Sapienza University of Rome

About: Sapienza University of Rome is a education organization based out in Rome, Lazio, Italy. It is known for research contribution in the topics: Population & Large Hadron Collider. The organization has 62002 authors who have published 155468 publications receiving 4397244 citations. The organization is also known as: La Sapienza & Università La Sapienza di Roma.

A Novel Concept for the Synthesis of an Improved LiFePO4 Lithium Battery Cathode

Abstract: This paper describes the synthesis and the properties of a kinetically improved cathode material. The novel aspect of the synthesis is based on a critical step involving the dispersion of metal (e.g., copper or silver) at a very low concentration (1 wt %). This metal addition does not affect the structure of the cathode but considerably improves its kinetics in terms of capacity delivery and cycle life. Such an enhancement of the electrochemical properties has been ascribed to a reduction of the particle size and to an increase of the bulk intra- and interparticle electronic conductivity of both effects being promoted by the finely dispersed metal powders. This improved conductivity favors the response of thus substantiating its interest as new cathode for advanced lithium ion batteries. © 2002 The Electrochemical Society. All rights reserved.

Autosomal recessive hypercholesterolemia caused by mutations in a putative LDL receptor adaptor protein.

Abstract: Atherogenic low density lipoproteins are cleared from the circulation by hepatic low density lipoprotein receptors (LDLR). Two inherited forms of hypercholesterolemia result from loss of LDLR activity: autosomal dominant familial hypercholesterolemia (FH), caused by mutations in the LDLR gene, and autosomal recessive hypercholesterolemia (ARH), of unknown etiology. Here we map the ARH locus to a ∼1-centimorgan interval on chromosome 1p35 and identify six mutations in a gene encoding a putative adaptor protein (ARH). ARH contains a phosphotyrosine binding (PTB) domain, which in other proteins binds NPXY motifs in the cytoplasmic tails of cell-surface receptors, including the LDLR. ARH appears to have a tissue-specific role in LDLR function, as it is required in liver but not in fibroblasts.