Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.
about
Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelinInteraction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2Rotavirus non-structural proteins: structure and functionRotavirus viroplasm fusion and perinuclear localization are dynamic processes requiring stabilized microtubulesThe Isoform of Protein Kinase CKI Is Responsible for Hepatitis C Virus NS5A HyperphosphorylationThe flaviviral methyltransferase is a substrate of Casein Kinase 1Reconciliation of rotavirus temperature-sensitive mutant collections and assignment of reassortment groups D, J, and K to genome segmentsNew tags for recombinant protein detection and O-glycosylation reporters.Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication.The formation of viroplasm-like structures by the rotavirus NSP5 protein is calcium regulated and directed by a C-terminal helical domainRotavirus replication is correlated with S/G2 interphase arrest of the host cell cycleWhole genome sequence and phylogenetic analyses reveal human rotavirus G3P[3] strains Ro1845 and HCR3A are examples of direct virion transmission of canine/feline rotaviruses to humans.An ATPase activity associated with the rotavirus phosphoprotein NSP5.Phosphorylation events during viral infections provide potential therapeutic targets.Phosphoproteomic analysis reveals the importance of kinase regulation during orbivirus infection.Heterologous expression of antigenic peptides in Bacillus subtilis biofilms.Mammalian casein kinase 1alpha and its leishmanial ortholog regulate stability of IFNAR1 and type I interferon signaling.Rotavirus NSP1 Requires Casein Kinase II-Mediated Phosphorylation for Hijacking of Cullin-RING Ligases.Hyperphosphorylation of the rotavirus NSP5 protein is independent of serine 67, [corrected] NSP2, or [corrected] the intrinsic insolubility of NSP5 is regulated by cellular phosphatases.A novel form of rotavirus NSP2 and phosphorylation-dependent NSP2-NSP5 interactions are associated with viroplasm assembly.The viral transactivator HBx protein exhibits a high potential for regulation via phosphorylation through an evolutionarily conserved mechanism.Fusion of tags induces spurious phosphorylation of rotavirus NSP5.Plasmodesmal-associated protein kinase in tobacco and Arabidopsis recognizes a subset of non-cell-autonomous proteins.Identification of a small molecule that compromises the structural integrity of viroplasms and rotavirus double-layered particles.Molecular characterization of the porcine group A rotavirus NSP2 and NSP5/6 genes from São Paulo State, Brazil, in 2011/12.Casein kinase 1α: biological mechanisms and theranostic potential.
P2860
Q24654811-F3DCF139-1EE4-4506-A6F3-D733FAFB2A40Q24672464-875D60AF-BDFD-4F02-8665-6178D9602B1EQ27027535-AE4E0DF5-EED0-41EF-B677-84BBBE8034FEQ27313339-3FFD2E5D-5352-47E0-9B44-6FE76778C054Q27477609-356CC173-CC0F-4FF5-A5B9-755049C49786Q27490519-6C8BE10D-5E54-4145-946A-FA75377A8C2EQ28743106-1927E236-8A1A-40AB-963C-A3EF6333E8B4Q30815323-AF8886D5-DDE8-4456-9558-17DB6E055915Q35139285-54E55E05-EFD2-40D3-80EA-D7873C6F6B1DQ36315068-DB20E73D-D850-451E-B57F-413ECFE4F974Q36407402-FD6F236D-F195-4E5E-A89A-A3C95529212FQ36953775-A5389B07-C459-4076-B326-99CF7A54B052Q37242950-4F812BE6-0911-46B3-A2BC-9B1F5103D0C0Q37960427-1109F23A-506B-456A-8361-7ACCBACBE90CQ38603209-72EEACD4-EF58-4B41-B7EE-9599A28CDC14Q39499097-2879F090-8266-4317-A5AF-28F96692CFC6Q39791119-FC44BFCC-C178-42B4-B014-AB3EC104B948Q40066025-C0EB860A-A1C8-47F2-B30B-40EADFD4041CQ40324521-70A87360-2E05-4036-84A6-8F05A6BA313EQ41909023-092DF30D-E0A8-4687-BCE2-8F7464BE82C2Q41997275-7EC47A84-9107-42DC-B09D-C48372FFBAC3Q43156418-0761BF47-5ABA-477A-A091-C7FC23BF8A29Q46073381-8011690D-64C6-4394-8037-A9206606C198Q47344559-11A5E5E4-2726-4204-BAB8-41A9BCC533A1Q51867016-E457C66E-2D6A-4653-BF4C-41CA9E00DA9EQ54940982-1CFE5CAE-03C8-47B0-97A6-5844A0DEEC83
P2860
Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@en
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@nl
type
label
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@en
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@nl
prefLabel
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@en
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@nl
P2093
P2860
P356
P1476
Uncoupling substrate and activ ...... tial for hyperphosphorylation.
@en
P2093
Bartosz Muszynski
Germaine Jacob
Jorge E Allende
Oscar R Burrone
P2860
P304
16304-16309
P356
10.1073/PNAS.0406691101
P407
P577
2004-11-01T00:00:00Z