J
John Wagner
Researcher at McGill University
Publications - 32
Citations - 2005
John Wagner is an academic researcher from McGill University. The author has contributed to research in topics: Protein tyrosine phosphatase & Hepcidin. The author has an hindex of 24, co-authored 32 publications receiving 1894 citations. Previous affiliations of John Wagner include National Research Council & Massachusetts Institute of Technology.
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Journal ArticleDOI
Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice
Kong E. You-Ten,Eric S. Muise,Annick Itié,Eva Michaliszyn,John Wagner,Serge Jothy,Wayne S. Lapp,Michel L. Tremblay +7 more
TL;DR: It is demonstrated that hematopoietic failure in TC-PTP −/− animals was not due to a stem cell defect, but rather to a stromal cell deficiency.
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The Architecture of the Multisubunit Trapp I Complex Suggests a Model for Vesicle Tethering.
Yeon-Gil Kim,Stefan Raunser,Christine Munger,John Wagner,Young-Lan Song,Miroslaw Cygler,Thomas Walz,Byung-Ha Oh,Michael Sacher +8 more
TL;DR: This study provides the most comprehensive view of a multisubunit vesicle tethering complex to date, based on which a model for the function of this complex, involving Rab1-GTP and long, coiled-coil tethers, is presented.
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Neuroendocrine dysplasia in mice lacking protein tyrosine phosphatase sigma.
Mounib Elchebly,John Wagner,Timothy E. Kennedy,Christian Lanctôt,Eva Michaliszyn,Annick Itié,Jacques Drouin,Michel L. Tremblay +7 more
TL;DR: Results suggest that tyrosine phosphorylation-dependent signalling pathways regulated by PTP-σ influence the proliferation and/or adhesiveness of various cell types in the developing hypothalamo-pituitary axis.
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The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1----6)-beta-D-glucan synthesis and normal cell growth.
TL;DR: Results indicate a role for (1----6)-beta-D-glucan in normal cell growth and suggest a model for sequential assembly of (1 ----6)- beta- D-glucaan in the yeast secretory pathway.
Journal ArticleDOI
Bacterial polysaccharide co-polymerases share a common framework for control of polymer length.
Ante Tocilj,Christine Munger,A. Proteau,Renato Morona,Leanne Purins,Eunice Ajamian,John Wagner,Magdalene Papadopoulos,Luisa Van Den Bosch,John L. Rubinstein,James Féthière,Allan Matte,Miroslaw Cygler,Miroslaw Cygler +13 more
TL;DR: Crystal structures of the periplasmic domains of three PCPs that impart substantially different chain length distributions to surface polysaccharides are reported, suggesting that the top of the PCP oligomers is an important region for determiningpolysaccharide modal length.