Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.
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The Pathogenic A116V Mutation Enhances Ion-Selective Channel Formation by Prion Protein in Membranes.The native state of prion protein (PrP) directly inhibits formation of PrP-amyloid fibrils in vitro.How cooperative are protein folding and unfolding transitions?Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.
P2860
Partially Unfolded Forms of the Prion Protein Populated under Misfolding-promoting Conditions: CHARACTERIZATION BY HYDROGEN EXCHANGE MASS SPECTROMETRY AND NMR.
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Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
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Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
@en
type
label
Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
@ast
Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
@en
prefLabel
Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
@ast
Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
@en
P2093
P2860
P356
P1476
Partially Unfolded Forms of th ...... NGE MASS SPECTROMETRY AND NMR.
@en
P2093
Jayant B Udgaonkar
Ranabir Das
Roumita Moulick
P2860
P304
25227-25240
P356
10.1074/JBC.M115.677575
P407
P577
2015-08-25T00:00:00Z