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박철민

Park, Cheol-Min
Synthetic and Medicinal Chemistry Lab.
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Selective binding of bryostatin analogues to the cysteine rich domains of protein kinase C isozymes

Author(s)
Wender, PALippa, BPark, Cheol-MinIrie, KNakahara, AOhigashi, H
Issued Date
1999-06
DOI
10.1016/S0960-894X(99)00263-2
URI
https://scholarworks.unist.ac.kr/handle/201301/8571
Fulltext
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0033591714
Citation
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, v.9, no.12, pp.1687 - 1690
Abstract
Designed bryostatin analogues are assayed for binding affinity to individual cysteine rich domains of several protein kinase C (PKC) isozymes. These analogues exhibit significant selectivity for the PKCδ-C1B peptide in terms of absolute affinity and the PKCδ-C1A peptide in terms of relative affinity when compared to phorbol-12,13-dibutyrate.
Publisher
PERGAMON-ELSEVIER SCIENCE LTD
ISSN
0960-894X

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