Control of translational repression by protein-protein interactions.
about
Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2ASH1 mRNA localization in three acts.Crystal structure of the coat protein from the GA bacteriophage: model of the unassembled dimerDirect genetic selection of two classes of R17/MS2 coat proteins with altered capsid assembly properties and expanded RNA-binding activities.Real-time RNA profiling within a single bacteriumIsolation of viral coat protein mutants with altered assembly and aggregation properties.The RNA binding site of bacteriophage MS2 coat protein.Dynamical determinants of drug-inducible gene expression in a single bacterium.Complementation of RNA binding site mutations in MS2 coat protein heterodimers.MS2 coat protein mutants which bind Qbeta RNA.Mutations that increase the affinity of a translational repressor for RNA.Crystallization of the MS2 translational repressor alone and complexed to bromouridineEvidence that viral RNAs have evolved for efficient, two-stage packaging.Proteins binding to 5' untranslated region sites: a general mechanism for translational regulation of mRNAs in human and yeast cellsFixed and live visualization of RNAs in Drosophila oocytes and embryosA platform for actively loading cargo RNA to elucidate limiting steps in EV-mediated delivery.Tethering of proteins to RNAs by bacteriophage proteins.Alteration of the Saccharomyces cerevisiae COX2 mRNA 5'-untranslated leader by mitochondrial gene replacement and functional interaction with the translational activator protein PET111.RNA dynamics in live Escherichia coli cells.Application of live-cell RNA imaging techniques to the study of retroviral RNA trafficking.Non-encapsidation activities of the capsid proteins of positive-strand RNA viruses.Illuminating Messengers: An Update and Outlook on RNA Visualization in Bacteria.Evolved orthogonal ribosome purification for in vitro characterization.Structural studies of MS2 bacteriophage virus particle disassembly by nuclear magnetic resonance relaxation measurements.Probing sequence-specific RNA recognition by the bacteriophage MS2 coat protein.Minimally invasive determination of mRNA concentration in single living bacteria.Tethered Function Assays as Tools to Elucidate the Molecular Roles of RNA-Binding Proteins.Cotranslational coat protein-mediated inhibition of potyviral RNA translation.Structure-based design of supercharged, highly thermoresistant antibodies.Impact of chemical and structural anisotropy on the electrophoretic mobility of spherical soft multilayer particles: the case of bacteriophage MS2.Adaptation of Tri-molecular fluorescence complementation allows assaying of regulatory Csr RNA-protein interactions in bacteria.An integrated approach to extreme thermostabilization and affinity maturation of an antibody
P2860
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P2860
Control of translational repression by protein-protein interactions.
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Control of translational repression by protein-protein interactions.
@ast
Control of translational repression by protein-protein interactions.
@en
type
label
Control of translational repression by protein-protein interactions.
@ast
Control of translational repression by protein-protein interactions.
@en
prefLabel
Control of translational repression by protein-protein interactions.
@ast
Control of translational repression by protein-protein interactions.
@en
P2860
P356
P1476
Control of translational repression by protein-protein interactions.
@en
P2093
P2860
P304
P356
10.1093/NAR/20.7.1649
P407
P577
1992-04-01T00:00:00Z