about
Modeling the dynamics of the solvated SL1 domain of HIV-1 genomic RNA.Modeling (15)N NMR chemical shift changes in protein backbone with pressure.Modeling of the Zn2+ binding in the 1-16 region of the amyloid beta peptide involved in Alzheimer's disease.Generalized electrostatic model of the wrapping of DNA around oppositely charged proteins.Combined EPR and molecular modeling study of PPI dendrimers interacting with copper ions: effect of generation and maltose decoration.A first-principle calculation of the XANES spectrum of Cu(2+) in water.Wrapped-around models for the lac operon complex.Modeling the Cu+ binding in the 1-16 region of the amyloid-β peptide involved in Alzheimer's disease.Modeling the interplay of glycine protonation and multiple histidine binding of copper in the prion protein octarepeat subdomains.Designing generalized statistical ensembles for numerical simulations of biopolymers.Modeling copper binding to the amyloid-β peptide at different pH: toward a molecular mechanism for Cu reduction.Towards a high-throughput modelling of copper reactivity induced by structural disorder in amyloid peptides.Zn induced structural aggregation patterns of β-amyloid peptides by first-principle simulations and XAS measurements.Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Aβ Peptide and O2.Identifying, by first-principles simulations, Cu[amyloid-β] species making Fenton-type reactions in Alzheimer's disease.Metal ions and intrinsically disordered proteins and peptides: from Cu/Zn amyloid-β to general principles.The mechanism of hydrogen uptake in [NiFe] hydrogenase: first-principles molecular dynamics investigation of a model compound.Ab initio simulations of Cu binding sites on the N-terminal region of prion protein.Impact of Cu(II) Binding on Structures and Dynamics of Aβ42 Monomer and Dimer: Molecular Dynamics Study.Modeling the dynamics of a mutated stem-loop in the SL1 domain of HIV-1Lai genomic RNA by 1H-NOESY spectra.Smoluchowski dynamics of the vnd/NK-2 homeodomain from Drosophila melanogaster: first-order mode-coupling approximation.Multi-scale theoretical approach to X-ray absorption spectra in disordered systems: an application to the study of Zn(ii) in waterExploring the Reactions of β-Amyloid (Aβ) Peptide 1–28 with AlIIIand FeIIIIonsConformational Dynamics of Hyaluronan in Solution. 2. Mode-Coupling Diffusion Approach to OligomersUnderstanding the Exceptional Properties of Nitroacetamides in Water: A Computational Model Including the SolventMeasuring electron sharing between atoms in first-principle simulationsThe enzymatic mechanism of carboxypeptidase: a molecular dynamics studyMode-coupling smoluchowski dynamics of a double-stranded DNA oligomerMolecular statistics of cytochrome c: structural plasticity and molecular environmentElectrostatic interactions with histone tails may bend linker DNA in chromatinModeling H3 histone N-terminal tail and linker DNA interactionsInsights into the mechanisms of amyloid formation of Zn(II)-Ab11-28: pH-dependent zinc coordination and overall charge as key parameters for kinetics and the structure of Zn(II)-Ab11-28 aggregatesCopper Binding Induces Polymorphism in Amyloid-β Peptide: Results of Computational ModelsComputational Model to Unravel the Function of Amyloid-β Peptides in Contact with a Phospholipid MembraneDealing with Cu reduction in X-ray absorption spectroscopy experimentsComputational models explain how copper binding to amyloid-β peptide oligomers enhances oxidative pathways
P50
Q30789262-2537BB82-A242-48F3-AA85-084E7F8E6C73Q31126228-23356AC4-711B-4D60-ACBE-5FCD679B6812Q33509039-3F48570F-355C-415D-BAF3-A4A1D3DD305DQ36748437-7BA0DBEA-D44E-441A-806A-346906A5B953Q38304001-8CEF347A-D265-48A0-807A-0301CE4970BFQ40475545-6CCD0616-37EA-4CC1-BCDD-B228EBD652CCQ41005667-9F0A9BB0-C3FF-4DF4-9401-78595BBBF237Q42840663-3936E499-DE3C-4C91-9296-040CBB33349AQ43433755-326B4858-1C70-4BC1-970E-FD5A0F371AE4Q45154378-D7E53FEB-B138-4F71-98ED-22D35774642BQ45221656-AD127EE7-52D9-47A7-B38C-70DE3BC63B51Q46237665-51E6F500-ECB1-4D99-BE60-F8092180883AQ46558162-F3795137-4225-4E63-B3AF-1A923646BAA6Q46629246-2C2E16FF-4E80-4444-A76E-EFC3AFAC0D43Q46650994-A586C412-219A-4E17-875B-104B856DAD5CQ46887798-B1CF76B6-B53A-452B-9479-4EA16A0169DEQ50064034-2D1EEFB9-1393-4B8A-AF2A-0B3279A707C2Q50088409-3E3D1CD7-EA6C-4B41-9F8F-3F93B70A5550Q51618830-C3DB3EBD-AFFB-4188-9C89-E7EE5E959BEAQ52054981-01E3B471-F372-452A-8ADC-09F4EFB0A72EQ52568351-784B8859-FE4C-47EE-AB72-5BB516662F9FQ57040822-EA7D6798-B210-4435-A53D-AD8B4DCECF46Q58856065-33D53A2D-373D-4147-8F38-A7AD3D9455F2Q60405425-208C3207-44D2-46E3-ACB2-C48C95ED407BQ60957188-171B7F0D-9C03-4462-8D60-C6BFE75E5EC8Q61857779-24DDF88D-7FE6-4367-A340-392DF308A4B8Q72367448-FE0CCE6C-FEDC-424F-9A70-BCE809151A99Q73047545-945C7031-CFF0-4C47-8D78-4D59CE3797B7Q79280594-47415BD5-FB95-4D3A-BCDB-18F9EA28F137Q81225422-709C93C5-575B-4BC3-A227-ADC712FB647FQ83324658-274C08F9-149E-49A2-8507-552226895C79Q84526980-E142B837-1808-4341-939E-C1B1E755A758Q89349165-5773C812-5FAB-41B1-ACDA-098D0CD76FF6Q90652931-87477796-992E-4850-8033-97304D22977FQ91574034-47E82491-989E-48F2-9585-85C669681718Q92995422-1DEB434A-319C-45AD-88CA-44B8F6319C8D
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Giovanni La Penna
@ast
Giovanni La Penna
@en
Giovanni La Penna
@es
Giovanni La Penna
@nl
Giovanni La Penna
@sl
type
label
Giovanni La Penna
@ast
Giovanni La Penna
@en
Giovanni La Penna
@es
Giovanni La Penna
@nl
Giovanni La Penna
@sl
prefLabel
Giovanni La Penna
@ast
Giovanni La Penna
@en
Giovanni La Penna
@es
Giovanni La Penna
@nl
Giovanni La Penna
@sl
P1053
E-5241-2011
P106
P21
P2798
P31
P3829
P496
0000-0002-8619-4867