H
Hassan Y. Naim
Researcher at University of Veterinary Medicine Vienna
Publications - 194
Citations - 6508
Hassan Y. Naim is an academic researcher from University of Veterinary Medicine Vienna. The author has contributed to research in topics: Endoplasmic reticulum & Apical membrane. The author has an hindex of 41, co-authored 184 publications receiving 5486 citations. Previous affiliations of Hassan Y. Naim include Hannover Medical School & University of Veterinary Medicine Hanover.
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Journal ArticleDOI
Deglycosylation by small intestinal epithelial cell beta-glucosidases is a critical step in the absorption and metabolism of dietary flavonoid glycosides in humans.
Kitti Németh,Geoff W. Plumb,Jean-Guy Berrin,Nathalie Juge,Ralf Jacob,Hassan Y. Naim,Gary Williamson,Dallas M. Swallow,Paul A. Kroon +8 more
TL;DR: The absorption of dietary flavonoid glycosides in humans involves a critical deglycosylation step that is mediated by epithelial β-glucosidases (LPH andCBG), indicating a role of human LPH and CBG from small intestine in flavonoids absorption and metabolism.
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The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
TL;DR: This manuscript will review the general structure, regulation and function of HSP90 family and their potential role in pathophysiology.
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Requirement for galectin-3 in apical protein sorting
Delphine Delacour,Catharina I. Cramm-Behrens,Hervé Drobecq,André Le Bivic,Hassan Y. Naim,Ralf Jacob +5 more
TL;DR: The identification of the lectin galectin-3 delivering non-raft-dependent glycoproteins in the lumen of LAVs in a carbohydrate-dependent manner suggests a direct role of galectIn-3 in apical sorting as a sorting receptor.
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Structural Basis for Substrate Selectivity in Human Maltase-Glucoamylase and Sucrase-Isomaltase N-terminal Domains
Lyann Sim,Carly Willemsma,Sankar Mohan,Hassan Y. Naim,B. Mario Pinto,David R. Rose,David R. Rose +6 more
TL;DR: Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for α-1,6 substrates.
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Analysis of ACE2 in polarized epithelial cells: surface expression and function as receptor for severe acute respiratory syndrome-associated coronavirus.
Xiaofeng Ren,Jörg Glende,Marwan Alfalah,Victor de Vries,Christel Schwegmann-Wessels,Xiuxia Qu,Lei Tan,Thomas Tschernig,Hongkui Deng,Hassan Y. Naim,Georg Herrler +10 more
TL;DR: In a histological analysis of the respiratory tract, ACE2 was detected in the trachea, main bronchus and alveoli, and occasionally also in the small bronchi, which will help to understand the pathogenesis of SARS-CoV infection.