ERK is involved in multiple cell signaling pathways through its interacting proteins. By </span><i><span style="font-size:12px;font-family:Verdana;">in</span></i> <i><s...ERK is involved in multiple cell signaling pathways through its interacting proteins. By </span><i><span style="font-size:12px;font-family:Verdana;">in</span></i> <i><span style="font-size:12px;font-family:Verdana;">silico</span></i><span style="font-size:12px;font-family:Verdana;"> analysis, earlier we have identified 22 putative ERK interacting proteins namely;ephrin type-B receptor 2 isoform 2 precursor (EPHB2), mitogen-activated protein kinase 1</span></span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:10pt;"><span style="font-size:12px;font-family:Verdana;">(MAPK1), interleukin-17 receptor D precursor (IL17RD), WD repeat domain containing 83 (WDR83), </span><span style="font-size:12px;font-family:Verdana;">tescalcin (Tesc), mitogen-activated protein kinase kinase kinase 4 (MAPP3K4),</span><span style="font-size:12px;font-family:Verdana;"> kinase suppressor of Ras2 (KSR2), mitogen-activated protein kinase kinase 6 (MAP3K6), UL16 binding protein 2 (ULBP2), UL16 binding protein 1 (ULBP1), dual specificity phosphatase 14 (DUSP14), dual specificity phosphatase 6 (DUSP6), hyaluronan-mediated motility receptor (RHAMM), kinase D interacting substrate of 220</span></span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:12px;font-family:Verdana;">kDa (KININS220), membrane-associated guanylate kinase (MAGI3), phosphoprotein enriched in astrocytes 15</span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:12px;font-family:Verdana;">(PEA15), typtophenyl-tRNA synthetase, cytoplasmic (WARS), dual specificity phosphatase 9 (DUSP9), mitogen-activated protein kinase kinase kinase 1</span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:12px;font-family:Verdana;">(MAP3K1), UL16 binding protein 3 (ULBP3), SLAM family member 7 isoform a precursor (SLAMMF7) and mitogen activated protein kinase kinase kinase 11 (MAP3K11) (</span><span "="" style="font-size:10pt;"><a href="file:///E:/%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2021/0225-wqs-%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89(1)/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89/7-1390595.docx#T1"><b><span color:#943634;"="" style="font-size: 12px;font-family: Verdana;">Table 1</span></b></a></span><span "="" style="font-size:10pt;"><span style="font-size:12px;font-family:Verdana;">). However, prediction of secondary structure and domain/motif present in aforementioned ERK interacting proteins is not studied. In this paper, </span><i><span style="font-size:12px;font-family:Verdana;">in</span></i></span><i><span style="font-size:10.0pt;font-family:;" "=""> </span><span style="font-size:12px;font-family:Verdana;" "="">silico</span></i><span "="" style="font-size:12px;font-family:Verdana;"> prediction of secondary structure of ERK interacting proteins was done by SOPMA and motif/domain identification using motif search. Briefly, SOPMA predicted higher random coil and alpha helix percentage in these proteins (</span><span "="" style="font-size:10pt;"><a href="file:///E:/%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2021/0225-wqs-%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89(1)/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89/7-1390595.docx#T2"><b><span color:#943634;"="" style="font-size: 12px;font-family: Verdana;">Table 2</span></b></a></span><span "="" style="font-size:12px;font-family:Verdana;">)</span><span "="" style="font-size:12px;font-family:Verdana;"> and</span><span "="" style="font-size:12px;font-family:Verdana;"> motif scan predicted serine/threonine kinases active site signature and protein kinase ATP binding region in majority of ERK interacting proteins. Moreover, few have commonly dual specificity protein phosphatase family and tyrosine specific protein phosphatase domains (</span><span "="" style="font-size:10pt;"><a href="file:///E:/%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2021/0225-wqs-%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89(1)/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89/7-1390595.docx#T3"><b><span color:#943634;"="" style="font-size: 12px;font-family: Verdana;">Table 3</span></b></a></span><span "="" style="font-size:12px;font-family:Verdana;">). Such study may be helpful to design engineered molecules for regulating ERK dependent pathways in disease condition.展开更多
Percolating composites with negative permittivity can be promising candidates for metamaterials.Herein,novel all-organic composite films containing of random coil polypyrrole(PPy)and poly(-vinylidene fluoride)(PVDF)ar...Percolating composites with negative permittivity can be promising candidates for metamaterials.Herein,novel all-organic composite films containing of random coil polypyrrole(PPy)and poly(-vinylidene fluoride)(PVDF)are fabricated via a solution casting method.The random coil PPy is prepared by oxidative template assembly approach for the first time.The experimental result indicates that the negative permittivity is easily adjusted through controlling the random coil PPy contents.Especially,the random coil PPy contents exceeded 7 wt% the negative permittivity appear attributed to the formation of 3D interconnected PPy network.This facile approach not only opens a new way to preparing negative permittivity of all-organic composite films,but also points out a route to facilitate the practical applications of metamaterials.展开更多
文摘ERK is involved in multiple cell signaling pathways through its interacting proteins. By </span><i><span style="font-size:12px;font-family:Verdana;">in</span></i> <i><span style="font-size:12px;font-family:Verdana;">silico</span></i><span style="font-size:12px;font-family:Verdana;"> analysis, earlier we have identified 22 putative ERK interacting proteins namely;ephrin type-B receptor 2 isoform 2 precursor (EPHB2), mitogen-activated protein kinase 1</span></span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:10pt;"><span style="font-size:12px;font-family:Verdana;">(MAPK1), interleukin-17 receptor D precursor (IL17RD), WD repeat domain containing 83 (WDR83), </span><span style="font-size:12px;font-family:Verdana;">tescalcin (Tesc), mitogen-activated protein kinase kinase kinase 4 (MAPP3K4),</span><span style="font-size:12px;font-family:Verdana;"> kinase suppressor of Ras2 (KSR2), mitogen-activated protein kinase kinase 6 (MAP3K6), UL16 binding protein 2 (ULBP2), UL16 binding protein 1 (ULBP1), dual specificity phosphatase 14 (DUSP14), dual specificity phosphatase 6 (DUSP6), hyaluronan-mediated motility receptor (RHAMM), kinase D interacting substrate of 220</span></span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:12px;font-family:Verdana;">kDa (KININS220), membrane-associated guanylate kinase (MAGI3), phosphoprotein enriched in astrocytes 15</span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:12px;font-family:Verdana;">(PEA15), typtophenyl-tRNA synthetase, cytoplasmic (WARS), dual specificity phosphatase 9 (DUSP9), mitogen-activated protein kinase kinase kinase 1</span><span "="" style="font-size:10pt;"> </span><span "="" style="font-size:12px;font-family:Verdana;">(MAP3K1), UL16 binding protein 3 (ULBP3), SLAM family member 7 isoform a precursor (SLAMMF7) and mitogen activated protein kinase kinase kinase 11 (MAP3K11) (</span><span "="" style="font-size:10pt;"><a href="file:///E:/%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2021/0225-wqs-%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89(1)/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89/7-1390595.docx#T1"><b><span color:#943634;"="" style="font-size: 12px;font-family: Verdana;">Table 1</span></b></a></span><span "="" style="font-size:10pt;"><span style="font-size:12px;font-family:Verdana;">). However, prediction of secondary structure and domain/motif present in aforementioned ERK interacting proteins is not studied. In this paper, </span><i><span style="font-size:12px;font-family:Verdana;">in</span></i></span><i><span style="font-size:10.0pt;font-family:;" "=""> </span><span style="font-size:12px;font-family:Verdana;" "="">silico</span></i><span "="" style="font-size:12px;font-family:Verdana;"> prediction of secondary structure of ERK interacting proteins was done by SOPMA and motif/domain identification using motif search. Briefly, SOPMA predicted higher random coil and alpha helix percentage in these proteins (</span><span "="" style="font-size:10pt;"><a href="file:///E:/%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2021/0225-wqs-%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89(1)/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89/7-1390595.docx#T2"><b><span color:#943634;"="" style="font-size: 12px;font-family: Verdana;">Table 2</span></b></a></span><span "="" style="font-size:12px;font-family:Verdana;">)</span><span "="" style="font-size:12px;font-family:Verdana;"> and</span><span "="" style="font-size:12px;font-family:Verdana;"> motif scan predicted serine/threonine kinases active site signature and protein kinase ATP binding region in majority of ERK interacting proteins. Moreover, few have commonly dual specificity protein phosphatase family and tyrosine specific protein phosphatase domains (</span><span "="" style="font-size:10pt;"><a href="file:///E:/%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2021/0225-wqs-%E5%B7%A5%E4%BD%9C%E8%AE%B0%E5%BD%95/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89(1)/2%E6%9C%88%20WJNS11.1%20%E6%8F%92%E9%A1%B5%E7%A0%81%20%E4%BB%98%E5%96%9C%E4%BB%81%20%EF%BC%887%EF%BC%89/7-1390595.docx#T3"><b><span color:#943634;"="" style="font-size: 12px;font-family: Verdana;">Table 3</span></b></a></span><span "="" style="font-size:12px;font-family:Verdana;">). Such study may be helpful to design engineered molecules for regulating ERK dependent pathways in disease condition.
基金supported by the Ministry of Science and Technology of China through 973-project under Grant(2015CB654601)National Nature Science Foundation of China(51902167)+1 种基金Fund in Ningbo UniversityKey Laboratory of Engineering Dielectrics and Its Application(Harbin University of Science and Technology),Ministry of Education.
文摘Percolating composites with negative permittivity can be promising candidates for metamaterials.Herein,novel all-organic composite films containing of random coil polypyrrole(PPy)and poly(-vinylidene fluoride)(PVDF)are fabricated via a solution casting method.The random coil PPy is prepared by oxidative template assembly approach for the first time.The experimental result indicates that the negative permittivity is easily adjusted through controlling the random coil PPy contents.Especially,the random coil PPy contents exceeded 7 wt% the negative permittivity appear attributed to the formation of 3D interconnected PPy network.This facile approach not only opens a new way to preparing negative permittivity of all-organic composite films,but also points out a route to facilitate the practical applications of metamaterials.