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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/40204

Title: In Silico Prediction and In Vitro Characterization of Multifunctional Human RNase3
Authors: Pei-Chun Lien
Ping-Hsueh Kuo
Chien-Jung Chen
Hsiu-Hui Chang
Shun-lung Fang
Wei-Shuo Wu
Yiu-Kay Lai
Tun-Wen Pai
Margaret Dah-Tsyr Chang
Contributors: 國立臺灣海洋大學:資訊工程學系
Date: 2013
Issue Date: 2017-01-16T05:40:38Z
Publisher: BioMed Research International
Abstract: Abstract: Human ribonucleases A (hRNaseA) superfamily consists of thirteen members with high-structure similarities but exhibits divergent physiological functions other than RNase activity. Evolution of hRNaseA superfamily has gained novel functions which may be preserved in a unique region or domain to account for additional molecular interactions. hRNase3 has multiple functions including ribonucleolytic, heparan sulfate (HS) binding, cellular binding, endocytic, lipid destabilization, cytotoxic, and antimicrobial activities. In this study, three putative multifunctional regions, 34RWRCK38 (HBR1), 75RSRFR79 (HBR2), and 101RPGRR105 (HBR3), of hRNase3 have been identified employing in silico sequence analysis and validated employing in vitro activity assays. A heparin binding peptide containing HBR1 is characterized to act as a key element associated with HS binding, cellular binding, and lipid binding activities. In this study, we provide novel insights to identify functional regions of hRNase3 that may have implications for all hRNaseA superfamily members.
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/40204
Appears in Collections:[資訊工程學系] 期刊論文

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