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The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding siteThe crystal structure of the sorcin calcium binding domain provides a model of Ca2+-dependent processes in the full-length proteinThe X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocketThe mutations Lys 114 --> Gln and Asp 126 --> Asn disrupt an intersubunit salt bridge and convert Listeria innocua Dps into its natural mutant Listeria monocytogenes Dps. Effects on protein stability at Low pHStructural basis of enzymatic (S)-norcoclaurine biosynthesisThe X-ray structure of the zinc transporter ZnuA from Salmonella enterica discloses a unique triad of zinc-coordinating histidinesA gold-containing drug against parasitic polyamine metabolism: the X-ray structure of trypanothione reductase from Leishmania infantum in complex with auranofin reveals a dual mechanism of enzyme inhibitionThe crystal structure of Giardia duodenalis 14-3-3 in the apo form: when protein post-translational modifications make the differenceKineococcus radiotolerans Dps forms a heteronuclear Mn-Fe ferroxidase center that may explain the Mn-dependent protection against oxidative stressInhibitory Effect of Silver Nanoparticles on Trypanothione Reductase Activity and Leishmania infantum ProliferationInhibition of Leishmania infantum trypanothione reductase by azole-based compounds: a comparative analysis with its physiological substrate by X-ray crystallographyThe Salmonella enterica ZinT structure, zinc affinity and interaction with the high-affinity uptake protein ZnuA provide insight into the management of periplasmic zincThe crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperaturesMolecular Dynamics Simulations and Structural Analysis of Giardia duodenalis 14-3-3 Protein-Protein InteractionsSalmonella enterica serovar Typhimurium growth is inhibited by the concomitant binding of Zn(II) and a pyrrolyl-hydroxamate to ZnuA, the soluble component of the ZnuABC transporterSorcin links calcium signaling to vesicle trafficking, regulates Polo-like kinase 1 and is necessary for mitosisA Practical Approach to Protein Crystallography.Cloning, expression, crystallization and preliminary X-ray data analysis of norcoclaurine synthase from Thalictrum flavum.Trypanothione reductase from Leishmania infantum: cloning, expression, purification, crystallization and preliminary X-ray data analysis.Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli.Structural basis of Sorcin-mediated calcium-dependent signal transductionInhibition of Leishmania infantum trypanothione reductase by diaryl sulfide derivatives.Structural insights into the enzymes of the trypanothione pathway: targets for antileishmaniasis drugs.Sorcin, a calcium binding protein involved in the multidrug resistance mechanisms in cancer cells.A novel antimicrobial approach based on the inhibition of zinc uptake in Salmonella enterica.Polyamine-trypanothione pathway: an update.Structural characterization of Giardia duodenalis thioredoxin reductase (gTrxR) and computational analysis of its interaction with NBDHEX.Glucose transportation in the brain and its impairment in Huntington disease: one more shade of the energetic metabolism failure?Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput dockingBinding of doxorubicin to Sorcin impairs cell death and increases drug resistance in cancer cells.Metal- and metalloid-containing drugs for the treatment of trypanosomatid diseases.Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus.Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus.Metal-based compounds as prospective antileishmanial agents: inhibition of trypanothione reductase by selected gold complexes.Iron incorporation into Escherichia coli Dps gives rise to a ferritin-like microcrystalline core.Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide reductase.Information transfer in the penta-EF-hand protein sorcin does not operate via the canonical structural/functional pairing. A study with site-specific mutants.The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties.Crystalization and preliminary X-ray crystallographic analysis of the laminarinase endo-beta-1,3-glucanase from Pyrococcus furiosus.The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants.
P50
Q27620915-7BE8983D-4076-4BD9-BFC1-036E1AC3F8DFQ27638647-E59934FC-579E-45F7-AE3A-3CFF3C98F2D2Q27638879-56A3D188-816B-4F0D-A95B-2C470BF28D8AQ27643397-D38BF6F8-FA55-41F2-BFCB-5BC3BA2DDCCFQ27652886-1331BC2D-749B-4EA4-AD19-09D970129627Q27667621-790D2EA0-603C-4091-9693-81BEF53AD6D2Q27671675-C6372CE3-2C9C-4A77-9680-F1EE35606B47Q27682395-241EE95B-391B-4EB0-81B2-61DADAF2EFD2Q27683965-F7897B6E-AB82-4CAC-998D-E5CC4B501125Q27684102-4D6D0E2C-70FC-437D-BEFE-F2CB753A7940Q27684748-BAF4579E-3A98-4BC7-895F-AFBA16DAA197Q27687211-23EBF2D2-10DA-4183-96F4-5AEE4A7A1104Q27695650-3463864E-399C-4477-AB04-5AE4A0E52906Q27702592-CFC116CE-B5E6-442A-9D09-C7A83FF9A559Q27703219-AC1200D2-532E-403B-A678-19C66EF53CC4Q28538622-E0659674-6A7C-42F6-BE2A-9689CC50B9F7Q30395755-5578350C-446C-4748-B44A-A9C39BC9F046Q31151629-5930C797-F3D0-44E5-97D2-F2F078725AF2Q33406583-DD5EAA9A-D73C-47A9-B5E1-15AEDA9BFD86Q34128990-61D9B948-D85C-4224-8A47-E3D62581F92FQ35844069-352557B9-C0D7-4C62-9A05-F79107906674Q36252376-74EA71EE-E87E-43A9-B23E-58E1F7681A3CQ38154346-66A259BC-D40A-46EC-954D-4C6B650A2E09Q38246811-59918CDE-04E0-4D44-8C15-FBD6B67D001EQ38668518-46D8479E-BA5E-46D4-BD0B-C22538C6AAB2Q38783627-D88B3C8B-E402-4758-8A0A-E15778553BF0Q38800833-264D7F21-5D5A-447A-885D-FBEB303BCE15Q39233225-E93D245F-A34D-464C-87C7-3CE14DFD4F4CQ40396694-FB9F1A08-4D48-411A-BC70-04B8C5F3E5CCQ41335631-27E84064-0971-4702-A4FA-0B2F3CAEC725Q41996108-CDED4A2F-E4D3-490D-A04B-FB07D62556A5Q43021244-F24872EF-929E-46EF-8CA1-CF771478E176Q43021639-63CC0249-30FA-4C55-9576-35497B541C1DQ43433143-4C38DB22-173C-4A6C-81F8-2112FE2B95F5Q44090729-6175079E-15D8-41BB-BE74-A72589CF5365Q44381482-9E883B83-8C26-45D9-8E5E-5BC9BABEAC94Q44414490-5B68AA26-AAE8-4D04-89FC-7A4EAE9FE730Q45182299-C3688A6F-68E8-494B-91BB-25378C651A96Q45198455-9CAC3C14-5BA3-42B7-83F5-754B181C3608Q46431868-D91C9A9A-474B-44BD-B6A3-D99B50EF6B98
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Andrea Ilari
@ast
Andrea Ilari
@en
Andrea Ilari
@es
Andrea Ilari
@nl
type
label
Andrea Ilari
@ast
Andrea Ilari
@en
Andrea Ilari
@es
Andrea Ilari
@nl
prefLabel
Andrea Ilari
@ast
Andrea Ilari
@en
Andrea Ilari
@es
Andrea Ilari
@nl
P1053
T-5501-2017
P106
P1153
6601938545
P31
P3829
P496
0000-0002-7754-399X