Differential regulation of protein subdomain activity with caged bivalent ligands.
about
High-resolution structures of two complexes between thrombin and thrombin-binding aptamer shed light on the role of cations in the aptamer inhibitory activityDuplex-quadruplex motifs in a peculiar structural organization cooperatively contribute to thrombin binding of a DNA aptamerThrough-bond effects in the ternary complexes of thrombin sandwiched by two DNA aptamers.Highly efficient control of thrombin activity by multivalent nanoparticles.Dependence of aptamer activity on opposed terminal extensions: improvement of light-regulation efficiency.Optochemical control of deoxyoligonucleotide function via a nucleobase-caging approach.5-Fluoro pyrimidines: labels to probe DNA and RNA secondary structures by 1D 19F NMR spectroscopy.Light-activatable molecular beacons with a caged loop sequence.Gold and Silver Nanomaterial-Based Optical Sensing Systems
P2860
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P2860
Differential regulation of protein subdomain activity with caged bivalent ligands.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
@zh-cn
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2009年學術文章
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name
Differential regulation of protein subdomain activity with caged bivalent ligands.
@en
Differential regulation of protein subdomain activity with caged bivalent ligands.
@nl
type
label
Differential regulation of protein subdomain activity with caged bivalent ligands.
@en
Differential regulation of protein subdomain activity with caged bivalent ligands.
@nl
prefLabel
Differential regulation of protein subdomain activity with caged bivalent ligands.
@en
Differential regulation of protein subdomain activity with caged bivalent ligands.
@nl
P2093
P2860
P356
P1433
P1476
Differential regulation of protein subdomain activity with caged bivalent ligands.
@en
P2093
Alexander Heckel
Bernd Pötzsch
Daniel F Freitag
Günter Mayer
Jens Müller
Thomas Höver
P2860
P304
P356
10.1002/CBIC.200800814
P577
2009-03-01T00:00:00Z