Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation.
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Systemic amyloidosis: lessons from β2-microglobulin.Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.Molecular dynamics simulations of β2-microglobulin interaction with hydrophobic surfaces.Citrate-stabilized gold nanoparticles hinder fibrillogenesis of a pathological variant of β2-microglobulin.
P2860
Reduction of conformational mobility and aggregation in W60G β2-microglobulin: assessment by 15N NMR relaxation.
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2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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name
Reduction of conformational mo ...... essment by 15N NMR relaxation.
@en
Reduction of conformational mo ...... essment by 15N NMR relaxation.
@nl
type
label
Reduction of conformational mo ...... essment by 15N NMR relaxation.
@en
Reduction of conformational mo ...... essment by 15N NMR relaxation.
@nl
prefLabel
Reduction of conformational mo ...... essment by 15N NMR relaxation.
@en
Reduction of conformational mo ...... essment by 15N NMR relaxation.
@nl
P2093
P2860
P50
P356
P1476
Reduction of conformational mo ...... sessment by 15N NMR relaxation
@en
P2093
Devrim Gümral
Gennaro Esposito
Monica Stoppini
Paolo Viglino
Sofia Giorgetti
P2860
P304
P356
10.1002/MRC.4018
P577
2013-10-18T00:00:00Z