L'AZIONE DI DISCONOSCIMENTO DELLA PATERNITÀ ALLA LUCE DELLA RIFORMA DELLA FILIAZIONE.

La presente trattazione, partendo da un’analisi su come siano cambiati in seguito alla recente riforma della filiazione: il concetto di famiglia, la responsabilità genitoriale, la filiazione all’interno del matrimonio e al di fuori, con la finalità di una loro equiparazione, si occupa di inquadrare gli effetti di tale normativa nell’ambito dell’azione di disconoscimento della paternità. Le novità introdotte per effetto del l. 219/2012 e del d.lgs. 154/2013, in tale ambito, sono state analizzate raffrontandole a quella che è stata l’evoluzione della disciplina a partire dal codice civile del 1942, le sue modifiche ad opera della riforma del diritto di famiglia e degli interventi giurisprudenziali in materia. Proseguendo sono stati esaminati alcuni aspetti pratici e attuali dell’azione di disconoscimento: •la sua sostanziale omogeneità con il riconoscimento per difetto di veridicità, sottolineando le diverse finalità dei due istituti che giustificano il persistere di alcune differenze; •la possibilità di esercizio dell’azione in seguito all’utilizzo di tecniche di procreazione medicalmente assistita, illustrando la posizione della giurisprudenza e della dottrina prima della l. 40/2004, e la sua regolamentazione successivamente alla sua introduzione; •il riconoscimento del diritto all’ascolto del minore nei procedimenti che lo riguardano e in particolare nel giudizio di disconoscimento, questo diritto è stato riconosciuto da molti anni dalle convenzioni internazionali, ma solo di recente è stato introdotto nel nostro ordinamento. L’esercizio di tale azione è stato comparato poi alla disciplina degli altri stati europei. Nel capitolo finale sono state compiute alcune osservazioni circa i punti critici della normativa della filiazione e gli interventi auspicabili

Functional analysis of dsRNAs (L1, L3, L5, and M2) associated with isometric 34-nm virions of Agaricus bisporus (white button mushroom)

cDNA clones of dsRNAs associated with La France disease of Agaricus bisporus were isolated, Clones corresponding to L1 and L5 dsRNAs were sequenced. The deduced amino acid sequence of L1 dsRNA (1078 amino acids, M(r) 121K) showed significant homology with RNA-dependent RNA polymerases of other dsRNA viruses. The deduced amino acid sequence of L5 dsRNA (724 amino acids, M(r) 82K) showed no homology with known proteins. Amino acid sequences of tryptic digests of three virion-associated proteins were determined. The 34-nm virion-associated protein of M(r) 115K was encoded by the L1 dsRNA, thus identifying this protein as the RNA-dependent RNA polymerase. The virion-associated protein of M(r) 90K was encoded by the previously sequenced L3 dsRNA. A cDNA clone of the previously sequenced M2 dsRNA was expressed in Escherichia coli and antibodies raised against this protein reacted only with a protein present in the cytoplasm of diseased A. bisporus fruit bodies but not in the 34-nm virions. (C) 1996 Academic Press, Inc

The Assembly of Individual Chaplin Peptides from Streptomyces coelicolor into Functional Amyloid Fibrils

The self-association of proteins into amyloid fibrils offers an alternative to the natively folded state of many polypeptides. Although commonly associated with disease, amyloid fibrils represent the natural functional state of some proteins, such as the chaplins from the soil-dwelling bacterium Streptomyces coelicolor, which coat the aerial mycelium and spores rendering them hydrophobic. We have undertaken a biophysical characterisation of the five short chaplin peptides ChpD-H to probe the mechanism by which these peptides self-assemble in solution to form fibrils. Each of the five chaplin peptides produced synthetically or isolated from the cell wall is individually surface-active and capable of forming fibrils under a range of solution conditions in vitro. These fibrils contain a highly similar cross-β core structure and a secondary structure that resembles fibrils formed in vivo on the spore and mycelium surface. They can also restore the growth of aerial hyphae to a chaplin mutant strain. We show that cysteine residues are not required for fibril formation in vitro and propose a role for the cysteine residues conserved in four of the five short chaplin peptides

Diffusion of hydrophobin proteins in solution and interactions with a graphite surface

<p>Abstract</p> <p>Background</p> <p>Hydrophobins are small proteins produced by filamentous fungi that have a variety of biological functions including coating of spores and surface adhesion. To accomplish these functions, they rely on unique interface-binding properties. Using atomic-detail implicit solvent rigid-body Brownian dynamics simulations, we studied the diffusion of HFBI, a class II hydrophobin from <it>Trichoderma reesei</it>, in aqueous solution in the presence and absence of a graphite surface.</p> <p>Results</p> <p>In the simulations, HFBI exists in solution as a mixture of monomers in equilibrium with different types of oligomers. The oligomerization state depends on the conformation of HFBI. When a Highly Ordered Pyrolytic Graphite (HOPG) layer is present in the simulated system, HFBI tends to interact with the HOPG layer through a hydrophobic patch on the protein.</p> <p>Conclusions</p> <p>From the simulations of HFBI solutions, we identify a tetrameric encounter complex stabilized by non-polar interactions between the aliphatic residues in the hydrophobic patch on HFBI. After the formation of the encounter complex, a local structural rearrangement at the protein interfaces is required to obtain the tetrameric arrangement seen in HFBI crystals. Simulations performed with the graphite surface show that, due to a combination of a geometric hindrance and the interaction of the aliphatic sidechains with the graphite layer, HFBI proteins tend to accumulate close to the hydrophobic surface.</p

Amyloids - A functional coat for microorganisms

Amyloids are filamentous protein structures ~10 nm wide and 0.1–10 µm long that share a structural motif, the cross-β structure. These fibrils are usually associated with degenerative diseases in mammals. However, recent research has shown that these proteins are also expressed on bacterial and fungal cell surfaces. Microbial amyloids are important in mediating mechanical invasion of abiotic and biotic substrates. In animal hosts, evidence indicates that these protein structures also contribute to colonization by activating host proteases that are involved in haemostasis, inflammation and remodelling of the extracellular matrix. Activation of proteases by amyloids is also implicated in modulating blood coagulation, resulting in potentially life-threatening complications.