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High intracellular stability of the spidroin N-terminal domain in spite of abundant amyloidogenic segments revealed by in-cell hydrogen/deuterium exchange mass spectrometry

Kaldmae, Margit; Leppert, Axel; Chen, Gefei; Sarr, Medoune; Sahin, Cagla; Nordling, Kerstin; Kronqvist, Nina; Gonzalvo-Ulla, Marta; Fritz, Nicolas; Abelein, Axel; Lain, Sonia; Biverstal, Henrik; Jornvall, Hans; Lane, David P.; Rising, Anna; Johansson, Jan; Landreh, Michael (2019). High intracellular stability of the spidroin N-terminal domain in spite of abundant amyloidogenic segments revealed by in-cell hydrogen/deuterium exchange mass spectrometry. FEBS Journal.10.1111/febs.15169.
ajakirjaartikkel
Kaldmae, Margit; Leppert, Axel; Chen, Gefei; Sarr, Medoune; Sahin, Cagla; Nordling, Kerstin; Kronqvist, Nina; Gonzalvo-Ulla, Marta; Fritz, Nicolas; Abelein, Axel; Lain, Sonia; Biverstal, Henrik; Jornvall, Hans; Lane, David P.; Rising, Anna; Johansson, Jan; Landreh, Michael
  • Inglise
FEBS Journal
HOBOKEN
1742-464X
2019
11
Ilmunud
1.1. Teadusartiklid, mis on kajastatud Web of Science andmebaasides Science Citation Index Expanded, Social Sciences Citation Index, Arts & Humanities Citation Index ja/või andmebaasis Scopus (v.a. kogumikud)
WOS

Viited terviktekstile

dx.doi.org/10.1111/febs.15169

Seotud asutused

Lisainfo

Article
hydrogen; deuterium exchange mass spectrometry; intracellular protein folding; protein aggregation; spider silk