J
J J Cassiman
Researcher at Katholieke Universiteit Leuven
Publications - 66
Citations - 4340
J J Cassiman is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Chromosomal translocation & Proteoglycan. The author has an hindex of 35, co-authored 66 publications receiving 4219 citations.
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Journal ArticleDOI
Consensus on the use and interpretation of cystic fibrosis mutation analysis in clinical practice
Carlo Castellani,Harry Cuppens,Milan Macek,J J Cassiman,Eitan Kerem,Peter R. Durie,Elizabeth Tullis,B.M. Assael,Cristina Bombieri,A. Brown,Teresa Casals,Mireille Claustres,Garry R. Cutting,Els Dequeker,John A Dodge,Iolo Doull,Philip M. Farrell,Claude Férec,E. Girodon,M. Johannesson,Batsheva Kerem,Michael R. Knowles,Anne Munck,Pier Franco Pignatti,Dragica Radojkovic,Paolo Rizzotti,Martin Schwarz,Manfred Stuhrmann,Maria Tzetis,Julian Zielenski,Joseph Elborn +30 more
TL;DR: The conclusions of a consensus conference to address the use and interpretation of CF mutation analysis in clinical settings are described, including the use of CFTR genotype for prediction of prognosis in people with CF at the time of their diagnosis is not recommended.
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Developmental changes in heparan sulfate expression: in situ detection with mAbs.
TL;DR: The results suggest that heparan sulfate abounds at sites of active morphogenesis and that the expression of this glycosaminoglycan is developmentally regulated.
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Cell surface heparan sulfate proteoglycans from human vascular endothelial cells. Core protein characterization and antithrombin III binding properties.
TL;DR: The results imply that glypican may specifically contribute to the antithrombotic properties of the vascular wall.
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Demonstration of an alpha2-macroglobulin receptor in human fibroblasts, absent in tumor-derived cell lines.
TL;DR: Evidence is provided that two tumor-derived cell lines, which were previously shown to have a low intracellular a2M content under steady state culture conditions, are devoid of the specific azM binding site at their plasma membrane.
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Molecular cloning of amphiglycan, a novel integral membrane heparan sulfate proteoglycan expressed by epithelial and fibroblastic cells.
TL;DR: An antisense oligonucleotide primer is synthesized that matches a supposedly conserved sequence in messages for heparan sulfate proteoglycans with transmembrane orientations and is proposed to name this proteoglycan "amphiglycan" referring to its domain structure which extends on both sides of the plasmamembrane, and to its localization around cells of both epithelial and fibroblastic origin.