There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 168 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 161 | - |
dc.citation.title | EXPERIMENTAL AND MOLECULAR MEDICINE | - |
dc.citation.volume | 37 | - |
dc.contributor.author | Song, M | - |
dc.contributor.author | Kim, MJ | - |
dc.contributor.author | Ha, S | - |
dc.contributor.author | Park, JB | - |
dc.contributor.author | Ryu, SH | - |
dc.contributor.author | Suh, PG | - |
dc.date.accessioned | 2023-12-22T10:36:19Z | - |
dc.date.available | 2023-12-22T10:36:19Z | - |
dc.date.created | 2015-01-16 | - |
dc.date.issued | 2005-06 | - |
dc.description.abstract | Phospholipase C-gamma 1, containing two SH2 and one SH3 domains which participate in the interaction between signaling molecules, plays a significant role in the growth factor-induced signal transduction. However, the role of the SH domains in the growth factor-induced PLC-gamma 1 regulation is unclear. By peptide-mass fingerprinting analysis, we have identified SHIN as the binding protein for the SH3 domain of PLC-gamma 1. SHIP1 was co-immunoprecipitated with PLC-gamma 1 and potentiated EGF-induced PLC-gamma 1 activation. However, inositol 5'-phosphatase activity of SHIN was not required for the potentiation of EGF-induced PLC-gamma 1 activation. Taken together, these results suggest that SHIP1 may function as an adaptor protein which can potentiate EGF-induced PLC-gamma 1 activation without regards to its inositol 5'-phosphatase activity. | - |
dc.identifier.bibliographicCitation | EXPERIMENTAL AND MOLECULAR MEDICINE, v.37, no.3, pp.161 - 168 | - |
dc.identifier.issn | 1226-3613 | - |
dc.identifier.scopusid | 2-s2.0-22244447751 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/10828 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=22244447751 | - |
dc.identifier.wosid | 000230510800003 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY | - |
dc.title | Inositol 5 '-phosphatase, SHIP1 interacts with phospholipase C-gamma 1 and modulates EGF-induced PLC activity | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | epidermal growth factor | - |
dc.subject.keywordAuthor | phospholipase | - |
dc.subject.keywordAuthor | C-gamma 1 | - |
dc.subject.keywordAuthor | SH2 domain-containing inositol 5 &apos |
- |
dc.subject.keywordAuthor | -phosphatase | - |
dc.subject.keywordAuthor | SH3 domain | - |
dc.subject.keywordPlus | TYROSINE-PHOSPHORYLATED PROTEIN | - |
dc.subject.keywordPlus | C-GAMMA-1 | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | SRC | - |
dc.subject.keywordPlus | SHC | - |
dc.subject.keywordPlus | 5-PHOSPHATASE | - |
dc.subject.keywordPlus | FIBROBLASTS | - |
dc.subject.keywordPlus | PHOSPHATASE | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | DOMAINS | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.