Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization

T.D. Dang, H. Nguyen, M. Merkx, L. Brunsveld

Research output: Contribution to journalArticleAcademicpeer-review

65 Citations (Scopus)
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Abstract

At the double: Cucurbit[8]uril-mediated protein dimerization enables reversible control over strong enzyme activation of caspases. Simple addition of a short N-terminal FGG motif allows for a supramolecular-mediated 50-fold enhancement of caspase-9 catalytic activity.
Original languageEnglish
Pages (from-to)2915-2919
Number of pages4
JournalAngewandte Chemie - International Edition
Volume52
Issue number10
DOIs
Publication statusPublished - 2013

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Dimerization
Caspase 9
Enzyme activity
Caspases
Catalyst activity
Enzymes
Chemical activation
Proteins
cucurbit(8)uril

Cite this

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title = "Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization",
abstract = "At the double: Cucurbit[8]uril-mediated protein dimerization enables reversible control over strong enzyme activation of caspases. Simple addition of a short N-terminal FGG motif allows for a supramolecular-mediated 50-fold enhancement of caspase-9 catalytic activity.",
author = "T.D. Dang and H. Nguyen and M. Merkx and L. Brunsveld",
year = "2013",
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journal = "Angewandte Chemie - International Edition",
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Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization. / Dang, T.D.; Nguyen, H.; Merkx, M.; Brunsveld, L.

In: Angewandte Chemie - International Edition, Vol. 52, No. 10, 2013, p. 2915-2919.

Research output: Contribution to journalArticleAcademicpeer-review

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T1 - Supramolecular control of enzyme activity through cucurbit[8]uril mediated dimerization

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AU - Nguyen, H.

AU - Merkx, M.

AU - Brunsveld, L.

PY - 2013

Y1 - 2013

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AB - At the double: Cucurbit[8]uril-mediated protein dimerization enables reversible control over strong enzyme activation of caspases. Simple addition of a short N-terminal FGG motif allows for a supramolecular-mediated 50-fold enhancement of caspase-9 catalytic activity.

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DO - 10.1002/anie.201208239

M3 - Article

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VL - 52

SP - 2915

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

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