J
Jan T. Rasmussen
Researcher at Aarhus University
Publications - 62
Citations - 2848
Jan T. Rasmussen is an academic researcher from Aarhus University. The author has contributed to research in topics: Lactadherin & Peptide sequence. The author has an hindex of 28, co-authored 61 publications receiving 2563 citations.
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Journal ArticleDOI
Functional analyses of two cellular binding domains of bovine lactadherin.
Mikkel Holmen Andersen,Helle Graversen,Sergey N. Fedosov,Torben E. Petersen,Jan T. Rasmussen +4 more
TL;DR: Results show that lactadherin can act as link between two surfaces by binding to integrin receptors through its N-terminus and to phospholipids through its C- terminus, and mediation between artificial phosphatidyl serine membranes and MCF-7 cells.
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Inhibitory effects of human and bovine milk constituents on rotavirus infections.
A.S. Kvistgaard,Lone Tjener Pallesen,Carlos F. Arias,Susana López,Torben E. Petersen,Christian W. Heegaard,Jan T. Rasmussen +6 more
TL;DR: It is shown that human, and not bovine, lactadherin inhibits Wa rotavirus infection in vitro, and a bovina macromolecular whey protein fraction turned out to have an efficient and versatile inhibitory activity against rotav virus.
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Lactadherin binds selectively to membranes containing phosphatidyl-L-serine and increased curvature.
TL;DR: The membrane-binding properties that correlate to the anticoagulant capacity are characterized and lactadherin resembles factor VIII and V with stereoselective preference for phosphatidyl-L-serine and preference for highly curved membranes.
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Characterization of glycoprotein PAS-6/7 from membranes of bovine milk fat globules.
TL;DR: Results obtained by amino acid analyses, amino-acid-sequence analyses, carbohydrate-composition determinations, and MS analyses of glycopeptides revealed that both proteins were glycosylated with a carbohydrate structure that contained galactose, N-acetylgalactosamine and fucose.
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Isolation and characterization of MUC15, a novel cell membrane‐associated mucin
TL;DR: The deduced amino-acid sequences of human and bovine MUC15 demonstrated structural hallmarks characteristic for other membrane-bound mucins, such as a serine, threonine, and proline-rich extracellular region with several potential glycosylation sites, a putative transmembrane domain, and a short cytoplasmic C-terminal.