Identifying protein phosphorylation sites with kinase substrate specificity on human viruses.
about
Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic StrategiesTranscriptomic analysis of human norovirus NS1-2 protein highlights a multifunctional role in murine monocytesAn intelligent system for identifying acetylated lysine on histones and nonhistone proteinsViralPhos: incorporating a recursively statistical method to predict phosphorylation sites on virus proteins.Incorporating substrate sequence motifs and spatial amino acid composition to identify kinase-specific phosphorylation sites on protein three-dimensional structures.GSHSite: exploiting an iteratively statistical method to identify s-glutathionylation sites with substrate specificityCharacterization and identification of protein O-GlcNAcylation sites with substrate specificity.Single nucleoprotein residue modulates arenavirus replication complex formation.A new scheme to discover functional associations and regulatory networks of E3 ubiquitin ligases.UbiSite: incorporating two-layered machine learning method with substrate motifs to predict ubiquitin-conjugation site on lysines.In-depth proteomic analysis of Varroa destructor: Detection of DWV-complex, ABPV, VdMLV and honeybee proteins in the miteInvestigation and identification of protein carbonylation sites based on position-specific amino acid composition and physicochemical features.dbPTM 2016: 10-year anniversary of a resource for post-translational modification of proteinsDbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications.Involvement of the cellular phosphatase DUSP1 in vaccinia virus infection.RegPhos 2.0: an updated resource to explore protein kinase-substrate phosphorylation networks in mammals.MDD-Palm: Identification of protein S-palmitoylation sites with substrate motifs based on maximal dependence decomposition.A complex signaling network involving protein kinase CK2 is required for hepatitis C virus core protein-mediated modulation of the iron-regulatory hepcidin gene expression.UbiNet: an online resource for exploring the functional associations and regulatory networks of protein ubiquitylation.MDD-SOH: exploiting maximal dependence decomposition to identify S-sulfenylation sites with substrate motifs.MDD-carb: a combinatorial model for the identification of protein carbonylation sites with substrate motifs.
P2860
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P2860
Identifying protein phosphorylation sites with kinase substrate specificity on human viruses.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Identifying protein phosphoryl ...... specificity on human viruses.
@ast
Identifying protein phosphoryl ...... specificity on human viruses.
@en
type
label
Identifying protein phosphoryl ...... specificity on human viruses.
@ast
Identifying protein phosphoryl ...... specificity on human viruses.
@en
prefLabel
Identifying protein phosphoryl ...... specificity on human viruses.
@ast
Identifying protein phosphoryl ...... specificity on human viruses.
@en
P2093
P2860
P1433
P1476
Identifying protein phosphoryl ...... specificity on human viruses.
@en
P2093
Cheng-Tsung Lu
Chiu-Yun Chiang
Kai-Yao Huang
Min-Gang Su
Neil Arvin Bretaña
Shun-Long Weng
Tzong-Yi Lee
P2860
P304
P356
10.1371/JOURNAL.PONE.0040694
P407
P577
2012-07-23T00:00:00Z