about
Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthaseStructural studies on the synchronization of catalytic centers in glutamate synthaseThe active conformation of glutamate synthase and its binding to ferredoxinThe subnanometer resolution structure of the glutamate synthase 1.2-MDa hexamer by cryoelectron microscopy and its oligomerization behavior in solution: functional implicationsPlasmodium falciparum ferredoxin-NADP+ reductase His286 plays a dual role in NADP(H) binding and catalysisCrystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2Active site plasticity in D-amino acid oxidase: a crystallographic analysisPurification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase.Structure-function studies of glutamate synthases: a class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation.Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate.Structure--function studies on the iron-sulfur flavoenzyme glutamate synthase: an unexpectedly complex self-regulated enzyme.Structure-function studies on the complex iron-sulfur flavoprotein glutamate synthase: the key enzyme of ammonia assimilation.Genomic and functional analyses unveil the response to hyphal wall stress in Candida albicans cells lacking β(1,3)-glucan remodeling.Energy matters: mitochondrial proteomics for biomedicine.MICAL, the flavoenzyme participating in cytoskeleton dynamicsStructure-function studies of MICAL, the unusual multidomain flavoenzyme involved in actin cytoskeleton dynamics.Cold Denaturation of the HIV-1 Protease Monomer.Synthesis and biological evaluation of new amino acids structurally related to the antitumor agent acivicin.Glutamate synthase: a complex iron-sulphur flavoprotein.Molecular dynamics simulation of the interaction between the complex iron-sulfur flavoprotein glutamate synthase and its substrates.The complex folding behavior of HIV-1-protease monomer revealed by optical-tweezer single-molecule experiments and molecular dynamics simulations.Influence of divalent cations on the catalytic properties and secondary structure of unadenylylated glutamine synthetase from Azospirillum brasilense.Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit.First-principles molecular dynamics investigation of the D-amino acid oxidative half-reaction catalyzed by the flavoenzyme D-amino acid oxidase.Quaternary structure of Azospirillum brasilense NADPH-dependent glutamate synthase in solution as revealed by synchrotron radiation x-ray scattering.Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution.L-lactate dehydrogenation in flavocytochrome b2: a first principles molecular dynamics study.The unexpected structural role of glutamate synthase [4Fe-4S](+1,+2) clusters as demonstrated by site-directed mutagenesis of conserved C residues at the N-terminus of the enzyme beta subunit.Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process.Key Role of the Adenylate Moiety and Integrity of the Adenylate-Binding Site for the NAD(+)/H Binding to Mitochondrial Apoptosis-Inducing Factor.Human histone demethylase LSD1 reads the histone code.A single tyrosine hydroxyl group almost entirely controls the NADPH specificity of Plasmodium falciparum ferredoxin-NADP+ reductase.Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains.Phenylglyoxal modification of arginines in mammalian D-amino-acid oxidase.Kinetic isotope effects on the oxidation of reduced nicotinamide adenine dinucleotide phosphate by the flavoprotein methylenetetrahydrofolate reductase.Activation and coupling of the glutaminase and synthase reaction of glutamate synthase is mediated by E1013 of the ferredoxin-dependent enzyme, belonging to loop 4 of the synthase domain.Structural studies on the subunits of glutamate synthase from Azospirillum brasilense.Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism.
P50
Q24328953-9D281C6B-8DBF-4BE0-A71F-6E343FC44D18Q27629777-2BF72D0E-2AF2-433A-A2D3-D07D46C5E771Q27638882-E1601134-310D-444F-BEB8-3C3AE7D1C1D7Q27641457-44AEC616-3A38-463D-9150-65203DFD03DEQ27649544-01E08793-C110-4485-81BC-B40E3A0046AFQ27657358-E06449E9-F731-48C4-932C-EDCB33692E86Q27733284-74FB6023-91FC-487E-B2EC-3E0EF4CF16F6Q27737574-429A1ACD-D545-4925-8322-B640E8620839Q28591706-A008D46C-BFE5-4960-9D0C-62F5C1D57B69Q33944923-70CDEF2B-8FDF-4A30-8708-5ED97719E6A2Q34011186-77D14DCE-BD3B-4018-82AB-26A2FC02423FQ35723640-04C70038-EC48-4EB2-B1C1-23D4CA650ADAQ35974356-27E82B32-EC22-4E52-8139-62B9420ECF62Q36249624-60F6AF35-B99D-4D3D-B371-44FF0E16248FQ37089979-CCB331E2-6B24-4503-A541-340C09A87C50Q37829412-D42686D7-2CDE-423E-857E-51CCE7EA375FQ38093723-93DDD8C1-B9A0-4D3E-B7D6-B6B662DCE992Q39365508-37BD90FF-9BA0-4620-AAB5-40484944076FQ40346779-C979ECA8-A361-46CC-B5CF-BD246BBC81FEQ40633907-C9496EBE-087A-4DE7-A6A2-0F7A1757F77BQ41011339-10F9FC2A-A729-4F86-B960-F699DD77B3F6Q41858613-69E1B213-149E-4484-B828-19E099916A2FQ42192385-9B0819A3-FFA5-4D44-888A-D22F3ECD319AQ43614162-7AA52D3E-33EF-4B50-9528-9240391E2088Q44031425-A4A9B8CF-B90D-40FB-9786-0ADE7E41B29AQ44228053-A0DB7827-5A85-4FD3-8F02-8F9C00E5579DQ44460169-FFD6409D-C2E3-478B-8560-DBD81CFD8D24Q44606813-21506C4D-4341-4A7E-8BB1-6768050D9FE4Q46060439-980EEF57-5CD0-4531-917C-983C5F9A9C6CQ46409844-E3676FA7-181C-42FE-BFD6-283119FFA2D4Q46422899-6E5BC26A-CE6C-42C3-9E5F-1AA177D45DB1Q46448803-0F38A4D7-424B-4BDA-96AF-FF271161F811Q46751765-2D5BA881-0ABF-45DD-B47D-A8164500EC16Q47877009-638A36B7-7C31-4664-A175-0196F306A4D1Q50335798-144AF979-B023-4025-BE8F-848BAF3DD11CQ52590213-6659AEFC-12F9-4317-B2E6-1FE5823C645AQ52686661-D29EDE73-DCA9-49DC-8C18-5B01FC15857FQ54444809-D5FDF2BF-2A37-47CD-81F9-044F7B9875C5Q54711166-5A46B687-A70D-41C6-8E71-88FEC2B189CBQ54962323-9897A82A-01F8-4F83-923E-87AE06182C2C
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Maria Antonietta Vanoni
@ast
Maria Antonietta Vanoni
@en
Maria Antonietta Vanoni
@es
Maria Antonietta Vanoni
@nl
Maria Antonietta Vanoni
@sl
type
label
Maria Antonietta Vanoni
@ast
Maria Antonietta Vanoni
@en
Maria Antonietta Vanoni
@es
Maria Antonietta Vanoni
@nl
Maria Antonietta Vanoni
@sl
prefLabel
Maria Antonietta Vanoni
@ast
Maria Antonietta Vanoni
@en
Maria Antonietta Vanoni
@es
Maria Antonietta Vanoni
@nl
Maria Antonietta Vanoni
@sl
P106
P1153
35568743400
P21
P2798
P31
P496
0000-0001-7213-732X