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pro vyhledávání: '"Casford, Samuel T."'
Autor:
Limbocker, Ryan, Chia, Sean, Ruggeri, Francesco S., Perni, Michele, Cascella, Roberta, Heller, Gabriella T., Meisl, Georg, Mannini, Benedetta, Habchi, Johnny, Michaels, Thomas C. T., Challa, Pavan K., Ahn, Minkoo, Casford, Samuel T., Fernando, Nilumi, Xu, Catherine K., Kloss, Nina D., Cohen, Samuel I. A., Kumita, Janet R., Cecchi, Cristina, Zasloff, Michael, Linse, Sara, Knowles, Tuomas P. J., Chiti, Fabrizio, Vendruscolo, Michele, Dobson, Christopher M.
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Nature Communications
Nature Communications
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ42) are key pathogenic agents in Alzheimer’s disease (AD). To investigate the relationship between Aβ42 aggregation and its cyt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::41a3541c60bc8a068ed7e8623b5d6545
https://doaj.org/article/e4aca3eea6e44315b03de5b6488da79d
https://doaj.org/article/e4aca3eea6e44315b03de5b6488da79d
Autor:
Limbocker, Ryan, Chia, Sean, Ruggeri, Francesco S., Perni, Michele, Cascella, Roberta, Heller, Gabriella T., Meisl, Georg, Mannini, Benedetta, Habchi, Johnny, Michaels, Thomas C.T., Challa, Pavan K., Ahn, Minkoo, Casford, Samuel T., Fernando, Nilumi, Xu, Catherine K., Kloss, Nina D., Cohen, Samuel I.A., Kumita, Janet R., Cecchi, Cristina, Zasloff, Michael, Linse, Sara, Knowles, Tuomas P.J., Chiti, Fabrizio, Vendruscolo, Michele, Dobson, Christopher M.
Publikováno v:
Nature Communications, 10(1)
Nature Communications 10 (2019) 1
Nature Communications 10 (2019) 1
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ 42 ) are key pathogenic agents in Alzheimer’s disease (AD). To investigate the relationship between Aβ 42 aggregation and its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::a490556daa4f7ac3025b22929f28e636
Akademický článek
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Autor:
Limbocker, Ryan, Chia, Sean, Ruggeri, Francesco S., Perni, Michele, Cascella, Roberta, Heller, Gabriella T., Meisl, Georg, Mannini, Benedetta, Habchi, Johnny, Michaels, Thomas C. T., Challa, Pavan K., Ahn, Minkoo, Casford, Samuel T., Fernando, Nilumi, Xu, Catherine K., Kloss, Nina D., Cohen, Samuel I. A., Kumita, Janet R., Cecchi, Cristina, Zasloff, Michael
Publikováno v:
Nature Communications; 1/15/2019, Vol. 10 Issue 1, p1-1, 1p
Autor:
Limbocker, Ryan, Chia, Sean, Ruggeri, Francesco S, Perni, Michele, Cascella, Roberta, Heller, Gabriella T, Meisl, Georg, Mannini, Benedetta, Habchi, Johnny, Michaels, Thomas CT, Challa, Pavan K, Ahn, Minkoo, Casford, Samuel T, Fernando, Nilumi, Xu, Catherine K, Kloss, Nina D, Cohen, Samuel IA, Kumita, Janet R, Cecchi, Cristina, Zasloff, Michael, Linse, Sara, Knowles, Tuomas PJ, Chiti, Fabrizio, Vendruscolo, Michele, Dobson, Christopher M
Transient oligomeric species formed during the aggregation process of the 42-residue form of the amyloid-β peptide (Aβ42) are key pathogenic agents in Alzheimer's disease (AD). To investigate the relationship between Aβ42 aggregation and its cytot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40c212943137fc6fad7330806e28254f