Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3.
about
A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosisRapid Folding and Unfolding of Apaf-1 CARDThermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.Allosteric modulation of caspase 3 through mutagenesisPhage display and structural studies reveal plasticity in substrate specificity of caspase-3a from zebrafishTunable allosteric library of caspase-3 identifies coupling between conserved water molecules and conformational selectionA bifunctional allosteric site in the dimer interface of procaspase-3Modifying caspase-3 activity by altering allosteric networks.Reassembly of active caspase-3 is facilitated by the propeptide.Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3.Modifications to a common phosphorylation network provide individualized control in caspases.
P2860
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P2860
Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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name
Ionic interactions near the lo ...... r stability of (pro)caspase 3.
@en
Ionic interactions near the lo ...... ent and the dimer stability of
@nl
type
label
Ionic interactions near the lo ...... r stability of (pro)caspase 3.
@en
Ionic interactions near the lo ...... ent and the dimer stability of
@nl
prefLabel
Ionic interactions near the lo ...... r stability of (pro)caspase 3.
@en
Ionic interactions near the lo ...... ent and the dimer stability of
@nl
P2093
P2860
P356
P1433
P1476
Ionic interactions near the lo ...... r stability of (pro)caspase 3.
@en
P2093
A Clay Clark
Ashutosh Tripathy
Brett Feeney
Cristina Pop
P2860
P304
P356
10.1042/BJ20040693
P407
P577
2004-12-01T00:00:00Z