THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN-I AT 2.2 ANGSTROM RESOLUTION - MOLECULAR-FEATURES OF OXYGEN AVIDITY
Authors: YANG J KLOEK AP GOLDBERG DE MATHEWS FS
Citation: J. Yang et al., THE STRUCTURE OF ASCARIS HEMOGLOBIN DOMAIN-I AT 2.2 ANGSTROM RESOLUTION - MOLECULAR-FEATURES OF OXYGEN AVIDITY, Proceedings of the National Academy of Sciences of the United Statesof America, 92(10), 1995, pp. 4224-4228
REFINED STRUCTURE OF CYTOCHROME B(562) FROM ESCHERICHIA-COLI AT 1.4 ANGSTROM RESOLUTION
Authors: HAMADA K BETHGE PH MATHEWS FS
Citation: K. Hamada et al., REFINED STRUCTURE OF CYTOCHROME B(562) FROM ESCHERICHIA-COLI AT 1.4 ANGSTROM RESOLUTION, Journal of Molecular Biology, 247(5), 1995, pp. 947-962
THE CYTOCHROME SUBUNIT IS NECESSARY FOR COVALENT FAD ATTACHMENT TO THE FLAVOPROTEIN SUBUNIT OF P-CRESOL METHYLHYDROXYLASE
Authors: KIM J FULLER JH KUUSK V CUNANE L CHEN ZW MATHEWS FS MCINTIRE WS
Citation: J. Kim et al., THE CYTOCHROME SUBUNIT IS NECESSARY FOR COVALENT FAD ATTACHMENT TO THE FLAVOPROTEIN SUBUNIT OF P-CRESOL METHYLHYDROXYLASE, The Journal of biological chemistry, 270(52), 1995, pp. 31202-31209
SUBUNIT INTERACTIONS IN ASCARIS HEMOGLOBIN OCTAMER FORMATION
Authors: MINNING DM KLOEK AP YANG J MATHEWS FS GOLDBERG DE
Citation: Dm. Minning et al., SUBUNIT INTERACTIONS IN ASCARIS HEMOGLOBIN OCTAMER FORMATION, The Journal of biological chemistry, 270(38), 1995, pp. 22248-22253
ELECTRON-TUNNELING IN SUBSTRATE-REDUCED TRIMETHYLAMINE DEHYDROGENASE - KINETICS OF ELECTRON-TRANSFER AND ANALYSIS OF THE TUNNELING PATHWAY
Authors: WILSON EK MATHEWS FS PACKMAN LC SCRUTTON NS
Citation: Ek. Wilson et al., ELECTRON-TUNNELING IN SUBSTRATE-REDUCED TRIMETHYLAMINE DEHYDROGENASE - KINETICS OF ELECTRON-TRANSFER AND ANALYSIS OF THE TUNNELING PATHWAY, Biochemistry, 34(8), 1995, pp. 2584-2591
ON THE EVOLUTION OF ALTERNATE CORE PACKING IN EIGHTFOLD BETA ALPHA-BARRELS/
Authors: RAINE ARC SCRUTTON NS MATHEWS FS
Citation: Arc. Raine et al., ON THE EVOLUTION OF ALTERNATE CORE PACKING IN EIGHTFOLD BETA ALPHA-BARRELS/, Protein science, 3(10), 1994, pp. 1889-1892
Risultati: 1-25 | 26-42