P
Peder Madsen
Researcher at Aarhus University
Publications - 122
Citations - 8950
Peder Madsen is an academic researcher from Aarhus University. The author has contributed to research in topics: Complementary DNA & Gel electrophoresis. The author has an hindex of 50, co-authored 117 publications receiving 8473 citations. Previous affiliations of Peder Madsen include Lundbeck & Aarhus University Hospital.
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Journal ArticleDOI
Sortilin is essential for proNGF-induced neuronal cell death
Anders Nykjaer,Ramee Lee,Kenneth K. Teng,Pernille Jansen,Pernille Jansen,Peder Madsen,Morten Nielsen,Christian Jacobsen,Marco Kliemannel,Elisabeth Schwarz,Thomas E. Willnow,Barbara L. Hempstead,Claus Munck Petersen +12 more
TL;DR: It is reported that proNGF creates a signalling complex by simultaneously binding to p 75NTR and sortilin, which acts as a co-receptor and molecular switch governing the p75NTR-mediated pro-apoptotic signal induced by proNGf.
Journal ArticleDOI
The sortilin cytoplasmic tail conveys Golgi–endosome transport and binds the VHS domain of the GGA2 sorting protein
Morten Nielsen,Peder Madsen,Erik Ilsø Christensen,Anders Nykjaer,Jørgen Gliemann,Dagmar Kasper,Regina Pohlmann,Claus Munck Petersen +7 more
TL;DR: Evidence is provided suggesting that sortilin is the first example of a mammalian receptor targeted by the recently described GGA family of cytosolic sorting proteins, which condition the Vps10p‐mediated sorting of yeast carboxypeptidase Y.
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Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography
Claus Munck Petersen,Morten Nielsen,Anders Nykjaer,Linda Jacobsen,Niels Tommerup,Hanne H. Rasmussen,Hans Røigaard,Jørgen Gliemann,Peder Madsen,Søren K. Moestrup +9 more
TL;DR: Exercise of a chimeric receptor containing the cytoplasmic tail of gp95/sortilin demonstrates evidence that the tail conveys colocalization with the cation-independent mannose6-phosphate receptor in endosomes and the Golgi compartment.
Journal ArticleDOI
Molecular cloning, occurrence, and expression of a novel partially secreted protein "psoriasin" that is highly up-regulated in psoriatic skin.
Peder Madsen,Hanne H. Rasmussen,Henrik Leffers,Bent Honoré,Kurt Dejgaard,Eydfinnur Olsen,Jette Kiil,Else Walbum,Annette H. Andersen,Bodil Basse,Jette B. Lauridsen,Gitte P. Ratz,Ariana Celis,Joël Vandekerckhove,Julio E. Celis +14 more
TL;DR: Psoriasin was not detected in normal human fibroblasts, lymphocytes, endothelial cells and transformed epithelial cells of keratinocyte origin, suggesting that its overexpression by psoriatic keratinocytes may be linked to the inflammatory stimuli.
Journal ArticleDOI
Molecular Cloning and Expression of a Novel Keratinocyte Protein (Psoriasis-associated fatty acid-binding protein [PA-FABP]) that Is Highly Up-Regulated in Psoriatic Skin and that Shares Similarity to Fatty Acid-Binding Proteins
TL;DR: 2D gel protein analysis of normal primary keratinocytes cultured for at least 8 d under conditions that promoted incomplete terminal differentiation revealed a strong up-regulation of PA-FABP, psoriasin, calgranulins A and B, and a few other proteins that are highly expressed in psoriatic skin.