Structural basis for the control of translation initiation during stress - Wikidata - wikimedia - TriplyDB

Structural basis for the control of translation initiation during stress

Structural basis for the control of translation initiation during stress

http://www.wikidata.org/entity/Q28289449

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Restoration of weak phase-contrast images recorded with a high degree of defocus: the "twin image" problem associated with CTF correction L11 domain rearrangement upon binding to RNA and thiostrepton studied by NMR spectroscopy Structural Aspects of RbfA Action during Small Ribosomal Subunit Assembly Cryo-EM study of the spinach chloroplast ribosome reveals the structural and functional roles of plastid-specific ribosomal proteins The structure of the eukaryotic ribosome at 3.0 Å resolution Structure ofVibrio choleraeribosome hibernation promoting factor The initiation of mammalian protein synthesis and mRNA scanning mechanism How Hibernation Factors RMF, HPF, and YfiA Turn Off Protein Synthesis Ribosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coli Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ Lactococcus lactis YfiA is necessary and sufficient for ribosome dimerization A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography Simulation of modulated protein crystal structure and diffraction data in a supercell and in superspace.Mass spectrometry of hydrogen/deuterium exchange in 70S ribosomal proteins from E. coli.Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting.Large-scale analysis of post-translational modifications in E. coli under glucose-limiting conditions.PSRP1 is not a ribosomal protein, but a ribosome-binding factor that is recycled by the ribosome-recycling factor (RRF) and elongation factor G (EF-G).Natural selection retains overrepresented out-of-frame stop codons against frameshift peptides in prokaryotes.Structural updates of alignment of protein domains and consequences on evolutionary models of domain superfamilies Comparative genomics and transcriptomics of trait-gene association The bacterial translation stress response.The Listeria monocytogenes hibernation-promoting factor is required for the formation of 100S ribosomes, optimal fitness, and pathogenesis.Proteomics of arsenic stress in the gram-positive organism Exiguobacterium sp. PS NCIM 5463.Characterization of hibernating ribosomes in mammalian cells.Long-term survival of Borrelia burgdorferi lacking the hibernation promotion factor homolog in the unfed tick vector.Structure of the Bacillus subtilis hibernating 100S ribosome reveals the basis for 70S dimerization.Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems.Review on bacterial stress topics.The weird and wonderful world of bacterial ribosome regulation.Ribosome hibernation factor promotes Staphylococcal survival and differentially represses translation Identification of a new endogenous metabolite and the characterization of its protein interactions through an immobilization approach.Comprehensive analysis of phosphorylated proteins of Escherichia coli ribosomes.Adaptation of enteropathogenic Yersinia to low growth temperature.One-bead coarse-grained model for RNA dynamics.Role of the ribosome-associated protein PY in the cold-shock response of Escherichia coli.Resuscitation of Pseudomonas aeruginosa from dormancy requires hibernation promoting factor (PA4463) for ribosome preservation.The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF.Cryo-EM structure of the spinach chloroplast ribosome reveals the location of plastid-specific ribosomal proteins and extensions.The role of ribosome recycling factor in dissociation of 70S ribosomes into subunits.

P2860

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P2860

Structural basis for the control of translation initiation during stress

http://www.wikidata.org/entity/Q28289449

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2004 nî lūn-bûn

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2004 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2004年の論文

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2004年論文

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2004年论文

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Structural basis for the control of translation initiation during stress

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Nature Structural & Molecular Biology

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Structural basis for the control of translation initiation during stress

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Antón Vila-Sanjurjo

http://www.w3.org/2001/XMLSchema#string

Barbara-S Schuwirth

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Cathy W Hau

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Jamie H D Cate

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P2860

Tools for the automatic identification and classification of RNA base pairs

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Structure of the 30S ribosomal subunit

Crystal structure of an initiation factor bound to the 30S ribosomal subunit

Crystal structure of the ribosome at 5.5 A resolution

The path of messenger RNA through the ribosome

Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold

Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli

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