D. Milardi

发表

Analytical model and multiscale simulations of Aβ peptide aggregation in lipid membranes: towards a unifying description of conformational transitions, oligomerization and membrane damage.

M. Karttunen, Martina Pannuzzo, D. Milardi, 2013, Physical chemistry chemical physics : PCCP.

Insulin-Degrading Enzyme Is a Non Proteasomal Target of Carfilzomib and Affects the 20S Proteasome Inhibition by the Drug

P. Cascio, F. Polticelli, M. Coletta, 2022, Biomolecules.

The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges

S. Marini, P. Lacal, G. Graziani, 2020, Pharmacology & Therapeutics.

Phospholipids Critical Micellar Concentrations Trigger Different Mechanisms of Intrinsically Disordered Proteins Interaction with Model Membranes.

D. Milardi, A. Raudino, C. La Rosa, 2018, The journal of physical chemistry letters.

Site directed mutagenesis of insulin-degrading enzyme allows singling out the molecular basis of peptidase versus E1-like activity: the role of metal ions.

M. Arizzi, D. Milardi, G. Grasso, 2019, Metallomics : integrated biometal science.

A neglected modulator of insulin-degrading enzyme activity and conformation: The pH.

C. Satriano, D. Milardi, G. Grasso, 2015, Biophysical chemistry.

EXPERIMENTAL MODEL FOR THE THERMAL DENATURATION OF AZURIN : A KINETIC STUDY

D. Milardi, R. Guzzi, L. Sportelli, 1996 .

The effects of scan rate and protein concentration on DSC thermograms of bovine superoxide dismutase

D. Milardi, C. L. Rosa, D. Grasso, 1995 .

Cations as switches of amyloid-mediated membrane disruption mechanisms: calcium and IAPP.

J. Brender, A. Ramamoorthy, D. Milardi, 2013, Biophysical journal.

Silybins are stereospecific regulators of the 20S proteasome.

G. Tundo, M. Coletta, D. Milardi, 2022, Bioorganic & medicinal chemistry.

Modulation of the 20S Proteasome Activity by Porphyrin Derivatives Is Steered through Their Charge Distribution

M. Coletta, M. Stefanelli, G. Tundo, 2022, Biomolecules.

Synthesis, biophysical characterization and anti-HIV activity of d(TG3AG) Quadruplexes bearing hydrophobic tails at the 5'-end.

J. Balzarini, D. Milardi, C. La Rosa, 2014, Bioorganic & medicinal chemistry.

The Ionophoric Activity of a Pro-Apoptotic VEGF165 Fragment on HUVEC Cells

M. Trincavelli, C. Martini, D. La Mendola, 2020, International journal of molecular sciences.

Extracellular truncated tau causes early presynaptic dysfunction associated with Alzheimer’s disease and other tauopathies

A. Borreca, M. Ciotti, A. Pittaluga, 2017, Oncotarget.

Calcium-activated membrane interaction of the islet amyloid polypeptide: implications in the pathogenesis of type II diabetes mellitus.

D. Milardi, C. La Rosa, M. Sciacca, 2008, Archives of biochemistry and biophysics.

Dipyridamole for tracking amyloidogenic proteins aggregation and enhancing polyubiquitination.

S. Sortino, D. Milardi, G. Grasso, 2022, Archives of biochemistry and biophysics.

Copper(II) ions affect the gating dynamics of the 20S proteasome: a molecular and in cell study

E. Rizzarelli, M. Salmona, G. Pappalardo, 2016, Scientific Reports.

Aβ and Tau Interact with Metal Ions, Lipid Membranes and Peptide-Based Amyloid Inhibitors: Are These Common Features Relevant in Alzheimer’s Disease?

G. Pappalardo, D. Milardi, G. Sabatino, 2022, Molecules.

Trehalose conjugates of silybin as prodrugs for targeting toxic Aβ aggregates.

G. Melacini, C. Bongiorno, N. Spinella, 2020, ACS chemical neuroscience.

Strategy to discover full-length amyloid-beta peptide ligands using high-efficiency microarray technology

C. Bongiorno, N. Spinella, C. Galati, 2017, Beilstein journal of nanotechnology.

Silybins inhibit human IAPP amyloid growth and toxicity through stereospeci ﬁ c interactions BBA - Proteins and Proteomics

I. Ilie, D. Milardi, A. Santoro, 2022 .

Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly.

D. Milardi, C. La Rosa, D. Grasso, 2005, Archives of biochemistry and biophysics.

Neurodegeneration: Metallostasis and Proteostasis

E. Rizzarelli, D. Milardi, 2011 .

Targeting immunoproteasome in neurodegeneration: A glance to the future.

P. Cascio, M. Coletta, P. Lacal, 2022, Pharmacology & therapeutics.

Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues.

E. Rizzarelli, G. Pappalardo, D. Milardi, 2005, Chemistry.

Differential scanning calorimetry of the irreversible denaturation of bovine superoxide dismutase

D. Milardi, C. L. Rosa, D. Grasso, 1994 .

Resveratrol interferes with the aggregation of membrane-bound human-IAPP: a molecular dynamics study.

D. Milardi, A. Raudino, C. La Rosa, 2015, European journal of medicinal chemistry.

Ubiquitin Associates with the N-Terminal Domain of Nerve Growth Factor: The Role of Copper(II) Ions.

G. Arena, E. Rizzarelli, D. Milardi, 2016, Chemistry.

Sequential Application of Ligand and Structure Based Modeling Approaches to Index Chemicals for Their hH4R Antagonism

Anwar Rayan, Salvatore Guccione, Livia Basile, 2014, PloS one.

Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03394c

M. Coletta, V. Nicoletti, C. Iacobucci, 2019, Chemical science.

Deciphering the zinc coordination properties of the prokaryotic zinc finger domain: The solution structure characterization of Ros87 H42A functional mutant.

D. Milardi, L. Russo, R. Fattorusso, 2014, Journal of inorganic biochemistry.

Inorganic stressors of ubiquitin.

G. Arena, E. Rizzarelli, G. Frasca, 2013, Inorganic chemistry.

Zinc(II) complexes of ubiquitin: speciation, affinity and binding features.

G. Arena, E. Rizzarelli, D. Milardi, 2011, Chemistry.

Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding.

A. Magrì, G. Natile, E. Rizzarelli, 2007, Angewandte Chemie.

Amino- and chloro-8-hydroxyquinolines and their copper complexes as proteasome inhibitors and antiproliferative agents.

D. Milardi, C. Sgarlata, G. Vecchio, 2017, Metallomics : integrated biometal science.

Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: synergism among multiple depletions.

D. Milardi, C. La Rosa, M. Verbeet, 2003, Archives of biochemistry and biophysics.

New comprehensive studies of a gold(III) Dithiocarbamate complex with proven anticancer properties: Aqueous dissolution with cyclodextrins, pharmacokinetics and upstream inhibition of the ubiquitin-proteasome pathway.

P. Caliceti, G. Pappalardo, D. Milardi, 2017, European journal of medicinal chemistry.

Endogenous and artificial miRNAs explore a rich variety of conformations: a potential relationship between secondary structure and biological functionality

C. Croce, G. Piccialli, A. Pulvirenti, 2020, Scientific Reports.

Stabilization vs. destabilization of G-quadruplex superstructures: the role of the porphyrin derivative having spermine arms.

G. Piccialli, R. Purrello, D. Milardi, 2017, Physical chemistry chemical physics : PCCP.

Cationic porphyrins are reversible proteasome inhibitors.

Danilo Milardi, R. Purrello, D. Milardi, 2012, Journal of the American Chemical Society.

Zinc to cadmium replacement in the prokaryotic zinc-finger domain.

D. Milardi, L. Russo, R. Fattorusso, 2014, Metallomics : integrated biometal science.

Structural characterization of the thermal unfolding pathway of human VEGFR1 D2 domain

D. Milardi, R. Fattorusso, C. Isernia, 2021, The FEBS journal.

The change of conditions does not affect Ros87 downhill folding mechanism

D. Milardi, L. Russo, R. Fattorusso, 2020, Scientific Reports.

Structural Zn(II) implies a switch from fully cooperative to partly downhill folding in highly homologous proteins.

D. Milardi, L. Russo, R. Fattorusso, 2013, Journal of the American Chemical Society.

Substitution of the Native Zn(II) with Cd(II), Co(II) and Ni(II) Changes the Downhill Unfolding Mechanism of Ros87 to a Completely Different Scenario

D. Milardi, L. Russo, R. Fattorusso, 2020, International journal of molecular sciences.

Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc00166a

S. Gianni, M. Coletta, D. Milardi, 2018, Chemical science.

Multiple functions of insulin-degrading enzyme: a metabolic crosslight?

P. van Endert, F. Polticelli, M. Coletta, 2017, Critical reviews in biochemistry and molecular biology.

Silybins inhibit human IAPP amyloid growth and toxicity through stereospecific interactions.

A. Caflisch, I. Ilie, D. Milardi, 2022, Biochimica et biophysica acta. Proteins and proteomics.

Investigation on the solid-phase synthesis of silybin prodrugs and their timed-release.

D. Milardi, G. Di Fabio, V. Romanucci, 2021, Bioorganic & medicinal chemistry.

Modulating Aβ aggregation by tyrosol-based ligands: The crucial role of the catechol moiety.

D. Milardi, Fabio Lolicato, R. Bernini, 2020, Biophysical chemistry.

Inhibition of Aβ Amyloid Growth and Toxicity by Silybins: The Crucial Role of Stereochemistry.

M. Salmona, L. Diomede, C. Bongiorno, 2017, ACS chemical neuroscience.

Carnosine Inhibits Aβ42 Aggregation by Perturbing the H‐Bond Network in and around the Central Hydrophobic Cluster

A. Caflisch, E. Rizzarelli, A. Corazza, 2013, Chembiochem : a European journal of chemical biology.

Amyloid growth and membrane damage: Current themes and emerging perspectives from theory and experiments on Aβ and hIAPP.

D. Milardi, C. La Rosa, Federica Scollo, 2018, Biochimica et biophysica acta. Biomembranes.

The Role of Cholesterol in Driving IAPP-Membrane Interactions.

C. Satriano, A. Ramamoorthy, D. Milardi, 2016, Biophysical journal.

Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes.

S. Radford, A. Caflisch, E. Gazit, 2021, Chemical reviews.

Symmetry-breaking transitions in the early steps of protein self-assembly

Trang N. Do, F. Fraternali, M. Karttunen, 2020, European Biophysics Journal.

Defective proteasome biogenesis into skin fibroblasts isolated from Rett syndrome subjects with MeCP2 non-sense mutations.

S. Marini, L. Campagnolo, G. Valacchi, 2020, Biochimica et biophysica acta. Molecular basis of disease.

Amyloid-Mediated Mechanisms of Membrane Disruption

D. Milardi, C. La Rosa, M. Sciacca, 2021 .

The interplay between lipid and Aβ amyloid homeostasis in Alzheimer's Disease: risk factors and therapeutic opportunities.

G. Tundo, M. Coletta, D. Milardi, 2021, Chemistry and physics of lipids.

Pyrazolones Activate the Proteasome by Gating Mechanisms and Protect Neuronal Cells from β‐Amyloid Toxicity

V. Nicoletti, M. Arizzi, G. Tundo, 2019, ChemMedChem.

Metal Binding to Prion Protein

E. Rizzarelli, G. Pappalardo, D. Milardi, 2003 .

A molecular dynamics study on the conformational stability of PrP 180–193 helix II prion fragment

C. Zannoni, E. Rizzarelli, D. Milardi, 2004 .

The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes.

E. Rizzarelli, D. Milardi, C. La Rosa, 2004, Chemical communications.

Identification of a novel adiponectin receptor and opioid receptor dual acting agonist as a potential treatment for diabetic neuropathy.

K. Chan, D. Milardi, L. Basile, 2022, Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie.

Computational Comparison of Imidazoline Association with the I2 Binding Site in Human Monoamine Oxidases

Salvatore Guccione, Rona R. Ramsay, Livia Basile, 2014, J. Chem. Inf. Model..

Lipid-Chaperone Hypothesis: A Common Molecular Mechanism of Membrane Disruption by Intrinsically Disordered Proteins.

Bikash R. Sahoo, Jennifer C. Lee, A. Ramamoorthy, 2020, ACS chemical neuroscience.

α-Helical Structures Drive Early Stages of Self-Assembly of Amyloidogenic Amyloid Polypeptide Aggregate Formation in Membranes

Danilo Milardi, Mikko Karttunen, M. Karttunen, 2013, Scientific Reports.

Aβ8-20 Fragment as an Anti-Fibrillogenic and Neuroprotective Agent: Advancing toward Efficient Alzheimer’s Disease Treatment

G. Pappalardo, D. Milardi, G. Sabatino, 2023, ACS chemical neuroscience.

The active role of Ca2+ ions in Aβ-mediated membrane damage.

D. Milardi, C. La Rosa, M. Sciacca, 2018, Chemical communications.

Copper(II) and zinc(II) dependent effects on Aβ42 aggregation: a CD, Th-T and SFM study

G. Pappalardo, D. Milardi, S. Cataldo, 2013 .

Insulin has multiple antiamyloidogenic effects on human neuronal cells.

G. Pandini, R. Vigneri, A. Copani, 2013, Endocrinology.

Thermodynamics and kinetics of the thermal unfolding of plastocyanin

D. Milardi, C. La Rosa, R. Guzzi, 1998, European Biophysics Journal.

An alternative approach in the structure-based predictions of the thermodynamics of protein unfolding.

D. Milardi, C. La Rosa, D. Grasso, 1997, Biophysical chemistry.

Theoretical basis for differential scanning calorimetric analysis of multimeric proteins.

D. Milardi, D. Grasso, C. Rosa, 1996, Biophysical chemistry.

Contributions of polar and apolar groups to the thermodynamic stability of azurin

D. Milardi, D. Grasso, S. Fasone, 1996 .

Extended theoretical analysis of irreversible protein thermal unfolding.

D. Milardi, C. La Rosa, D. Grasso, 1994, Biophysical chemistry.

Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States

M. Coletta, G. Tundo, R. Purrello, 2020, International journal of molecular sciences.

The insulin-degrading enzyme is an allosteric modulator of the 20S proteasome and a potential competitor of the 19S

M. Coletta, S. Marini, G. Tundo, 2018, Cellular and Molecular Life Sciences.

Electrostatic Map Of Proteasome α-Rings Encodes The Design of Allosteric Porphyrin-Based Inhibitors Able To Affect 20S Conformation By Cooperative Binding

R. Paolesse, M. Coletta, M. Stefanelli, 2017, Scientific Reports.

Cationic porphyrins are tunable gatekeepers of the 20S proteasome† †Electronic supplementary information (ESI) available: It is reporting computational details, semi-log plots of residual CP activities, Molprobity results. See DOI: 10.1039/c5sc03312h

G. Tundo, M. Coletta, R. Purrello, 2015, Chemical science.

The double faced role of copper in Aβ homeostasis: A survey on the interrelationship between metal dyshomeostasis, UPS functioning and autophagy in neurodegeneration

M. Coletta, S. Marini, G. Tundo, 2017 .

Determination of the Conformation of the Human VDAC1 N‐Terminal Peptide, a Protein Moiety Essential for the Functional Properties of the Pore

R. Benz, A. Messina, V. De Pinto, 2007, Chembiochem : a European journal of chemical biology.

Conformational Properties and Functional Role of VDAC N-Terminal Peptide

A. Messina, A. Magrì, G. Pappalardo, 2006 .

The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: a DSC study

G. Pappalardo, D. Milardi, G. Impellizzeri, 2002 .

DSC study of the interaction of the prion peptide PrP106–126 with artificial membranes

E. Rizzarelli, D. Milardi, D. Grasso, 2001 .

Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP12–18 and IAPP21–27 peptides

D. Milardi, M. Sciacca, D. Grasso, 2010 .

The role of aromatic side-chains in amyloid growth and membrane interaction of the islet amyloid polypeptide fragment LANFLVH

D. Milardi, M. Sciacca, D. Grasso, 2010, European Biophysics Journal.

Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptide

G. Colombo, D. Milardi, C. La Rosa, 2015, Scientific Reports.

Evaluation of thermodynamic properties of irreversible protein thermal unfolding measured by DSC

D. Milardi, G. Manetto, D. Grasso, 2005 .

Copper, differently from zinc, affects the conformation, oligomerization state and activity of bradykinin.

I. Naletova, V. Nicoletti, A. Pietropaolo, 2016, Metallomics : integrated biometal science.

Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: the role of copper(II) ions, pH, and membrane mimicking environments.

D. La Mendola, E. Rizzarelli, G. Pappalardo, 2010, The journal of physical chemistry. B.

Steered molecular dynamics studies reveal different unfolding pathways of prions from mammalian and non-mammalian species

D. Milardi, D. Grasso, M. Pappalardo, 2007 .

A model for the thermal unfolding of amicyanin

D. Milardi, C. La Rosa, R. Guzzi, 2002, European Biophysics Journal.

Probing the helical stability in a VEGF-mimetic peptide.

D. Milardi, R. Fattorusso, A. Romanelli, 2021, Bioorganic chemistry.

The insulin degrading enzyme activates ubiquitin and promotes the formation of K48 and K63 diubiquitin.

E. Rizzarelli, A. Pietropaolo, D. Milardi, 2015, Chemical communications.

Repurposing of Copper(II)-chelating Drugs for the Treatment of Neurodegenerative Diseases.

G. Pappalardo, D. Milardi, V. Lanza, 2017, Current medicinal chemistry.

The role of copper(II) in the aggregation of human amylin.

A. Magrì, V. Nicoletti, G. Pappalardo, 2014, Metallomics : integrated biometal science.

The effect of copper/zinc replacement on the folding free energy of wild type and Cys3Ala/Cys26Ala azurin.

D. Milardi, C. La Rosa, R. Guzzi, 2003, International journal of biological macromolecules.

A blend of two resveratrol derivatives abolishes hIAPP amyloid growth and membrane damage.

J. Brender, A. Ramamoorthy, D. Milardi, 2018, Biochimica et biophysica acta. Biomembranes.

A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant.

D. Milardi, C. La Rosa, R. Guzzi, 1999, Biophysical journal.

Tau/Aβ chimera peptides: a Thioflavin-T and MALDI-TOF study of Aβ amyloidosis in the presence of Cu(II) or Zn(II) ions and Total Lipid Brain Extract (TLBE) vesicles.

G. Pappalardo, D. Milardi, M. Sciacca, 2021, Chemistry and physics of lipids.

Molecular and cytotoxic properties of hIAPP17-29 and rIAPP17-29 fragments: a comparative study with the respective full-length parent polypeptides.

G. Pappalardo, D. Milardi, M. Giuffrida, 2014, European journal of medicinal chemistry.

Unveiling the unfolding pathway of FALS associated G37R SOD1 mutant: a computational study.

D. Milardi, C. La Rosa, D. Grasso, 2010, Molecular bioSystems.

Calorimetric Evidences for Copper(II)-Regulated Chiral Recognition Between Decanucleotide 5′d(CTGGATCCAG)2 and ALA-TRP Dipeptides

D. Milardi, D. Grasso, V. Cucinotta, 1997 .

Homology‐based Modeling of Rhodopsin‐like Family Members in the Inactive State: Structural Analysis and Deduction of Tips for Modeling and Optimization

D. Milardi, S. Guccione, A. Rayan, 2017, Molecular informatics.

Tau/Aβ chimera peptides: Evaluating the dual function of metal coordination and membrane interaction in one sequence.

G. Pappalardo, D. Milardi, M. Sciacca, 2020, Journal of inorganic biochemistry.

The insulin-degrading enzyme is an allosteric modulator of the 20S proteasome and a potential competitor of the 19S

M. Coletta, S. Marini, G. Tundo, 2018, Cellular and Molecular Life Sciences.

The Role Played by the α‐Helix in the Unfolding Pathway and Stability of Azurin: Switching Between Hierarchic and Nonhierarchic Folding

D. Milardi, C. La Rosa, R. Guzzi, 2007, Chembiochem : a European journal of chemical biology.

Thermodynamics of the thermal unfolding of azurin

D. Milardi, R. Guzzi, L. Sportelli, 1995 .

Role of electrostatics in the thermal stability of ubiquitin

D. Milardi, M. Sciacca, D. Grasso, 2006 .

Interactions of two O-phosphorylresveratrol derivatives with model membranes.

D. Milardi, C. La Rosa, M. Sciacca, 2012, Archives of biochemistry and biophysics.

Interaction of prion peptide PrP 180-193 with DPPC model membranes: a thermodynamic study

E. Rizzarelli, D. Milardi, D. Grasso, 2003 .

Thermodynamics of azurin folding

D. Milardi, M. Sciacca, D. Grasso, 2008 .

The Role of Calcium, Lipid Membranes and Islet Amyloid Polypeptide in the Onset of Type 2 Diabetes: Innocent Bystanders or Partners in a Crime?

D. Milardi, C. La Rosa, M. Sciacca, 2014, Front. Endocrinol..

Endogenous and artificial miRNAs explore a rich variety of conformations: a potential relationship between secondary structure and biological functionality

C. Croce, G. Piccialli, A. Pulvirenti, 2020, Scientific Reports.

Molecular dynamics: new advances in drug discovery.

Matteo Pappalardo, Danilo Milardi, D. Milardi, 2015, European journal of medicinal chemistry.

Electronic Circular Dichroism Detects Conformational Changes Associated with Proteasome Gating Confirmed Using AFM Imaging

P. Osmulski, M. Gaczynska, R. Purrello, 2023, Biomolecules.

Environmental factors differently affect human and rat IAPP: conformational preferences and membrane interactions of IAPP17-29 peptide derivatives.

A. Magrì, E. Rizzarelli, G. Pappalardo, 2007, Chemistry.

A combined scanning dilatometric and differential scanning calorimetric study of the thermal unfolding of bovine serum albumin

D. Milardi, D. Grasso, S. Fasone, 1994 .

Ubiquitin binds the amyloid β peptide and interferes with its clearance pathways† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc03394c

M. Coletta, V. Nicoletti, C. Iacobucci, 2019, Chemical science.

Synthesis of New Tyrosol‐Based Phosphodiester Derivatives: Effect on Amyloid β Aggregation and Metal Chelation Ability

D. Milardi, M. Iuliano, G. De Tommaso, 2020, ChemMedChem.

G. Tundo, M. Coletta, R. Purrello, 2015, Chemical science.

Structural characterization of the porphyrins/proteasome interaction

M. Coletta, G. Tundo, M. Coletta, 2020 .

The role of the Cys2-Cys7 disulfide bridge in the early steps of Islet amyloid polypeptide aggregation: A molecular dynamics study

Martina Pannuzzo, D. Milardi, D. Grasso, 2008 .