Materials Map

Discover the materials research landscape. Find experts, partners, networks.

  • About
  • Privacy Policy
  • Legal Notice
  • Contact

The Materials Map is an open tool for improving networking and interdisciplinary exchange within materials research. It enables cross-database search for cooperation and network partners and discovering of the research landscape.

The dashboard provides detailed information about the selected scientist, e.g. publications. The dashboard can be filtered and shows the relationship to co-authors in different diagrams. In addition, a link is provided to find contact information.

×

Materials Map under construction

The Materials Map is still under development. In its current state, it is only based on one single data source and, thus, incomplete and contains duplicates. We are working on incorporating new open data sources like ORCID to improve the quality and the timeliness of our data. We will update Materials Map as soon as possible and kindly ask for your patience.

To Graph

1.080 Topics available

To Map

977 Locations available

693.932 PEOPLE
693.932 People People

693.932 People

Show results for 693.932 people that are selected by your search filters.

←

Page 1 of 27758

→
←

Page 1 of 0

→
PeopleLocationsStatistics
Naji, M.
  • 2
  • 13
  • 3
  • 2025
Motta, Antonella
  • 8
  • 52
  • 159
  • 2025
Aletan, Dirar
  • 1
  • 1
  • 0
  • 2025
Mohamed, Tarek
  • 1
  • 7
  • 2
  • 2025
Ertürk, Emre
  • 2
  • 3
  • 0
  • 2025
Taccardi, Nicola
  • 9
  • 81
  • 75
  • 2025
Kononenko, Denys
  • 1
  • 8
  • 2
  • 2025
Petrov, R. H.Madrid
  • 46
  • 125
  • 1k
  • 2025
Alshaaer, MazenBrussels
  • 17
  • 31
  • 172
  • 2025
Bih, L.
  • 15
  • 44
  • 145
  • 2025
Casati, R.
  • 31
  • 86
  • 661
  • 2025
Muller, Hermance
  • 1
  • 11
  • 0
  • 2025
Kočí, JanPrague
  • 28
  • 34
  • 209
  • 2025
Šuljagić, Marija
  • 10
  • 33
  • 43
  • 2025
Kalteremidou, Kalliopi-ArtemiBrussels
  • 14
  • 22
  • 158
  • 2025
Azam, Siraj
  • 1
  • 3
  • 2
  • 2025
Ospanova, Alyiya
  • 1
  • 6
  • 0
  • 2025
Blanpain, Bart
  • 568
  • 653
  • 13k
  • 2025
Ali, M. A.
  • 7
  • 75
  • 187
  • 2025
Popa, V.
  • 5
  • 12
  • 45
  • 2025
Rančić, M.
  • 2
  • 13
  • 0
  • 2025
Ollier, Nadège
  • 28
  • 75
  • 239
  • 2025
Azevedo, Nuno Monteiro
  • 4
  • 8
  • 25
  • 2025
Landes, Michael
  • 1
  • 9
  • 2
  • 2025
Rignanese, Gian-Marco
  • 15
  • 98
  • 805
  • 2025

Curran, Elizabeth

  • Google
  • 1
  • 11
  • 2

in Cooperation with on an Cooperation-Score of 37%

Topics

Publications (1/1 displayed)

  • 2022Proteasome activity modulates amyloid toxicity2citations

Places of action

Chart of shared publication
Brodsky, Jeffrey L.
1 / 1 shared
Potter, Huntington
1 / 1 shared
Coughlan, Christina
1 / 1 shared
Chial, Heidi J.
1 / 1 shared
Hansen, Kirk C.
1 / 1 shared
Mcmurray, Michael A.
1 / 1 shared
Aubuchon-Endsley, Nicki
1 / 1 shared
Goossens, Alicia
1 / 1 shared
Galvin, John
1 / 1 shared
Arteaga, Francisco
1 / 2 shared
Moore, Jeffrey
1 / 2 shared
Chart of publication period
2022

Co-Authors (by relevance)

  • Brodsky, Jeffrey L.
  • Potter, Huntington
  • Coughlan, Christina
  • Chial, Heidi J.
  • Hansen, Kirk C.
  • Mcmurray, Michael A.
  • Aubuchon-Endsley, Nicki
  • Goossens, Alicia
  • Galvin, John
  • Arteaga, Francisco
  • Moore, Jeffrey
OrganizationsLocationPeople

article

Proteasome activity modulates amyloid toxicity

  • Brodsky, Jeffrey L.
  • Potter, Huntington
  • Coughlan, Christina
  • Chial, Heidi J.
  • Hansen, Kirk C.
  • Mcmurray, Michael A.
  • Aubuchon-Endsley, Nicki
  • Goossens, Alicia
  • Curran, Elizabeth
  • Galvin, John
  • Arteaga, Francisco
  • Moore, Jeffrey
Abstract

<jats:title>Abstract</jats:title><jats:p>Alzheimer's disease (AD) is responsible for 60%–80% of identified cases of dementia. While the generation and accumulation of amyloid precursor protein (APP) fragments is accepted as a key step in AD pathogenesis, the precise role of these fragments remains poorly understood. To overcome this deficit, we induced the expression of the soluble C-terminal fragment of APP (C99), the rate-limiting peptide for the generation of amyloid fragments, in yeast that contain thermosensitive mutations in genes encoding proteasome subunits. Our previous work with this system demonstrated that these proteasome-deficient yeast cells, expressing C99 when proteasome activity was blunted, generated amyloid fragments similar to those observed in AD patients. We now report the phenotypic repercussions of inducing C99 expression in proteasome-deficient cells. We show increased levels of protein aggregates, cellular stress and chaperone expression, electron-dense accumulations in the nuclear envelope/ER, abnormal DNA condensation, and an induction of apoptosis. Taken together, these findings suggest that the generation of C99 and its associated fragments in yeast cells with compromised proteasomal activity results in phenotypes that may be relevant to the neuropathological processes observed in AD patients. These data also suggest that this yeast model should be useful for testing therapeutics that target AD-associated amyloid, since it allows for the assessment of the reversal of the perturbed cellular physiology observed when degradation pathways are dysfunctional.</jats:p>

Topics
  • impedance spectroscopy
  • toxicity