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Antonio Rossi

Researcher at University of Pavia

Publications -  115
Citations -  3414

Antonio Rossi is an academic researcher from University of Pavia. The author has contributed to research in topics: Type I collagen & Osteogenesis imperfecta. The author has an hindex of 34, co-authored 108 publications receiving 2985 citations.

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FGF signalling regulates bone growth through autophagy

TL;DR: It is shown that autophagy is induced in growth-plate chondrocytes during post-natal development and regulates the secretion of type II collagen (Col2), the major component of cartilage ECM, and is identified as a novel effector of FGF signalling in bone.
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Collagen Plays an Active Role in the Aggregation of β2-Microglobulin under Physiopathological Conditions of Dialysis-related Amyloidosis

TL;DR: Findings are consistent with the estimates resulting from a simplified collagen model whereby electrostatic effects can lead to high local concentrations of oppositely charged species, such as β2-m, that decay on moving away from the fiber surface.
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NANS-mediated synthesis of sialic acid is required for brain and skeletal development

TL;DR: It was found that Knockdown of nansa in zebrafish embryos resulted in abnormal skeletal development, and exogenously added sialic acid partially rescued the skeletal phenotype, and NANS-mediated synthesis of siala is required for early brain development and skeletal growth.
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A diastrophic dysplasia sulfate transporter (SLC26A2) mutant mouse: morphological and biochemical characterization of the resulting chondrodysplasia phenotype

TL;DR: A Dtdst knock-in mouse with a partial loss of function of the sulfate transporter was generated and homozygous mutant mice were characterized by growth retardation, skeletal dysplasia and joint contractures, thereby recapitulating essential aspects of the DTD phenotype in man.
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Heparin Strongly Enhances the Formation of β2-Microglobulin Amyloid Fibrils in the Presence of Type I Collagen

TL;DR: It is found that heparin promotes β2-m aggregation in solution at pH 6.4 and strongly accelerates amyloid deposition, and Morphology and structure of fibrils obtained in the presence of collagen andHeparin are highly similar to those of natural fibrILS.