On the orientation of the catalytic dyad in aspartic proteases.
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An acidic loop and cognate phosphorylation sites define a molecular switch that modulates ubiquitin charging activity in Cdc34-like enzymesMolecular dynamics of mesophilic-like mutants of a cold-adapted enzyme: insights into distal effects induced by the mutationsUnveiling a novel transient druggable pocket in BACE-1 through molecular simulations: Conformational analysis and binding mode of multisite inhibitors.DNA Damage in Major Psychiatric Diseases.
P2860
On the orientation of the catalytic dyad in aspartic proteases.
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2010 nî lūn-bûn
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2010年学术文章
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2010年学术文章
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On the orientation of the catalytic dyad in aspartic proteases.
@en
On the orientation of the catalytic dyad in aspartic proteases.
@nl
type
label
On the orientation of the catalytic dyad in aspartic proteases.
@en
On the orientation of the catalytic dyad in aspartic proteases.
@nl
prefLabel
On the orientation of the catalytic dyad in aspartic proteases.
@en
On the orientation of the catalytic dyad in aspartic proteases.
@nl
P356
P1433
P1476
On the orientation of the catalytic dyad in aspartic proteases.
@en
P2093
Amedeo Caflisch
Ran Friedman
P2860
P304
P356
10.1002/PROT.22674
P407
P577
2010-05-01T00:00:00Z