Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Matthias Gantner"'
Autor:
Matthias Gantner, Theodoros Laftsoglou, Honglin Rong, Vincent L. G. Postis, Lars J. C. Jeuken
Publikováno v:
Membranes, Vol 10, Iss 10, p 255 (2020)
Transition metals are essential trace elements and their high-affinity uptake is required for many organisms. Metal transporters are often characterised using metal-sensitive fluorescent dyes, limiting the metals and experimental conditions that can
Externí odkaz:
https://doaj.org/article/99fe156a12b241ea8237dbd4b57d4ac8
Autor:
Asen Daskalov, Matthias Gantner, Marielle Aulikki Wälti, Thierry Schmidlin, Celestine N Chi, Christian Wasmer, Anne Schütz, Johanna Ceschin, Corinne Clavé, Sandra Cescau, Beat Meier, Roland Riek, Sven J Saupe
Publikováno v:
PLoS Pathogens, Vol 10, Iss 6, p e1004158 (2014)
The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion fo
Externí odkaz:
https://doaj.org/article/809e9ec61a7d4cdf9fff4e06d3ad7584
Autor:
Lars J. C. Jeuken, Honglin Rong, Matthias Gantner, Vincent L. G. Postis, Theodoros Laftsoglou
Publikováno v:
Membranes, Vol 10, Iss 255, p 255 (2020)
Membranes
Volume 10
Issue 10
Membranes
Volume 10
Issue 10
Transition metals are essential trace elements and their high-affinity uptake is required for many organisms. Metal transporters are often characterised using metal-sensitive fluorescent dyes, limiting the metals and experimental conditions that can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eed6a7ba39c1fcf8ab2e9d9cf6c0f454
https://doi.org/10.3390/membranes10100255
https://doi.org/10.3390/membranes10100255
Autor:
Anne K. Schütz, Simone Hornemann, Adriano Aguzzi, Marielle A. Wälti, Anja Böckmann, Roland Riek, Per Hammarström, Riccardo Cadalbert, Cinzia Tiberi, Matthias Gantner, Beat H. Meier, K. Peter R. Nilsson, Ladina Greuter
Publikováno v:
ACS Chemical Neuroscience
ACS Chemical Neuroscience, American Chemical Society (ACS), 2018, 9 (3), pp.475-481. ⟨10.1021/acschemneuro.7b00397⟩
ACS Chemical Neuroscience, 9 (3)
ACS Chemical Neuroscience, American Chemical Society (ACS), 2018, 9 (3), pp.475-481. ⟨10.1021/acschemneuro.7b00397⟩
ACS Chemical Neuroscience, 9 (3)
Luminescent conjugated polythiophenes bind to amyloid proteins with high affinity. Their fluorescence properties, which are modulated by the detailed conformation in the bound state, are highly sensitive to structural features of the amyloid. Polythi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d66f0632fbb153acbd5e568b49f3fa8c
https://hal.archives-ouvertes.fr/hal-02322379
https://hal.archives-ouvertes.fr/hal-02322379
Autor:
Roland Riek, Marielle A. Wälti, Anne K. Schütz, Corinne Clavé, Christian Wasmer, Sandra Cescau, Johanna Ceschin, Sven J. Saupe, Beat H. Meier, Matthias Gantner, Asen Daskalov, Celestine N. Chi, Thierry Schmidlin
Publikováno v:
PLOS PATHOGENS
PLoS Pathogens
PLoS pathogens
PLoS Pathogens, 10 (6)
PLoS Pathogens, Vol 10, Iss 6, p e1004158 (2014)
PLoS Pathogens
PLoS pathogens
PLoS Pathogens, 10 (6)
PLoS Pathogens, Vol 10, Iss 6, p e1004158 (2014)
The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::696af7e1b5a64423da57a4806840566f
https://doi.org/10.1371/journal.ppat.1004158
https://doi.org/10.1371/journal.ppat.1004158