Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid.
about
Molecular dynamics investigation of the influence of anionic and zwitterionic interfaces on antimicrobial peptides' structure: implications for peptide toxicity and activityInvestigations into the membrane interactions of m-calpain domain V.Comparison between the behavior of different hydrophobic peptides allowing membrane anchoring of proteins.New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysisRegulation of calpain activity in rat brain with altered Ca2+ homeostasis.
P2860
Domain V of m-calpain shows the potential to form an oblique-orientated alpha-helix, which may modulate the enzyme's activity via interactions with anionic lipid.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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name
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@en
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@nl
type
label
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@en
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@nl
prefLabel
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@en
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@nl
P2093
P2860
P1433
P1476
Domain V of m-calpain shows th ...... teractions with anionic lipid.
@en
P2093
David Phoenix
Frederick Harris
Sarah Dennison
Ulrich Seydel
P2860
P304
P356
10.1046/J.1432-1033.2002.03225.X
P407
P577
2002-11-01T00:00:00Z