Manuela Bozzi
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View article: Diagnosis, Pathogenesis and Treatment of Muscular Dystrophy
Diagnosis, Pathogenesis and Treatment of Muscular Dystrophy Open
Muscular dystrophies are a group of inherited genetic disorders that involve an ever-growing number of genes [...]
View article: Misregulation of the Ubiquitin–Proteasome System and Autophagy in Muscular Dystrophies Associated with the Dystrophin–Glycoprotein Complex
Misregulation of the Ubiquitin–Proteasome System and Autophagy in Muscular Dystrophies Associated with the Dystrophin–Glycoprotein Complex Open
The stability of the sarcolemma is severely impaired in a series of genetic neuromuscular diseases defined as muscular dystrophies. These are characterized by the centralization of skeletal muscle syncytial nuclei, the replacement of muscl…
View article: Live cell optical super-resolution microscopy of dystroglycan mutants as a model for dystroglycanopathies in multiple cell lines
Live cell optical super-resolution microscopy of dystroglycan mutants as a model for dystroglycanopathies in multiple cell lines Open
Introduction Dystroglycan (DG) is an adhesion complex comprising two subunits, α-DG and β-DG, which interact non-covalently at the plasma membrane. As a component of the dystrophin-glycoprotein complex DGC, DG plays a crucial role in linki…
View article: The missense mutation C667F in murine β-dystroglycan causes embryonic lethality, myopathy and blood-brain barrier destabilization
The missense mutation C667F in murine β-dystroglycan causes embryonic lethality, myopathy and blood-brain barrier destabilization Open
Dystroglycan (DG) is an extracellular matrix receptor consisting of an α- and a β-DG subunit encoded by the DAG1 gene. The homozygous mutation (c.2006G>T, p.Cys669Phe) in β-DG causes muscle-eye-brain disease with multicystic leukodystro…
View article: Corrigendum: From adhesion complex to signaling hub: the dual role of dystroglycan
Corrigendum: From adhesion complex to signaling hub: the dual role of dystroglycan Open
[This corrects the article DOI: 10.3389/fmolb.2023.1325284.].
View article: From adhesion complex to signaling hub: the dual role of dystroglycan
From adhesion complex to signaling hub: the dual role of dystroglycan Open
Dystroglycan (DG) is a transmembrane protein widely expressed in multiple cells and tissues. It is formed by two subunits, α− and β-DG, and represents a molecular bridge between the outside and the inside of the cell, which is essential fo…
View article: A missense mutation (C667F) in β-dystroglycan results in reduced dystroglycan protein levels leading to myopathy and destabilization of the blood-brain and blood-retinal barrier protein network
A missense mutation (C667F) in β-dystroglycan results in reduced dystroglycan protein levels leading to myopathy and destabilization of the blood-brain and blood-retinal barrier protein network Open
Dystroglycan (DG) is a glycoprotein and extracellular matrix receptor consisting of an α-DG and a β-DG subunit encoded by the gene DAG1 . A homozygous missense mutation (c.2006G>T), resulting in an amino acid substitution (p.Cys669Phe) in …
View article: Verbascoside Elicits Its Beneficial Effects by Enhancing Mitochondrial Spare Respiratory Capacity and the Nrf2/HO-1 Mediated Antioxidant System in a Murine Skeletal Muscle Cell Line
Verbascoside Elicits Its Beneficial Effects by Enhancing Mitochondrial Spare Respiratory Capacity and the Nrf2/HO-1 Mediated Antioxidant System in a Murine Skeletal Muscle Cell Line Open
Muscle weakness and muscle loss characterize many physio-pathological conditions, including sarcopenia and many forms of muscular dystrophy, which are often also associated with mitochondrial dysfunction. Verbascoside, a phenylethanoid gly…
View article: Molecular Mechanisms Underlying Muscle Wasting in Huntington’s Disease
Molecular Mechanisms Underlying Muscle Wasting in Huntington’s Disease Open
Huntington’s disease (HD) is an autosomal dominant neurodegenerative disorder caused by pathogenic expansions of the triplet cytosine-adenosine-guanosine (CAG) within the Huntingtin gene. These expansions lead to a prolongation of the poly…
View article: 3D Graphene Scaffolds for Skeletal Muscle Regeneration: Future Perspectives
3D Graphene Scaffolds for Skeletal Muscle Regeneration: Future Perspectives Open
Although skeletal muscle can regenerate after injury, in chronic damages or in traumatic injuries its endogenous self-regeneration is impaired. Consequently, tissue engineering approaches are promising tools for improving skeletal muscle c…
View article: Identification and Modeling of a GT-A Fold in the α-Dystroglycan Glycosylating Enzyme LARGE1
Identification and Modeling of a GT-A Fold in the α-Dystroglycan Glycosylating Enzyme LARGE1 Open
The acetylglucosaminyltransferase-like protein LARGE1 is an enzyme that is responsible for the final steps of the post-translational modifications of dystroglycan (DG), a membrane receptor that links the cytoskeleton with the extracellular…
View article: The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site
The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site Open
Dystroglycan (DG) is a membrane receptor, belonging to the dystrophin-glycoprotein complex (DGC) and formed by two subunits, α-dystroglycan (α-DG) and β-dystroglycan (β -DG). The C-terminal domain of α-DG and the N-terminal extracellular d…
View article: Cover Image, Volume 39, Issue 2
Cover Image, Volume 39, Issue 2 Open
On the cover: This cover image, by Giulia Signorino et al., is based on the Research Article A dystroglycan mutation (p.Cys667Phe) associated to muscle-eye-brain disease with multicystic leucodystrophy results in ER-retention of the mutant…
View article: A dystroglycan mutation (p.Cys667Phe) associated to muscle-eye-brain disease with multicystic leucodystrophy results in ER-retention of the mutant protein
A dystroglycan mutation (p.Cys667Phe) associated to muscle-eye-brain disease with multicystic leucodystrophy results in ER-retention of the mutant protein Open
Dystroglycan (DG) is a cell adhesion complex composed by two subunits, the highly glycosylated α-DG and the transmembrane β-DG. In skeletal muscle, DG is involved in dystroglycanopathies, a group of heterogeneous muscular dystrophies chara…
View article: The effect of the pathological V72I, D109N and T190M missense mutations on the molecular structure of α-dystroglycan
The effect of the pathological V72I, D109N and T190M missense mutations on the molecular structure of α-dystroglycan Open
Dystroglycan (DG) is a highly glycosylated protein complex that links the cytoskeleton with the extracellular matrix, mediating fundamental physiological functions such as mechanical stability of tissues, matrix organization and cell polar…
View article: Structural flexibility of human α‐dystroglycan
Structural flexibility of human α‐dystroglycan Open
Dystroglycan ( DG ), composed of α and β subunits, belongs to the dystrophin‐associated glycoprotein complex. α‐ DG is an extracellular matrix protein that undergoes a complex post‐translational glycosylation process. The bifunctional glyc…
View article: X-ray diffraction: data collection and model refinement statistics.
X-ray diffraction: data collection and model refinement statistics. Open
a Values in parenthesis are given for the highest resolution shellb Rmerge = ∑hkl∑j│Ihkl, j-hkl>│/ ∑hkl∑j Ihkl, jc Rwork = ∑work-set│Fobs-Fcal│/ ∑work-set Fobsd Rfree = ∑test-set |Fobs-Fcal|/ ∑test-set FobsX-ray diffraction: data collectio…
View article: Relative stabilities of WT and T190M.
Relative stabilities of WT and T190M. Open
A. Equilibrium unfolding curves of WT and T190M. The red-shifts in the fluorescence peaks upon addition of GdnHCl indicate a progressive exposure of the tryptophan residues to the solvent: the data fit to a single cooperative transition fo…
View article: Superimposition of the WT and T190M mutant S6 domains.
Superimposition of the WT and T190M mutant S6 domains. Open
The models are represented as ribbons, with WT colored in pink-salmon and T190M colored in blue; Met 190 is highlighted in green and depicted as a ball-and-stick model. The “flexible loop” C-term residues Gln163 (T190M) and Asn160 (WT and …
View article: Cartoon depiction of the T190M crystal structure.
Cartoon depiction of the T190M crystal structure. Open
The two domains are colored in violet (Ig-like domain) and green (small ribosomal S6 subunit domain), respectively; the B1 and B5 β-strands are labeled for clarity. Spheres representation is employed for highlighting Met190. The loop regio…
View article: 3D Structured Illumination Microscopy images of U2OS cells expressing DG and DG<sup>T190M</sup> fused to EGFP.
3D Structured Illumination Microscopy images of U2OS cells expressing DG and DG<sup>T190M</sup> fused to EGFP. Open
DG-EGFP (A) and DGT190M-EGFP (B) are both localized specifically at the plasma membrane and accumulate in the cytoplasm. The columns show the individual images for DAPI (blue), EGFP (green), Cellmask Plasma Membrane Orange (red) and the re…
View article: Calculated σ<sub>A</sub>-weighted 2F<sub>o</sub>-F<sub>c</sub> map (contoured at 1.0 σ and colored in light-blue) and F<sub>o</sub>-F<sub>c</sub> map (contoured at ± 3.0 σ and colored in green for positive values and in orange for negative values).
Calculated σ<sub>A</sub>-weighted 2F<sub>o</sub>-F<sub>c</sub> map (contoured at 1.0 σ and colored in light-blue) and F<sub>o</sub>-F<sub>c</sub> map (contoured at ± 3.0 σ and colored in green for positive values and in orange for negative values). Open
The maps have been calculated following the Patterson search stage using the WT as a model (PDB id: 1U2C). The final model of T190M (colored in blue) is superposed to the initial Patterson search solution (colored in pink-salmon). Both mod…
View article: Details of the hydrogen bond networks involving selected water molecules and residues.
Details of the hydrogen bond networks involving selected water molecules and residues. Open
The structural elements of the N-terminal domain of α-DG are represented as ribbon; residues involved in the interaction networks are represented as sticks. Interatomic distances are reported in Å. The color scheme for WT and T190M models …
View article: SA-omit σ<sub>A</sub>-weighted 2F<sub>o</sub>-F<sub>c</sub> map (contoured at 1.0 σ and colored in grey) and F<sub>o</sub>-F<sub>c</sub> map (contoured at 3.0 σ and colored in green) overlaid with the loop region encompassing residues (156–163) as the T190M final model (PDB id 4WIQ).
SA-omit σ<sub>A</sub>-weighted 2F<sub>o</sub>-F<sub>c</sub> map (contoured at 1.0 σ and colored in grey) and F<sub>o</sub>-F<sub>c</sub> map (contoured at 3.0 σ and colored in green) overlaid with the loop region encompassing residues (156–163) as the T190M final model (PDB id 4WIQ). Open
Maps have been calculated using the T190M model, where residues (156–163) have been omitted from the calculation. The loop of the T190M final model nicely fits the 2Fo-Fc maps, which is indicative of the soundness of the built model.
View article: Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution
Proteasome Activity Is Affected by Fluctuations in Insulin-Degrading Enzyme Distribution Open
Insulin-Degrading-Enzyme (IDE) is a Zn2+-dependent peptidase highly conserved throughout evolution and ubiquitously distributed in mammalian tissues wherein it displays a prevalent cytosolic localization. We have recently demonstrated a no…