603 research outputs found
La donna e la tradizione cattolica, motore della ricerca epistemologica di Federico Fellini sul Gran Teatro del Mondo
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Organizational Change and Leadership: A Bibliometric Analysis
No full textIn this article, we present the main results concerning the bibliometric analysis we developed for exploring the relationship between leadership and organizational change. Today, change is a constant in organizations, and leadership is one of the main factors affecting its outcome. The main objective of this work is to provide a complete overview of the studies discussing the two chosen intertwined topics, that could represent a valid starting point for developing future research directions. The bibliometric analysis was carried out on 359 articles published in journals belonging to the AJG ranking. We carried out the descriptive analysis of the dataset as well as the thematic analysis. For the latter, beyond the Authors’ keywords distribution and co-occurrence analysis, we developed the thematic evolution, considering three specific phases in the publication trend, specifically 1974–2004, 2005–2014, and 2015–2023. We provide a description of the main themes debated in each phase as well as the most contributing papers
Effects of C282Y mutation in HFE protein structure and interactions, investigated by MD simulations: implication in hereditary hemochromatosis
No full textHereditary hemochromatosis (HH) is an autosomal recessive disease characterized by an improper regulation of iron uptake, leading to an iron overload in different specific organs. The responsible of HH is a mutated protein called HFE, formed by two domains: the 1,2 MHC-like domain and the 3 immunoglobulin-like domain.1 Wilde type HFE competes with iron-loaded transferrin (Tf) for binding to the transferrin receptor (TfR) at the cell surface. HFE interferes with Tf binding site on TfR and regulates iron absorption. The mutated protein is not able to bind TfR and the regulation fails, causing the iron overload.2 The predominant mutation in HH is the C282Y (C260Y in the mature protein) in the 3 domain, which converts a cysteine residue in a tyrosine, breaking a disulphide bond and affecting the association of HFE with a 2-microglobulin (2m) chain, preventing its externalization at the cell surface and its binding with TfR.3
In this work, we investigated the effects of C282Y (C260Y in the mature protein) mutation on the HFE structure and on its interaction with the 2m domain, by means of molecular dynamics simulation technique. We followed the evolution of the HFE-2m complex in the wt and mutated form, accelerating the structural changes by means of a temperature increment.
The mutated tyrosine comes to be in a hydrophobic environment and tries to move towards a more polar one enlarging the barrel, helped in this by the broken disulphide bond. PCA analysis allows to investigate how the reciprocal interactions of 3, 2m and MHC domains are affected by these conformational changes. Many conserved contacts are lost, but the main effect is the exposition of Trp60 residue of 2m, known to be fundamental for the association of 2m with the HFE chain
La pratica documentaristica di Pier Paolo Pasolini, tra impegno civile ed esplorazione antropologica
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