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Ferruccio Galbiati

Researcher at Albert Einstein College of Medicine

Publications -  34
Citations -  6027

Ferruccio Galbiati is an academic researcher from Albert Einstein College of Medicine. The author has contributed to research in topics: Caveolae & Caveolin. The author has an hindex of 30, co-authored 33 publications receiving 5847 citations. Previous affiliations of Ferruccio Galbiati include University of Milan & Yeshiva University.

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Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy.

TL;DR: Eight patients from two different families are described with a new form of autosomal dominant LGMD, which is proposed to call LGMD1C, associated with a severe deficiency of caveolin-3 in muscle fibres, and two mutations in the gene are identified that may interfere with caveolae formation at the muscle cell plasma membrane.
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Cell-type and Tissue-specific Expression of Caveolin-2 CAVEOLINS 1 AND 2 CO-LOCALIZE AND FORM A STABLE HETERO-OLIGOMERIC COMPLEX IN VIVO

TL;DR: A novel mono-specific monoclonal antibody probe is generated that recognizes only caveolin-2, but not caveolins-1 and -3, and results suggest that expression levels of caveolin 1, 2, and 3 can be independently up-regulated or down-regulated in response to a variety of distinct cellular cues.
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Targeted downregulation of caveolin‐1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade

TL;DR: Stable NIH 3T3 cells harboring antisense caveolin‐1 exhibit anchorage‐independent growth, form tumors in immunodeficient mice and show hyperactivation of the p42/44 MAP kinase cascade.
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Caveolin-3 Null Mice Show a Loss of Caveolae, Changes in the Microdomain Distribution of the Dystrophin-Glycoprotein Complex, and T-tubule Abnormalities

TL;DR: Analysis of skeletal muscle tissue from these caveolin-3 null mice reveals mild myopathic changes; an exclusion of the dystrophin-glycoprotein complex from lipid raft domains; and abnormalities in the organization of the T- Tubule system, with dilated and longitudinally oriented T-tubules.
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Constitutive and growth factor-regulated phosphorylation of caveolin-1 occurs at the same site (Tyr-14) in vivo: identification of a c-Src/Cav-1/Grb7 signaling cassette.

TL;DR: In this article, a monoclonal antibody (mAb) probe that recognizes only tyrosine 14-phosphorylated caveolin-1 was generated and shown to be the principal site for recognition by c-Src kinase; however, little is known about this phosphorylation event.