Identification of novel protein tyrosine phosphatase sigma inhibitors promoting neurite extension

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dc.contributor.authorHye Seon Lee-
dc.contributor.authorBonsu Ku-
dc.contributor.authorT H Park-
dc.contributor.authorH Park-
dc.contributor.authorJ K Choi-
dc.contributor.authorKyu Tae Chang-
dc.contributor.authorC H Kim-
dc.contributor.authorS E Ryu-
dc.contributor.authorSeung Jun Kim-
dc.date.accessioned2017-04-19T10:15:31Z-
dc.date.available2017-04-19T10:15:31Z-
dc.date.issued2016-
dc.identifier.issn0960894X-
dc.identifier.uri10.1016/j.bmcl.2015.11.026ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13030-
dc.description.abstractProtein tyrosine phosphatase sigma (PTPσ) is a potential target for the therapeutic treatment of neurological deficits associated with impaired neuronal recovery, as this protein is the receptor for chondroitin sulfate proteoglycan (CSPG), which is known to inhibit neuronal regeneration. Through a high-throughput screening approach started from 6400 representative compounds in the Korea Chemical Bank chemical library, we identified 11 novel PTPσ inhibitors that can be classified as flavonoid derivatives or analogs, with IC50 values ranging from 0.5 to 17.5 μM. Biochemical assays and structure-based active site-docking simulation indicate that our inhibitors are accommodated at the catalytic active site of PTPσ as surrogates for the phosphotyrosine group. Treatments of these compounds on PC-12 neuronal cells led to the recovery of neurite extension attenuated by CSPG treatment, demonstrating their potential as antineurodegenerative agents.-
dc.publisherElsevier-
dc.titleIdentification of novel protein tyrosine phosphatase sigma inhibitors promoting neurite extension-
dc.title.alternativeIdentification of novel protein tyrosine phosphatase sigma inhibitors promoting neurite extension-
dc.typeArticle-
dc.citation.titleBioorganic & Medicinal Chemistry Letters-
dc.citation.number1-
dc.citation.endPage93-
dc.citation.startPage87-
dc.citation.volume26-
dc.contributor.affiliatedAuthorBonsu Ku-
dc.contributor.affiliatedAuthorSeung Jun Kim-
dc.contributor.alternativeName이혜선-
dc.contributor.alternativeName구본수-
dc.contributor.alternativeName박태현-
dc.contributor.alternativeName박황서-
dc.contributor.alternativeName최중권-
dc.contributor.alternativeName장규태-
dc.contributor.alternativeName김철희-
dc.contributor.alternativeName류성언-
dc.contributor.alternativeName김승준-
dc.identifier.bibliographicCitationBioorganic & Medicinal Chemistry Letters, vol. 26, no. 1, pp. 87-93-
dc.identifier.doi10.1016/j.bmcl.2015.11.026-
dc.subject.keywordHigh-throughput screening-
dc.subject.keywordInhibitor-
dc.subject.keywordProtein tyrosine phosphatase-
dc.subject.keywordPTPr-
dc.subject.keywordReceptor type PTP-
dc.subject.localHigh-throughput screening-
dc.subject.localHigh-throughput screening (HTS)-
dc.subject.localInhibitor-
dc.subject.localProtein tyrosine phosphatase-
dc.subject.localPTPr-
dc.subject.localReceptor type PTP-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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