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Richard E. Pagano
Researcher at Mayo Clinic
Publications - 136
Citations - 16170
Richard E. Pagano is an academic researcher from Mayo Clinic. The author has contributed to research in topics: Golgi apparatus & Endocytosis. The author has an hindex of 69, co-authored 136 publications receiving 15583 citations. Previous affiliations of Richard E. Pagano include University of Rochester & Carnegie Institution for Science.
Papers
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Journal ArticleDOI
Pathways of clathrin-independent endocytosis.
Satyajit Mayor,Richard E. Pagano +1 more
TL;DR: The current understanding of various clathrin-independent mechanisms of endocytosis are reviewed and a classification scheme is proposed to help organize the data in this complex and evolving field.
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Use of resonance energy-transfer to monitor membrane-fusion
TL;DR: An assay for vesicle--vesicle fusion involving resonance energy transfer between N-(7-nitro-2,1,3-benzoxadiazol-4-yl), the energy donor, and rhodamine, the energy acceptor has been developed.
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A novel fluorescent ceramide analogue for studying membrane traffic in animal cells: accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor.
TL;DR: A series of ceramide analogues bearing the fluorophore boron dipyrromethene difluoride (BODIPY) were synthesized and evaluated as vital stains for the Golgi apparatus, and as tools for studying lipid traffic between the GolGi apparatus and the plasma membrane of living cells.
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Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
Matthew Kirkham,Akikazu Fujita,Rahul Chadda,Susan J. Nixon,Teymuras V. Kurzchalia,Deepak Sharma,Richard E. Pagano,John F. Hancock,Satyajit Mayor,Robert G. Parton +9 more
TL;DR: Using quantitative light microscopy and a modified immunoelectron microscopic technique, the entry pathway of the cholera toxin binding subunit (CTB) in primary embryonic fibroblasts is characterized and the major carriers involved in initial entry of CTB were identified as uncoated tubular or ring-shaped structures.
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Rab proteins mediate Golgi transport of caveola-internalized glycosphingolipids and correct lipid trafficking in Niemann-Pick C cells
Amit Choudhury,Michel Dominguez,Vishwajeet Puri,Deepak Sharma,Keishi Narita,Christine L. Wheatley,David L. Marks,Richard E. Pagano +7 more
TL;DR: A role for Rab7 and Rab9 in the Golgi targeting of glycosphingolipids is demonstrated and a new therapeutic approach for restoring normal lipid trafficking in NP-C cells is suggested.