Search results for: Michael Assfalg

Items from 1 to 20 out of 40 results

article

Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

Francesca Parolini, Elham Ataie Kachoie, Giulia Leo, Laura Civiero, more

Angewandte Chemie > 135 > 50 > n/a - n/a

Post‐translational modifications of Tau are emerging as key players in determining the onset and progression of different tauopathies such as Alzheimer's disease, and are recognized to mediate the structural diversity of the disease‐specific Tau amyloids. Here we show that the E3 ligase CHIP catalyzes the site‐specific ubiquitination of Tau filaments both in vitro and in cellular models, proving that...

article

Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

Francesca Parolini, Elham Ataie Kachoie, Giulia Leo, Laura Civiero, more

Angewandte Chemie International Edition > 62 > 50 > n/a - n/a

article

Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP

Francesca Munari, Luca Mollica, Carlo Valente, Francesca Parolini, more

Angewandte Chemie International Edition > 61 > 15 > n/a - n/a

The multi‐site ubiquitination of Tau protein found in Alzheimer's disease filaments hints at the failed attempt of neurons to remove early toxic species. The ubiquitin‐dependent degradation of Tau is regulated in vivo by the E3 ligase CHIP, a quality controller of the cell proteome dedicated to target misfolded proteins for degradation. In our study, by using site‐resolved NMR, biochemical and computational...

article

Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP

Francesca Munari, Luca Mollica, Carlo Valente, Francesca Parolini, more

Angewandte Chemie > 134 > 15 > n/a - n/a

article

Semisynthetic and Enzyme‐Mediated Conjugate Preparations Illuminate the Ubiquitination‐Dependent Aggregation of Tau Protein

Francesca Munari, Carlo G. Barracchia, Cinzia Franchin, Francesca Parolini, more

Angewandte Chemie > 132 > 16 > 6669 - 6673

In the brain of individuals with Alzheimer's disease, the regulatory protein ubiquitin is found conjugated to different lysine residues of tau protein assembled into pathological paired helical filaments. To shed light on the hitherto unexplored ubiquitination‐linked conformational transitions of tau, the availability of in vitro ubiquitin conjugation methods is of primary importance. In our work,...

article

Semisynthetic and Enzyme‐Mediated Conjugate Preparations Illuminate the Ubiquitination‐Dependent Aggregation of Tau Protein

Francesca Munari, Carlo G. Barracchia, Cinzia Franchin, Francesca Parolini, more

Angewandte Chemie International Edition > 59 > 16 > 6607 - 6611

article

Specific Interaction Sites Determine Differential Adsorption of Protein Structural Isomers on Nanoparticle Surfaces

Andrea Bortot, Serena Zanzoni, Mariapina D'Onofrio, Michael Assfalg

Chemistry – A European Journal > 24 > 22 > 5911 - 5919

In biological systems, nanoparticles (NPs) elicit bioactivity upon interaction with proteins. As a result of post‐translational modification, proteins occur in a variety of alternative covalent forms, including structural isomers, which present unique molecular surfaces. We aimed at a detailed description of the recognition of protein isomeric species by NP surfaces. The transient adsorption of isomeric...

article

Alzheimer’s disease-associated ubiquitin mutant Ubb+1: Properties of the carboxy-terminal domain and its influence on biomolecular interactions

Francesca Munari, Andrea Bortot, Michael Assfalg, Mariapina D’Onofrio

International Journal of Biological Macromolecules > 2018 > 108 > C > 24-31

Ubb⁺¹, a ubiquitin (Ub) mutant protein originating from misreading of the Ub B gene, is found accumulated in brain tissues of Alzheimer’s disease patients. The mutant attracts strong interest due to its possible participation in the molecular events leading to neurodegeneration. Ubb⁺¹ is composed of the globular domain of Ub, linked to a 19-residue C-terminal peptide. Based on NMR relaxation and solvent...

article

Molecular differences between human liver fatty acid binding protein and its T94A variant in their unbound and lipid-bound states

Mariapina D'Onofrio, Carlo Giorgio Barracchia, Andrea Bortot, Francesca Munari, more

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics > 2017 > 1865 > 9 > 1152-1159

Liver fatty acid binding protein (L-FABP) is an abundant cytosolic protein playing a central role in intracellular lipid trafficking. The L-FABP T94A variant, originating from one of the most common polymorphisms in the FABP family, is associated with several lipid-related disorders. However, the molecular factors that determine the observed functional differences are currently unknown.In our work,...

article

The long variant of human ileal bile acid-binding protein associated with colorectal cancer exhibits sub-cellular localization and lipid binding behaviour distinct from those of the common isoform

Mariapina D’Onofrio, Serena Zanzoni, Francesca Munari, Hugo L. Monaco, more

Biochimica et Biophysica Acta (BBA) - General Subjects > 2017 > 1861 > 9 > 2315-2324

Ileal bile acid-binding protein, IBABP, participates in the intracellular trafficking of bile salts and influences their signaling activities. The recently discovered variant, IBABP-L, bearing an N-terminal 49-amino acid extension, was found to be associated with colorectal cancer and to protect cancer cells from the cytotoxic effects of deoxycholate. However, the precise function and the molecular...

article

Unsaturated Long‐Chain Fatty Acids Are Preferred Ferritin Ligands That Enhance Iron Biomineralization

Serena Zanzoni, Katiuscia Pagano, Mariapina D'Onofrio, Michael Assfalg, more

Chemistry – A European Journal > 23 > 41 > 9879 - 9887

Ferritin is a ubiquitous nanocage protein, which can accommodate up to thousands of iron atoms inside its cavity. Aside from its iron storage function, a new role as a fatty acid binder has been proposed for this protein. The interaction of apo horse spleen ferritin (HoSF) with a variety of lipids has been here investigated through NMR spectroscopic ligand‐based experiments, to provide new insights...

article

Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell‐mimicking crowded solution

Francesca Munari, Andrea Bortot, Serena Zanzoni, Mariapina D'Onofrio, more

FEBS Letters > 591 > 7 > 979 - 990

Despite significant advancements in our understanding of ubiquitin‐mediated signaling, the influence of the intracellular environment on the formation of transient ubiquitin‐partner complexes remains poorly explored. In our work, we introduce macromolecular crowding as a first level of complexity toward the imitation of a cellular environment in the study of such interactions. Using NMR spectroscopy,...

article

Effects of macromolecular crowding on a small lipid binding protein probed at the single-amino acid level

Silvia Pérez Santero, Filippo Favretto, Serena Zanzoni, Roberto Chignola, more

Archives of Biochemistry and Biophysics > 2016 > 606 > C > 99-110

Macromolecular crowding is a distinctive feature of the cellular interior, influencing the behaviour of biomacromolecules. Despite significant advancements in the description of the effects of crowding on global protein properties, the influence of cellular components on local protein attributes has received limited attention. Here, we describe a residue-level systematic interrogation of the structural,...

article

The study of transient protein–nanoparticle interactions by solution NMR spectroscopy

Michael Assfalg, Laura Ragona, Katiuscia Pagano, Mariapina D'Onofrio, more

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics > 2016 > 1864 > 1 > 102-114

The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nanobio interfaces. Nanoparticles exhibit unique structures and properties, often different from the corresponding bulk materials, and the nature of their interactions with biological systems remains poorly characterized. Solution NMR spectroscopy is a mature technique for the...

article

The unique ligand binding features of subfamily-II iLBPs with respect to bile salts and related drugs

Filippo Favretto, Alberto Ceccon, Serena Zanzoni, Mariapina D’Onofrio, more

Prostaglandins, Leukotrienes and Essential Fatty Acids (PLEFA) > 2015 > 95 > Complete > 1-10

Intracellular lipid binding proteins (iLBPs) are a family of evolutionarily related small cytoplasmic proteins implicated in the transcellular transport of lipophilic ligands. Subfamily-II iLBPs include the liver fatty acid binding protein (L-FABP), and the ileal and the liver and ileal bile acid binding proteins (L-BABP and I-BABP). Atomic-level investigations during the past 15–20 years have delivered...

article

Bile salt recognition by human liver fatty acid binding protein

Filippo Favretto, Carlo Santambrogio, Mariapina D'Onofrio, Henriette Molinari, more

The FEBS Journal > 282 > 7 > 1271 - 1288

Fatty acid binding proteins (FABPs) act as intracellular carriers of lipid molecules, and play a role in global metabolism regulation. Liver FABP (L‐FABP) is prominent among FABPs for its wide ligand repertoire, which includes long‐chain fatty acids as well as bile acids (BAs). In this work, we performed a detailed molecular‐ and atomic‐level analysis of the interactions established by human L‐FABP...

article

The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins

Laura Ragona, Katiuscia Pagano, Simona Tomaselli, Filippo Favretto, more

BBA - Proteins and Proteomics > 2014 > 1844 > 7 > 1268-1278

Lipids are essential for many biological processes and crucial in the pathogenesis of several diseases. Intracellular lipid-binding proteins (iLBPs) provide mobile hydrophobic binding sites that allow hydrophobic or amphipathic lipid molecules to penetrate into and across aqueous layers. Thus iLBPs mediate the lipid transport within the cell and participate to a spectrum of tissue-specific pathways...

article

Searching for protein binding sites from Molecular Dynamics simulations and paramagnetic fragment-based NMR studies

Andrea Bernini, Lucia Henrici De Angelis, Edoardo Morandi, Ottavia Spiga, more

BBA - Proteins and Proteomics > 2014 > 1844 > 3 > 561-566

Hotspot delineation on protein surfaces represents a fundamental step for targeting protein–protein interfaces. Disruptors of protein–protein interactions can be designed provided that the sterical features of binding pockets, including the transient ones, can be defined. Molecular Dynamics, MD, simulations have been used as a reliable framework for identifying transient pocket openings on the protein...

article

¹H, ¹⁵N and ¹³C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov.

Clara Smal, Serena Zanzoni, Mariapina D’Onofrio, Henriette Molinari, more

Biomolecular NMR Assignments > 2014 > 8 > 2 > 415-418

A gene encoding a protein classified as alanyl-tRNA synthetase (AlaRS) was found in the genome of the psychrophilic bacteria Bizionia argentinensis. The enzyme is constituted by three domains with an evolutionarily conserved modular arrangement: the N-terminal aminoacylation domain, the editing domain and the C-terminal domain (C-Ala). Herein we report the near complete NMR resonance assignment of...

article

NMR investigation of the equilibrium partitioning of a water‐soluble bile salt protein carrier to phospholipid vesicles

Alberto Ceccon, Mariapina D'Onofrio, Serena Zanzoni, Dario Livio Longo, more

Proteins: Structure, Function, and Bioinformatics > 81 > 10 > 1776 - 1791

Membrane binding by cytosolic fatty acid binding proteins (FABP) appears to constitute a key step of intracellular lipid trafficking. We applied NMR spectroscopy to study the partitioning of a water‐soluble bile acid binding protein (BABP), belonging to the FABP family, between its free and lipid‐vesicle‐bound states. As the lipid‐bound protein was NMR‐invisible, the signals of the free biomolecule...

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Keywords

NMR SPECTROSCOPY (16)
NMR (6)
UBIQUITINATION (5)
MOLECULAR RECOGNITION (4)
PROTEINS (4)
BILE ACID BINDING PROTEIN (3)
CHIP E3 LIGASE (3)
PROTEIN DYNAMICS (3)
TAU PROTEIN (3)
UBIQUITIN (3)
ALZHEIMER'S DISEASE (2)
CHIP (2)
HETEROTYPIC COMPLEXES (2)
INTRACELLULAR LIPID BINDING PROTEIN (2)
LIPIDS (2)
MACROMOLECULAR CROWDING (2)
NUCLEAR MAGNETIC RESONANCE (2)
PARAMAGNETIC RELAXATION ENHANCEMENT (2)
PROTEIN MODIFICATIONS (2)
PROTEIN-LIGAND BINDING (2)
PROTEIN-PROTEIN INTERACTIONS (2)
SITE SELECTIVITY (2)
TAU AMYLOIDS (2)
BIZIONIA ARGENTINENSIS SP. NOV. (1)
AGGREGATION (1)
ALANYL-TRNA SYNTHETASE (1)
ALZHEIMER’S DISEASE (1)
AMPHITROPISM (1)
AMYLOID FIBRILS (1)
AMYLOIDFASERN (1)
AUTOMATIC ASSIGNMENT (1)
BILE ACIDS (1)
BILE SALT TRANSPORT (1)
BILE SALTS (1)
BINDING MECHANISMS (1)
BIOCHEMISTRY (1)
BIOMOLECULAR RECOGNITION (1)
CHEMICAL EXCHANGE SATURATION TRANSFER (1)
CHICKEN LIVER BILE ACID BINDING PROTEIN (1)
CHIP-E3-LIGASE (1)
CYTOCHROME C7 (1)
DIFFERENTIAL SCANNING CALORIMETRY (1)
DIFFUSION (1)
DOMAIN ORIENTATION (1)
DYNAMIC DRUG DESIGN (1)
ELECTRON TRANSFER (1)
FABP (1)
FATTY ACID BINDING PROTEIN (1)
FATTY ACIDS (1)
FERRITIN (1)
FRAGMENT-BASED HOTSPOT SCREENING (1)
GADOLINIUM (1)
HYDROGEN EXCHANGE (1)
IGA NEPHROPATHY (1)
ILEAL BILE ACID-BINDING PROTEIN (1)
INTERACTION (1)
INTERDOMAIN DYNAMICS (1)
INTRACELLULAR LIPID TRANSPORT (1)
LINE‐SHAPE ANALYSIS (1)
LIPID BINDING (1)
LIPID BINDING PROTEIN (1)
LIPID TRANSPORT (1)
LIPID VESICLE (1)
LIPID VESICLES (1)
LIPOSOMES (1)
LIVER BILE ACID BINDING PROTEIN (1)
LIVER FATTY ACID BINDING PROTEIN (1)
LONG VARIANT (1)
MASS SPECTROMETRY (1)
METABOLOMICS (1)
METAL COORDINATION (1)
MULTIHEME CYTOCHROMES (1)
NANOPARTICLE (1)
NANOPARTICLES (1)
NMR SOLUTION STRUCTURE (1)
PARAMAGNETIC PROBE (1)
POLYUBIQUITIN (1)
PROTEIN (1)
PROTEIN FOLDING/UNFOLDING (1)
PROTEIN LIGAND BINDING (1)
PROTEIN SEQUENCE (1)
PROTEIN STRUCTURE AND DYNAMICS (1)
PROTEIN-MEMBRANE INTERACTION (1)
PROTEIN–NANOPARTICLE INTERACTIONS (1)
PROTEIN–PROTEIN INTERACTION (1)
PSYCHROPHILIC BACTERIUM (1)
RECOMBINANT PROTEIN (1)
RELAXOMETRY (1)
RESIDUAL DIPOLAR COUPLINGS (1)
RESIDUAL STRUCTURE (1)
ROTATIONAL DIFFUSION (1)
SEMISYNTHESE (1)
SEMISYNTHESIS (1)
SOLVENT ACCESSIBILITY (1)
SPIN LABELING (1)
SPIN RELAXATION (1)
SUPEROXIDE DISMUTASE (1)
T94A VARIANT (1)
TAU-PROTEIN (1)
THERMODYNAMIC STABILITY OF PROTEINS (1)
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Elsevier (16)
Wiley (15)
ACS (6)
Springer (3)

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Search results for: Michael Assfalg

Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

Site‐Specific Ubiquitination of Tau Amyloids Promoted by the E3 Ligase CHIP

Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP

Structural Basis for Chaperone‐Independent Ubiquitination of Tau Protein by Its E3 Ligase CHIP

Semisynthetic and Enzyme‐Mediated Conjugate Preparations Illuminate the Ubiquitination‐Dependent Aggregation of Tau Protein

Semisynthetic and Enzyme‐Mediated Conjugate Preparations Illuminate the Ubiquitination‐Dependent Aggregation of Tau Protein

Specific Interaction Sites Determine Differential Adsorption of Protein Structural Isomers on Nanoparticle Surfaces

Alzheimer’s disease-associated ubiquitin mutant Ubb+1: Properties of the carboxy-terminal domain and its influence on biomolecular interactions

Molecular differences between human liver fatty acid binding protein and its T94A variant in their unbound and lipid-bound states

The long variant of human ileal bile acid-binding protein associated with colorectal cancer exhibits sub-cellular localization and lipid binding behaviour distinct from those of the common isoform

Unsaturated Long‐Chain Fatty Acids Are Preferred Ferritin Ligands That Enhance Iron Biomineralization

Identification of primary and secondary UBA footprints on the surface of ubiquitin in cell‐mimicking crowded solution

Effects of macromolecular crowding on a small lipid binding protein probed at the single-amino acid level

The study of transient protein–nanoparticle interactions by solution NMR spectroscopy

The unique ligand binding features of subfamily-II iLBPs with respect to bile salts and related drugs

Bile salt recognition by human liver fatty acid binding protein

The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins

Searching for protein binding sites from Molecular Dynamics simulations and paramagnetic fragment-based NMR studies

¹H, ¹⁵N and ¹³C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov.

NMR investigation of the equilibrium partitioning of a water‐soluble bile salt protein carrier to phospholipid vesicles

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