Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Juliette Janson"'
Publikováno v:
Molecular Genetics and Metabolism Reports, Vol 22, Iss , Pp - (2020)
Mucopolysaccharidosis III A (MPS IIIA) is an autosomal recessive lysosomal storage disorder caused by deficiency of the enzyme sulfamidase. The disorder results in accumulation of heparan sulfate, lysosomal enlargement and cellular and organ dysfunct
Externí odkaz:
https://doaj.org/article/9d2af5b0e9cc4632917c973c163332fd
Autor:
Susanne Gustavsson, Elisabet Ohlin Sjöström, Agneta Tjernberg, Juliette Janson, Ulrica Westermark, Tommy Andersson, Åsa Makower, Erik Arnelöf, Gudrun Andersson, Jan Svartengren, Carina Ekholm, Stefan Svensson Gelius
Publikováno v:
Molecular Genetics and Metabolism Reports, Vol 21, Iss , Pp - (2019)
Mucopolysaccharidosis type IIIA (MPS IIIA) is a lysosomal storage disorder (LSD) characterized by severe central nervous system (CNS) degeneration. The disease is caused by mutations in the SGSH gene coding for the lysosomal enzyme sulfamidase. Sulfa
Externí odkaz:
https://doaj.org/article/5c5925a40eaf4e558c81d318fcb0dd0e
Autor:
Jenny U Johansson, Jesper Ericsson, Juliette Janson, Simret Beraki, Davor Stanić, Slavena A Mandic, Martin A Wikström, Tomas Hökfelt, Sven Ove Ogren, Björn Rozell, Per-Olof Berggren, Christina Bark
Publikováno v:
PLoS Genetics, Vol 4, Iss 11, p e1000278 (2008)
Alternative splicing is an evolutionary innovation to create functionally diverse proteins from a limited number of genes. SNAP-25 plays a central role in neuroexocytosis by bridging synaptic vesicles to the plasma membrane during regulated exocytosi
Externí odkaz:
https://doaj.org/article/2c86a0d4010148f5a31eb107bae68898
Autor:
Åsa Makower, Susanne Gustavsson, Agneta Tjernberg, Stefan Svensson Gelius, Tommy Andersson, Juliette Janson, Erik Arnelöf, Per-Olof Edlund
Publikováno v:
Bioanalysis. 11:1389-1403
Aim: Accumulation of heparan sulfate (HS) is associated with the neurodegenerative disorder Mucopolysaccharidosis type IIIA (MPS IIIA). Here, we compare HS levels in brain and cerebrospinal fluid (CSF) of MPS IIIA mice after treatment with a chemical
Publikováno v:
Molecular Genetics and Metabolism Reports, Vol 22, Iss, Pp-(2020)
Molecular Genetics and Metabolism Reports
Molecular Genetics and Metabolism Reports
Mucopolysaccharidosis III A (MPS IIIA) is an autosomal recessive lysosomal storage disorder caused by deficiency of the enzyme sulfamidase. The disorder results in accumulation of heparan sulfate, lysosomal enlargement and cellular and organ dysfunct
Autor:
Karin Kaspersson, Juliette Janson, Johanna Fälting, Gvido Cebers, Samantha Budd Haeberlein, Fredrik Jeppsson, Susanna Eketjäll, Alan R. Kugler, Anna Bogstedt, Robert C. Alexander
Publikováno v:
Journal of Alzheimer's Disease
A growing body of pathological, biomarker, genetic, and mechanistic data suggests that amyloid accumulation, as a result of changes in production, processing, and/or clearance of brain amyloid-β peptide (Aβ) concentrations, plays a key role in the
Autor:
Sanja Juric, Janet Hoogstraate, Tjerk Bueters, Margareta Bergh, Olle Gissberg, Yin Hu, Pawel Baranczewski, Jenny U. Johansson, Juliette Janson, Carrie Tsoi, Anna Breitholtz-Emanuelsson, Anders E. G. Lindgren, Sveinn Briem, Anna-Karin Sohlenius-Sternbeck, Johan Bylund
Publikováno v:
Current Drug Metabolism. 17:253-270
Background: The disposition of a drug is dependent on interactions between the body and the drug, its molecular properties and the physical and biological barriers presented in the body. In order for a drug to have a desired pharmacological effect it
Publikováno v:
Molecular Genetics and Metabolism. 126:S79
Mucopolysaccharidosis type IIIA (MPS IIIA) is an autosomal recessive disorder caused by absence or deficiency of the lysosomal enzyme sulfamidase. Glycans of recombinant human sulfamidase were chemically modified to generate CM-rhSulfamidase with ret
Autor:
Christin Andersson, Per Ola Freskgård, Matthew Burrell, Lutz Jermutus, Carl I. Webster, Juliette Janson, Anna Bogstedt, Simon J. Henderson, Ulrich Haupts, Rajesh Narwal, Tom Goldschmidt, Ann-Charlott Steffen, Jan Tebbe, Susan B. Fowler, Paulina Appelkvist
Publikováno v:
Brain
Lowering levels of peripheral amyloid-β has been proposed as a strategy to reduce plaques in patients with Alzheimer’s disease. Henderson et al. test a modified version of the amyloid-degrading enzyme neprilysin in rats, monkeys and Tg2576 mice. L
Autor:
Karin Kolmodin, Juliette Janson, Britt-Marie Swahn, Stefan von Berg, Tjerk Bueters, Gvido Cebers, Ann-Cathrine Radesäter, Johanna Fälting, Fredrik Jeppsson, Susanne Gustavsson, Bart Ploeger, Sofia Karlström, Susanna Eketjäll, Lise-Lotte Olsson
Publikováno v:
Journal of Biological Chemistry. 287:41245-41257
β-Site amyloid precursor protein cleaving enzyme1 (BACE1) is one of the key enzymes involved in the processing of the amyloid precursor protein (APP) and formation of amyloid β peptide (Aβ) species. Because cerebral deposition of Aβ species might