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NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptorNMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain SwappingProbing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probeProbing the protein space for extending the detection of weak homology foldsNMR studies of protein hydration and TEMPOL accessibility.Molecular modelling of S1 and S2 subunits of SARS coronavirus spike glycoprotein.Three-dimensional computation of atom depth in complex molecular structures.Tendamistat surface accessibility to the TEMPOL paramagnetic probe.NMR studies of protein surface accessibility.On the dynamics of water molecules at the protein solute interfaces.ApreciseKUre: an approach of Precision Medicine in a Rare Disease.Cross-host evolution of severe acute respiratory syndrome coronavirus in palm civet and human.The use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility.Biochemical filtering of a protein-protein docking simulation identifies the structure of a complex between a recombinant antibody fragment and alpha-bungarotoxin.Interdomain tilt angle determines integrin-dependent function of the ninth and tenth FIII domains of human fibronectin.Efficacy and toxicity of the antimicrobial peptide M33 produced with different counter-ions.Investigations into the killing activity of an antimicrobial peptide active against extensively antibiotic-resistant K. pneumon iae and P. aeruginosa.Stable peptide inhibitors prevent binding of lethal and oedema factors to protective antigen and neutralize anthrax toxin in vivo.A structurally driven analysis of thiol reactivity in mammalian albumins.Structure and function correlations between the rat liver threonine deaminase and aminotransferases.ProCoCoA: A quantitative approach for analyzing protein core composition.Metal ion complexation and folding of linear peptides.NMR studies on Ni(II) induced cyclization of a histidine-tagged peptide.Searching for protein binding sites from Molecular Dynamics simulations and paramagnetic fragment-based NMR studies.NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.NMR studies of the inclusion complex between beta-cyclodextrin and paroxetine.Homogentisic acid induces aggregation and fibrillation of amyloidogenic proteins.A Computational Approach From Gene to Structure Analysis of the Human ABCA4 Transporter Involved in Genetic Retinal Diseases.Toward a generalized computational workflow for exploiting transient pockets as new targets for small molecule stabilizers: Application to the homogentisate 1,2-dioxygenase mutants at the base of rare disease Alkaptonuria.Prediction of quaternary assembly of SARS coronavirus peplomer.MD and NMR studies of alpha-bungarotoxin surface accessibility.Hot spot mapping of protein surfaces with TEMPOL: Bovine pancreatic RNase A as a model system.Near-infrared quantum dots labelled with a tumor selective tetrabranched peptide for in vivo imaging.On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus.NMR Studies of Lysozyme Surface Accessibility by Using Different Paramagnetic Relaxation ProbesA branched peptide mimotope of the nicotinic receptor binding site is a potent synthetic antidote against the snake neurotoxin alpha-bungarotoxinMolecular basis of branched peptides resistance to enzyme proteolysisProtein-thiol substitution or protein dethiolation by thiol/disulfide exchange reactions: the albumin modelNMR studies of BPTI aggregation by using paramagnetic relaxation reagentsMolecular definition of the interaction between a tumor-specific tetrabranched peptide and LRP6 receptor
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Q27637520-142687E3-0A4D-4FFE-A33A-993B1F353BA5Q27676787-E4C19A9D-460D-4451-8852-11F26F859415Q28344755-94E599F5-7562-415F-A799-841384A30784Q29028094-ABDFD4B6-108C-45B5-8D23-54281B27CCD6Q30333359-65B3C943-2395-4419-81C4-EC308EF0CF6FQ30336102-36202B57-FE15-426B-A4F7-7A7DC80E298EQ30350542-2B9E79C3-093E-4C29-9DF0-0CE9938D6EF6Q30585670-A3447C04-812F-47EC-A60D-812FA73CC0FFQ30660259-7F4DD30A-CDA8-43B6-8791-F5245E870417Q30975715-93805850-7D5C-4F3F-A87B-3D244F639A2EQ33564599-54FA4D68-6F8A-4550-9971-77B322BB229BQ33849474-A46D5798-D16A-440F-9CBE-5AF97396E6B5Q34250121-6D3BA856-C063-48E0-88D5-67F39FD58509Q38358920-6FCF4273-F12D-4435-8F2B-DE9A4074933BQ38912634-A290BD5E-ED1F-4AD5-93DB-D4E0BD6A1931Q39460911-4C0A2633-83BC-4A8C-AB2D-023B155EB725Q40184373-C773DC76-89ED-47DF-AE65-2EEE1AA596ECQ42071455-797614D6-1D43-47BB-925F-4DC0E13326ADQ42688210-2F6C7D98-B4AE-49AF-B730-91DD08B53E0BQ42693013-7A34A766-8C95-4F90-BCFD-67992B592BC6Q43442741-3A2E7E3D-9219-4C4D-86F4-6EBCFF4FEABBQ44019628-24B077AC-CE22-44BB-8EC9-C7CE36FC60E0Q44252713-BC587D3B-7A7C-4925-8FA4-57F153129D01Q44808304-1E110331-F72F-4AF9-A4D3-9E549D680A4DQ44921896-9C10B70E-C30B-4EB4-8543-E1D1FD8D190EQ44986957-9C9691F6-48C6-4424-9E13-B43F8D6C0CDCQ46589425-E68F0B4E-75E5-4FD2-BBD0-6BFE9BAFEA04Q47628653-012FB568-2BD7-4D4C-8050-D686144C9469Q47859966-9A548FCD-B061-4408-A870-994E811F57C8Q47893120-E2091162-84C9-4903-9323-823C0D3B4811Q50173672-A90E0F89-91E7-4B53-B287-F6F5295C2E4EQ51301434-B59FAFC4-A967-41A5-8240-8933BFAC98D7Q52676096-E9F5B01B-7103-41E1-9A27-1F3D9198C260Q54628430-749C5E19-B632-4B2F-876F-5DF53E6B3994Q59310273-53AC1C35-E160-4474-BEB5-F8F60C069B82Q74576778-CDC6A29C-6554-427E-81A0-454497E01B80Q80176085-96E73B65-519C-4AFC-9BC8-16B0BDEEAF19Q80559801-0E23887D-9980-461B-83B6-9C0F235C4E9FQ83180524-DD7A6ED4-5025-41BB-8BF6-29528A1E452EQ96581501-77209626-D46C-4B41-A878-104CE75DC259
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Andrea Bernini
@ast
Andrea Bernini
@en
Andrea Bernini
@es
Andrea Bernini
@nl
Andrea Bernini
@sl
type
label
Andrea Bernini
@ast
Andrea Bernini
@en
Andrea Bernini
@es
Andrea Bernini
@nl
Andrea Bernini
@sl
prefLabel
Andrea Bernini
@ast
Andrea Bernini
@en
Andrea Bernini
@es
Andrea Bernini
@nl
Andrea Bernini
@sl
P106
P31
P496
0000-0002-7528-2749