2018 |
Rasmussen, Jay; Krasemann, Susanne; Altmeppen, Hermann; Schwarz, Petra; Schelle, Juliane; Aguzzi, Adriano; Glatzel, Markus; Jucker, Mathias Infectious prions do not induce Aβ deposition in an in vivo seeding model (Journal Article) Acta Neuropathol, 135 (6), pp. 965–967, 2018, ISSN: 0001-6322, 1432-0533. (Links | BibTeX | Altmetric) @article{rasmussen_infectious_2018,
title = {Infectious prions do not induce Aβ deposition in an in vivo seeding model},
author = {Jay Rasmussen and Susanne Krasemann and Hermann Altmeppen and Petra Schwarz and Juliane Schelle and Adriano Aguzzi and Markus Glatzel and Mathias Jucker},
url = {http://link.springer.com/10.1007/s00401-018-1848-5},
doi = {10.1007/s00401-018-1848-5},
issn = {0001-6322, 1432-0533},
year = {2018},
date = {2018-01-01},
urldate = {2019-06-26},
journal = {Acta Neuropathol},
volume = {135},
number = {6},
pages = {965--967},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Klima, Cassidy L; Zaheer, Rahat; Cook, Shaun R; Rasmussen, Jay; Alexander, Trevor W; Potter, Andrew; Hendrick, Steve; McAllister, Tim A In silico identification and high throughput screening of antigenic proteins as candidates for a Mannheimia haemolytica vaccine (Journal Article) Veterinary Immunology and Immunopathology, 195 , pp. 19–24, 2018, ISSN: 01652427. (Links | BibTeX | Altmetric) @article{klima_silico_2018,
title = {In silico identification and high throughput screening of antigenic proteins as candidates for a Mannheimia haemolytica vaccine},
author = {Cassidy L Klima and Rahat Zaheer and Shaun R Cook and Jay Rasmussen and Trevor W Alexander and Andrew Potter and Steve Hendrick and Tim A McAllister},
url = {https://linkinghub.elsevier.com/retrieve/pii/S0165242717301435},
doi = {10.1016/j.vetimm.2017.11.004},
issn = {01652427},
year = {2018},
date = {2018-01-01},
urldate = {2019-06-26},
journal = {Veterinary Immunology and Immunopathology},
volume = {195},
pages = {19--24},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2017 |
Rasmussen, Jay; Jucker, Mathias; Walker, Lary C Aβ seeds and prions: How close the fit? (Journal Article) Prion, 11 (4), pp. 215–225, 2017, ISSN: 1933-6896, 1933-690X. (Links | BibTeX | Altmetric) @article{rasmussen__2017,
title = {Aβ seeds and prions: How close the fit?},
author = {Jay Rasmussen and Mathias Jucker and Lary C Walker},
url = {https://www.tandfonline.com/doi/full/10.1080/19336896.2017.1334029},
doi = {10.1080/19336896.2017.1334029},
issn = {1933-6896, 1933-690X},
year = {2017},
date = {2017-01-01},
urldate = {2019-06-26},
journal = {Prion},
volume = {11},
number = {4},
pages = {215--225},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Rasmussen, Jay; Mahler, Jasmin; Beschorner, Natalie; Kaeser, Stephan A; Häsler, Lisa M; Baumann, Frank; Nyström, Sofie; Portelius, Erik; Blennow, Kaj; Lashley, Tammaryn; Fox, Nick C; Sepulveda-Falla, Diego; Glatzel, Markus; Oblak, Adrian L; Ghetti, Bernardino; Nilsson, Peter K R; Hammarström, Per; Staufenbiel, Matthias; Walker, Lary C; Jucker, Mathias Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer’s disease (Journal Article) Proc Natl Acad Sci USA, 114 (49), pp. 13018–13023, 2017, ISSN: 0027-8424, 1091-6490. (Abstract | Links | BibTeX | Altmetric) @article{rasmussen_amyloid_2017,
title = {Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer’s disease},
author = {Jay Rasmussen and Jasmin Mahler and Natalie Beschorner and Stephan A Kaeser and Lisa M H\"{a}sler and Frank Baumann and Sofie Nystr\"{o}m and Erik Portelius and Kaj Blennow and Tammaryn Lashley and Nick C Fox and Diego Sepulveda-Falla and Markus Glatzel and Adrian L Oblak and Bernardino Ghetti and Peter K R Nilsson and Per Hammarstr\"{o}m and Matthias Staufenbiel and Lary C Walker and Mathias Jucker},
url = {http://www.pnas.org/lookup/doi/10.1073/pnas.1713215114},
doi = {10.1073/pnas.1713215114},
issn = {0027-8424, 1091-6490},
year = {2017},
date = {2017-01-01},
urldate = {2019-06-26},
journal = {Proc Natl Acad Sci USA},
volume = {114},
number = {49},
pages = {13018--13023},
abstract = {The molecular architecture of amyloids formed in vivo can be interrogated using luminescent conjugated oligothiophenes (LCOs), a unique class of amyloid dyes. When bound to amyloid, LCOs yield fluorescence emission spectra that reflect the 3D structure of the protein aggregates. Given that synthetic amyloid-β peptide (Aβ) has been shown to adopt distinct structural conformations with different biological activities, we asked whether Aβ can assume structurally and functionally distinct conformations within the brain. To this end, we analyzed the LCO-stained cores of β-amyloid plaques in postmortem tissue sections from frontal, temporal, and occipital neocortices in 40 cases of familial Alzheimer’s disease (AD) or sporadic (idiopathic) AD (sAD). The spectral attributes of LCO-bound plaques varied markedly in the brain, but the mean spectral properties of the amyloid cores were generally similar in all three cortical regions of individual patients. Remarkably, the LCO amyloid spectra differed significantly among some of the familial and sAD subtypes, and between typical patients with sAD and those with posterior cortical atrophy AD. Neither the amount of Aβ nor its protease resistance correlated with LCO spectral properties. LCO spectral amyloid phenotypes could be partially conveyed to Aβ plaques induced by experimental transmission in a mouse model. These findings indicate that polymorphic Aβ-amyloid deposits within the brain cluster as clouds of conformational variants in different AD cases. Heterogeneity in the molecular architecture of pathogenic Aβ among individuals and in etiologically distinct subtypes of AD justifies further studies to assess putative links between Aβ conformation and clinical phenotype.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The molecular architecture of amyloids formed in vivo can be interrogated using luminescent conjugated oligothiophenes (LCOs), a unique class of amyloid dyes. When bound to amyloid, LCOs yield fluorescence emission spectra that reflect the 3D structure of the protein aggregates. Given that synthetic amyloid-β peptide (Aβ) has been shown to adopt distinct structural conformations with different biological activities, we asked whether Aβ can assume structurally and functionally distinct conformations within the brain. To this end, we analyzed the LCO-stained cores of β-amyloid plaques in postmortem tissue sections from frontal, temporal, and occipital neocortices in 40 cases of familial Alzheimer’s disease (AD) or sporadic (idiopathic) AD (sAD). The spectral attributes of LCO-bound plaques varied markedly in the brain, but the mean spectral properties of the amyloid cores were generally similar in all three cortical regions of individual patients. Remarkably, the LCO amyloid spectra differed significantly among some of the familial and sAD subtypes, and between typical patients with sAD and those with posterior cortical atrophy AD. Neither the amount of Aβ nor its protease resistance correlated with LCO spectral properties. LCO spectral amyloid phenotypes could be partially conveyed to Aβ plaques induced by experimental transmission in a mouse model. These findings indicate that polymorphic Aβ-amyloid deposits within the brain cluster as clouds of conformational variants in different AD cases. Heterogeneity in the molecular architecture of pathogenic Aβ among individuals and in etiologically distinct subtypes of AD justifies further studies to assess putative links between Aβ conformation and clinical phenotype. |
Ye, Lan; Rasmussen, Jay; Kaeser, Stephan A; Marzesco, Anne‐Marie; Obermüller, Ulrike; Mahler, Jasmin; Schelle, Juliane; Odenthal, Jörg; Krüger, Christian; Fritschi, Sarah K; Walker, Lary C; Staufenbiel, Matthias; Baumann, Frank; Jucker, Mathias Aβ seeding potency peaks in the early stages of cerebral β‐amyloidosis (Journal Article) EMBO Rep., 18 (9), pp. 1536–1544, 2017, ISSN: 1469-221X, 1469-3178, 1469-221X, 1469-3178. (Links | BibTeX | Altmetric) @article{ye__2017,
title = {Aβ seeding potency peaks in the early stages of cerebral β‐amyloidosis},
author = {Lan Ye and Jay Rasmussen and Stephan A Kaeser and Anne‐Marie Marzesco and Ulrike Oberm\"{u}ller and Jasmin Mahler and Juliane Schelle and J\"{o}rg Odenthal and Christian Kr\"{u}ger and Sarah K Fritschi and Lary C Walker and Matthias Staufenbiel and Frank Baumann and Mathias Jucker},
url = {http://embor.embopress.org/lookup/doi/10.15252/embr.201744067},
doi = {10.15252/embr.201744067},
issn = {1469-221X, 1469-3178, 1469-221X, 1469-3178},
year = {2017},
date = {2017-01-01},
urldate = {2019-06-26},
journal = {EMBO Rep.},
volume = {18},
number = {9},
pages = {1536--1544},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2016 |
Klima, Cassidy L; Cook, Shaun R; Zaheer, Rahat; Laing, Chad; Gannon, Vick P; Xu, Yong; Rasmussen, Jay; Potter, Andrew; Hendrick, Steve; Alexander, Trevor W; McAllister, Tim A Comparative Genomic Analysis of Mannheimia haemolytica from Bovine Sources (Journal Article) PLoS ONE, 11 (2), pp. e0149520, 2016, ISSN: 1932-6203. (Links | BibTeX | Altmetric) @article{klima_comparative_2016,
title = {Comparative Genomic Analysis of Mannheimia haemolytica from Bovine Sources},
author = {Cassidy L Klima and Shaun R Cook and Rahat Zaheer and Chad Laing and Vick P Gannon and Yong Xu and Jay Rasmussen and Andrew Potter and Steve Hendrick and Trevor W Alexander and Tim A McAllister},
editor = {Baochuan Lin},
url = {https://dx.plos.org/10.1371/journal.pone.0149520},
doi = {10.1371/journal.pone.0149520},
issn = {1932-6203},
year = {2016},
date = {2016-01-01},
urldate = {2019-06-26},
journal = {PLoS ONE},
volume = {11},
number = {2},
pages = {e0149520},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2015 |
Rasmussen, Jay; Gilroyed, Brandon H; Reuter, Tim; Badea, Ana; Eudes, François; Graf, Robert; Laroche, André; Kav, Nat N V; McAllister, Tim A Protein can be taken up by damaged wheat roots and transported to the stem (Journal Article) J. Plant Biol., 58 (1), pp. 1–7, 2015, ISSN: 1226-9239, 1867-0725. (Links | BibTeX | Altmetric) @article{rasmussen_protein_2015,
title = {Protein can be taken up by damaged wheat roots and transported to the stem},
author = {Jay Rasmussen and Brandon H Gilroyed and Tim Reuter and Ana Badea and Fran\c{c}ois Eudes and Robert Graf and Andr\'{e} Laroche and Nat N V Kav and Tim A McAllister},
url = {http://link.springer.com/10.1007/s12374-014-0258-z},
doi = {10.1007/s12374-014-0258-z},
issn = {1226-9239, 1867-0725},
year = {2015},
date = {2015-02-01},
urldate = {2019-06-26},
journal = {J. Plant Biol.},
volume = {58},
number = {1},
pages = {1--7},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2014 |
Xu, Shanwei; Rasmussen, Jay; Ding, Ning; Neumann, Norman F; El-Din, Mohamed Gamal; Belosevic, Miodrag; McAllister, Tim Inactivation of infectious prions in the environment: a mini-review (Journal Article) Journal of Environmental Engineering and Science, 9 (2), pp. 125–136, 2014, ISSN: 1496-2551, 1496-256X. (Links | BibTeX | Altmetric) @article{xu_inactivation_2014,
title = {Inactivation of infectious prions in the environment: a mini-review},
author = {Shanwei Xu and Jay Rasmussen and Ning Ding and Norman F Neumann and Mohamed Gamal El-Din and Miodrag Belosevic and Tim McAllister},
url = {http://www.icevirtuallibrary.com/doi/10.1680/jees.13.00014},
doi = {10.1680/jees.13.00014},
issn = {1496-2551, 1496-256X},
year = {2014},
date = {2014-06-01},
urldate = {2019-06-26},
journal = {Journal of Environmental Engineering and Science},
volume = {9},
number = {2},
pages = {125--136},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Rasmussen, Jay; Gilroyed, Brandon H; Reuter, Tim; Dudas, Sandor; Neumann, Norman F; Balachandran, Aru; Kav, Nat NV; Graham, Catherine; Czub, Stefanie; McAllister, Tim A Can plants serve as a vector for prions causing chronic wasting disease? (Journal Article) Prion, 8 (1), pp. 136–142, 2014, ISSN: 1933-6896, 1933-690X. (Links | BibTeX | Altmetric) @article{rasmussen_can_2014,
title = {Can plants serve as a vector for prions causing chronic wasting disease?},
author = {Jay Rasmussen and Brandon H Gilroyed and Tim Reuter and Sandor Dudas and Norman F Neumann and Aru Balachandran and Nat NV Kav and Catherine Graham and Stefanie Czub and Tim A McAllister},
url = {http://www.tandfonline.com/doi/abs/10.4161/pri.27963},
doi = {10.4161/pri.27963},
issn = {1933-6896, 1933-690X},
year = {2014},
date = {2014-01-01},
urldate = {2019-06-26},
journal = {Prion},
volume = {8},
number = {1},
pages = {136--142},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Rasmussen, Jay; Gilroyed, Brandon H; Reuter, Tim; Badea, Ana; Eudes, François; Graf, Robert; Laroche, André; Kav, Nat N V; McAllister, Tim A Efficiency of protein as a nitrogen source for wheat and morphological changes in roots exposed to high protein concentrations (Journal Article) Can. J. Plant Sci., 94 (4), pp. 603–613, 2014, ISSN: 0008-4220, 1918-1833. (Links | BibTeX | Altmetric) @article{rasmussen_efficiency_2014,
title = {Efficiency of protein as a nitrogen source for wheat and morphological changes in roots exposed to high protein concentrations},
author = {Jay Rasmussen and Brandon H Gilroyed and Tim Reuter and Ana Badea and Fran\c{c}ois Eudes and Robert Graf and Andr\'{e} Laroche and Nat N V Kav and Tim A McAllister},
url = {http://www.nrcresearchpress.com/doi/10.4141/cjps2013-187},
doi = {10.4141/cjps2013-187},
issn = {0008-4220, 1918-1833},
year = {2014},
date = {2014-01-01},
urldate = {2019-06-26},
journal = {Can. J. Plant Sci.},
volume = {94},
number = {4},
pages = {603--613},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2013 |
Campeau, Jody L; Wu, Gengshu; Bell, John R; Rasmussen, Jay; Sim, Valerie L Early Increase and Late Decrease of Purkinje Cell Dendritic Spine Density in Prion-Infected Organotypic Mouse Cerebellar Cultures (Journal Article) PLoS ONE, 8 (12), pp. e81776, 2013, ISSN: 1932-6203. (Links | BibTeX | Altmetric) @article{campeau_early_2013,
title = {Early Increase and Late Decrease of Purkinje Cell Dendritic Spine Density in Prion-Infected Organotypic Mouse Cerebellar Cultures},
author = {Jody L Campeau and Gengshu Wu and John R Bell and Jay Rasmussen and Valerie L Sim},
editor = {Ilia V Baskakov},
url = {https://dx.plos.org/10.1371/journal.pone.0081776},
doi = {10.1371/journal.pone.0081776},
issn = {1932-6203},
year = {2013},
date = {2013-12-01},
urldate = {2019-06-26},
journal = {PLoS ONE},
volume = {8},
number = {12},
pages = {e81776},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
2012 |
Kooistra, Megan K; Leduc, Renee Y M; Dawe, Christine E; Fairbridge, Nicholas A; Rasmussen, Jay; Man, Julie H Y; Bujold, Mattea; Juriloff, Diana; King-Jones, Kirst; McDermid, Heather E Strain-specific modifier genes of textitCecr2 -associated exencephaly in mice: genetic analysis and identification of differentially expressed candidate genes (Journal Article) Physiological Genomics, 44 (1), pp. 35–46, 2012, ISSN: 1094-8341, 1531-2267. (Links | BibTeX | Altmetric) @article{kooistra_strain-specific_2012,
title = {Strain-specific modifier genes of textitCecr2 -associated exencephaly in mice: genetic analysis and identification of differentially expressed candidate genes},
author = {Megan K Kooistra and Renee Y M Leduc and Christine E Dawe and Nicholas A Fairbridge and Jay Rasmussen and Julie H Y Man and Mattea Bujold and Diana Juriloff and Kirst King-Jones and Heather E McDermid},
url = {http://www.physiology.org/doi/10.1152/physiolgenomics.00124.2011},
doi = {10.1152/physiolgenomics.00124.2011},
issn = {1094-8341, 1531-2267},
year = {2012},
date = {2012-01-01},
urldate = {2019-06-26},
journal = {Physiological Genomics},
volume = {44},
number = {1},
pages = {35--46},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Jay has had the opportunity to investigate different aspects of brain dysfunction in a variety of labs around the world. He first gained experience with neurodevelopment and neurodegeneration research during his BSc and MSc at the University of Alberta in Edmonton, Canada. Specifically, his research on prion diseases sparked his interest in neurodegeneration and the mechanisms behind brain deterioration. This led to the pursuit of a PhD in Tübingen, Germany in the lab of Professor Mathias Jucker starting in mid-2014 (Hertie Institute for Clinical Brain Research-HIH and the German Center for Neurodegenerative Diseases-DZNE). Here, Jay focused on the biochemical features of pathological protein deposits called senile plaques that are associated with Alzheimer’s disease and are made up of β-amyloid protein. This lead to the discovery that different subtypes of Alzheimer’s disease have distinct plaque features and that the earliest forms of deposited β-amyloid protein are uniquely influential in initiating a disease cascade.
