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
提出一种数据挖掘方法 MMHC来求解DNA序列模体。首先使用基于种子的错配聚类形成候选模体类,然后使用基于相对熵及聚类复杂度的深度优先判定(depth first determination,DFD)算法识别真正的模体类,最后使用保守区扫描法(conservation re...提出一种数据挖掘方法 MMHC来求解DNA序列模体。首先使用基于种子的错配聚类形成候选模体类,然后使用基于相对熵及聚类复杂度的深度优先判定(depth first determination,DFD)算法识别真正的模体类,最后使用保守区扫描法(conservation region scanning,CRS)及最大后验概率保值过滤法(MAP value-preservation filtering,MVPF)优化模体类。在两类DNA序列数据集上,将MMHC与三种经典的模体发现方法 MEME、AlignACE和SOMBRERO进行了对比试验。结果表明:对于大多数数据集,MMHC方法无论是在发现模体的可靠性及准确性方面,还是在反映背景种类的聚类结构方面,都明显优于三种经典的模体发现方法。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.
文摘提出一种数据挖掘方法 MMHC来求解DNA序列模体。首先使用基于种子的错配聚类形成候选模体类,然后使用基于相对熵及聚类复杂度的深度优先判定(depth first determination,DFD)算法识别真正的模体类,最后使用保守区扫描法(conservation region scanning,CRS)及最大后验概率保值过滤法(MAP value-preservation filtering,MVPF)优化模体类。在两类DNA序列数据集上,将MMHC与三种经典的模体发现方法 MEME、AlignACE和SOMBRERO进行了对比试验。结果表明:对于大多数数据集,MMHC方法无论是在发现模体的可靠性及准确性方面,还是在反映背景种类的聚类结构方面,都明显优于三种经典的模体发现方法。