Structure-Based Virtual Screening of Protein Tyrosine Phosphatase Inhibitors: Significance, Challenges, and Solutions
DC Field | Value | Language |
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dc.contributor.author | Reddy, Rallabandi Harikrishna | - |
dc.contributor.author | Kim, Hackyoung | - |
dc.contributor.author | Cha, Seungbin | - |
dc.contributor.author | Lee, Bongsoo | - |
dc.contributor.author | Kim, Young Jun | - |
dc.date.available | 2019-03-08T08:57:17Z | - |
dc.date.issued | 2017-05 | - |
dc.identifier.issn | 1017-7825 | - |
dc.identifier.issn | 1738-8872 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/4549 | - |
dc.description.abstract | Phosphorylation, a critical mechanism in biological systems, is estimated to be indispensable for about 30% of key biological activities, such as cell cycle progression, migration, and division. It is synergistically balanced by kinases and phosphatases, and any deviation from this balance leads to disease conditions. Pathway or biological activity-based abnormalities in phosphorylation and the type of involved phosphatase influence the outcome, and cause diverse diseases ranging from diabetes, rheumatoid arthritis, and numerous cancers. Protein tyrosine phosphatases (PTPs) are of prime importance in the process of dephosphorylation and catalyze several biological functions. Abnormal PTP activities are reported to result in several human diseases. Consequently, there is an increased demand for potential PTP inhibitory small molecules. Several strategies in structure-based drug designing techniques for potential inhibitory small molecules of PTPs have been explored along with traditional drug designing methods in order to overcome the hurdles in PTP inhibitor discovery. In this review, we discuss druggable PTPs and structure-based virtual screening efforts for successful PTP inhibitor design. | - |
dc.format.extent | 18 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY | - |
dc.title | Structure-Based Virtual Screening of Protein Tyrosine Phosphatase Inhibitors: Significance, Challenges, and Solutions | - |
dc.type | Article | - |
dc.identifier.doi | 10.4014/jmb.1701.01079 | - |
dc.identifier.bibliographicCitation | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.27, no.5, pp 878 - 895 | - |
dc.identifier.kciid | ART002224682 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000405680000002 | - |
dc.identifier.scopusid | 2-s2.0-85019742040 | - |
dc.citation.endPage | 895 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 878 | - |
dc.citation.title | JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | - |
dc.citation.volume | 27 | - |
dc.type.docType | Review | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Allosteric targeting | - |
dc.subject.keywordAuthor | cancers | - |
dc.subject.keywordAuthor | diabetes | - |
dc.subject.keywordAuthor | drug designing | - |
dc.subject.keywordAuthor | molecular docking | - |
dc.subject.keywordAuthor | protein tyrosine phosphatases | - |
dc.subject.keywordPlus | ACTIVE-SITE CYSTEINE | - |
dc.subject.keywordPlus | WPD-LOOP | - |
dc.subject.keywordPlus | PTP-SIGMA | - |
dc.subject.keywordPlus | SCORING FUNCTIONS | - |
dc.subject.keywordPlus | CDC25 PHOSPHATASES | - |
dc.subject.keywordPlus | CANCER METASTASIS | - |
dc.subject.keywordPlus | BINDING-SITES | - |
dc.subject.keywordPlus | DRUG DESIGN | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | BIOLOGICAL EVALUATION | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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