Andrea Cavalli

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Publications associées (29)

Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo

The fatty acid amide hydrolase (FAAH) regulates the endocannabinoid system cleaving primarily the lipid messenger anandamide. FAAH has been well characterized over the years and, importantly, it represents a promising drug target to treat several diseases, ...

2015

Computational insights into function and inhibition of fatty acid amide hydrolase

Ursula Röthlisberger, Giulia Palermo, Andrea Cavalli

The Fatty Acid Amide Hydrolase (FAAH) enzyme is a membrane-bound serine hydrolase responsible for the deactivating hydrolysis of a family of naturally occurring fatty acid amides. FAAH is a critical enzyme of the endocannabinoid system, being mainly respon ...

Elsevier2015

Hydrolysis of anandamide in FAAH shows that nitrogen inversion is key to efficient enzyme-assisted amide bond cleavage

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo

Amer Chemical Soc2014

Molecular dynamics and mutagenesis studies indicate structural flexibility as a key factor for substrate specificity in FAAH catalysis

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo

Amer Chemical Soc2014

Wagging the Tail: Essential Role of Substrate Flexibility in FAAH Catalysis

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo, Marilisa Neri

The serine hydrolase, fatty acid amide hydrolase (FAAH), is responsible for the intracellular degradation of anandamide and other bioactive fatty acid ethanolamides involved in the regulation of pain, inflammation, and other pathophysiological processes. T ...

Amer Chemical Soc2013

Molecular Simulations Highlight the Role of Metals in Catalysis and Inhibition of Type II Topoisomerase

Matteo Dal Peraro, Marco Stenta, Andrea Cavalli

Type II topoisomerase (topoII) is a metalloenzyme targeted by clinical antibiotics and anticancer agents. Here, we integrate existing structural data with molecular simulation and propose a model for the yet uncharacterized structure of the reactant state ...

Amer Chemical Soc2013

Fatty acid amide hydrolase (FAAH) substrate specificity understood via molecular dynamics

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo, Marilisa Neri

Amer Chemical Soc2013

Dynamics of catalytic metals during DNA cleavage in type II topoisomerase

Matteo Dal Peraro, Marco Stenta, Andrea Cavalli, Giulia Palermo

Amer Chemical Soc2013

Common mechanistic features among metallo-β-lactamases: a computational study of Aeromonas hydrophila CphA enzyme

Matteo Dal Peraro, Andrea Cavalli, Paolo Carloni

Metallo-β-lactamases (MβLs) constitute an increasingly serious clinical threat by giving rise to β-lactam antibiotic resistance. They accommodate in their catalytic pocket one or two zinc ions, which are responsible for the hydrolysis of β-lactams. Recent ...

2009

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Hydrolysis of anandamide in FAAH shows that nitrogen inversion is key to efficient enzyme-assisted amide bond cleavage

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo

Amer Chemical Soc2014

Molecular dynamics and mutagenesis studies indicate structural flexibility as a key factor for substrate specificity in FAAH catalysis

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo

Amer Chemical Soc2014

Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets

Ursula Röthlisberger, Pablo Campomanes Ramos, Andrea Cavalli, Giulia Palermo

2015