U
Ulla M. Wewer
Researcher at University of Copenhagen
Publications - 121
Citations - 11497
Ulla M. Wewer is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Laminin & Integrin. The author has an hindex of 59, co-authored 121 publications receiving 11051 citations. Previous affiliations of Ulla M. Wewer include Tokyo University of Pharmacy and Life Sciences & Statens Serum Institut.
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Journal ArticleDOI
A simplified laminin nomenclature
Monique Aumailley,Leena Bruckner-Tuderman,William G. Carter,Rainer Deutzmann,David Edgar,Peter Ekblom,Jürgen Engel,Eva Engvall,Erhard Hohenester,Jonathan C.R. Jones,Hynda K. Kleinman,M. Peter Marinkovich,George R. Martin,Ulrike Mayer,Guerrino Meneguzzi,Jeffrey H. Miner,Kaoru Miyazaki,Manuel Patarroyo,Mats Paulsson,Vito Quaranta,Joshua R. Sanes,Takako Sasaki,Kiyotoshi Sekiguchi,Lydia Sorokin,Jan F. Talts,Jan F. Talts,Karl Tryggvason,Jouni Uitto,Ismo Virtanen,Klaus von der Mark,Ulla M. Wewer,Yoshihiko Yamada,Peter D. Yurchenco +32 more
TL;DR: A new identification system for a trimer using three Arabic numerals, based on the alpha, beta and gamma chain numbers is introduced, which is introduced for laminin trimers.
Journal ArticleDOI
A Family of Insulin-Like Growth Factor II mRNA-Binding Proteins Represses Translation in Late Development
Jacob Nielsen,Jan Christiansen,Jens Lykke-Andersen,Anders H. Johnsen,Ulla M. Wewer,Finn Cilius Nielsen +5 more
TL;DR: The results imply that cytoplasmic 5′ UTR-binding proteins control IGF-II biosynthesis during late mammalian development.
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Murine muscular dystrophy caused by a mutation in the laminin alpha 2 (Lama2) gene.
TL;DR: The classic murine muscular dystrophy strain, dy, was first described almost 40 years ago and the molecular basis of an allele of dy, called dy 2J, is identified by detecting a mutation in the laminin α2 chain gene — the first identified mutation in lamin in-2.
Journal ArticleDOI
A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo
Brent Gilpin,Frosty Loechel,Marie-Geneviève Mattei,Eva Engvall,Reidar Albrechtsen,Ulla M. Wewer +5 more
TL;DR: A novel, secreted form of human ADAM 12 (meltrin α), designatedADAM 12-S (S for short), and a larger, membrane-bound form designated ADam 12-L (L for long form) are described, which have potential applications in the development of muscle-directed gene and cell therapies.
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ADAM 12-S cleaves IGFBP-3 and IGFBP-5 and is inhibited by TIMP-3.
TL;DR: The purification of full-length recombinant ADAM 12-S is described and it is demonstrated that it cleaves insulin-like growth factor binding protein-3 (IGFBP-3) and this result supports a role for ADAM 11-S in the degradation of IGF BP-3 in the blood of pregnant women.