Analysis of high-affinity binding of protein kinase R to double-stranded RNA
about
Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocityDirect activation of ribosome-associated double-stranded RNA-dependent protein kinase (PKR) by deoxynivalenol, anisomycin and ricin: a new model for ribotoxic stress response inductionStructural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR.Analysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations.Activation of TLR3 induces osteogenic responses in human aortic valve interstitial cells through the NF-κB and ERK1/2 pathwaysExosomes from HIV-1-infected Cells Stimulate Production of Pro-inflammatory Cytokines through Trans-activating Response (TAR) RNAActivation of PKR by short stem-loop RNAs containing single-stranded arms.Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Double-stranded RNA upregulates the expression of inflammatory mediators in human aortic valve cells through the TLR3-TRIF-noncanonical NF-κB pathway.Functional peptides for siRNA delivery.Regulation of PKR by RNA: formation of active and inactive dimers.Role of the Interdomain Linker in RNA-Activated Protein Kinase ActivationInteraction of PKR with single-stranded RNAImpact of the structural integrity of the three-way junction of adenovirus VAI RNA on PKR inhibition.The RIG-I-like receptor LGP2 inhibits Dicer-dependent processing of long double-stranded RNA and blocks RNA interference in mammalian cells.
P2860
Q34193963-9CAF7EBD-0206-4B9D-A25C-37D93DE5E7DBQ34792629-1B5EC6B4-8D21-4AC6-86AF-F73DBA5B8CB2Q35050656-DF1ECF82-A9FB-4A2F-8930-72507649CC30Q35073088-F873BE61-CEEC-4467-B62A-9E6D62793105Q35197529-76B1C328-2606-4B1D-8935-896F316A716EQ36466170-EB6EF1A8-35AD-4214-97B0-199D0E1D0CBFQ37015864-9DEB95D3-DB94-454E-9E4A-83B00D32E91EQ37652771-CE024EC7-BF4B-48DA-A5D0-6C93EEE658B7Q38644638-3F240785-3F29-45C6-9798-297DA3FC01FBQ38722969-80FB8F0C-431F-45D9-ABE3-97D68E0BD7A8Q38928987-EC1AAD61-4962-40B4-9259-7BD2D26380A8Q40406915-37C4A2D0-FD68-46D0-8706-503FB5948740Q41041212-373BDFD9-23E2-4820-96E7-DDE2F17459E7Q41968360-C3F3A736-F350-4979-BA73-DF5D5B2D8642Q47425918-7066A82D-ADC2-4F66-ACDA-FC6E8AC5B75BQ47551178-C527332F-70AB-4E25-B39D-8688A9376832
P2860
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@ast
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@en
type
label
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@ast
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@en
prefLabel
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@ast
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@en
P2093
P2860
P356
P1433
P1476
Analysis of high-affinity binding of protein kinase R to double-stranded RNA
@en
P2093
Bushra Husain
Ishita Mukerji
James L Cole
P2860
P304
P356
10.1021/BI301226H
P407
P577
2012-10-26T00:00:00Z