Structure, function and evolution of the signal recognition particle. - Test2 - elhamkhani - TriplyDB

Structure, function and evolution of the signal recognition particle.

Structure, function and evolution of the signal recognition particle.

http://www.wikidata.org/entity/Q35174625

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Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages Exome sequencing identifies autosomal-dominant SRP72 mutations associated with familial aplasia and myelodysplasia A nomenclature for all signal recognition particle RNAs Novel non-coding RNAs in Dictyostelium discoideum and their expression during development The 5e motif of eukaryotic signal recognition particle RNA contains a conserved adenosine for the binding of SRP72 Structures of SRP54 and SRP19, the Two Proteins that Organize the Ribonucleic Core of the Signal Recognition Particle from Pyrococcus furiosus Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor Structural basis of signal sequence surveillance and selection by the SRP–FtsY complex Optimization of heavy chain and light chain signal peptides for high level expression of therapeutic antibodies in CHO cells Compositional and structural features related to thermal stability in the archaea SRP19 and SRP54 signal recognition particle proteins.Homodimerization of the G protein SRbeta in the nucleotide-free state involves proline cis/trans isomerization in the switch II region.Differential regulation of the TRAIL death receptors DR4 and DR5 by the signal recognition particle Human RAS superfamily proteins and related GTPases.Identification of amino acid residues in protein SRP72 required for binding to a kinked 5e motif of the human signal recognition particle RNA GTPases and the origin of the ribosome.Posttranslational protein modification in Archaea.Archaea signal recognition particle shows the way.A telomerase holoenzyme protein enhances telomerase RNA assembly with telomerase reverse transcriptase.Streptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2.Malachite green derivatives for two-photon RNA detection.Two strategically placed base pairs in helix 8 of mammalian signal recognition particle RNA are crucial for the SPR19-dependent binding of protein SRP54 MrpL36p, a highly diverged L31 ribosomal protein homolog with additional functional domains in Saccharomyces cerevisiae mitochondria.Chemical approaches for structure and function of RNA in postgenomic era.SRP meets the ribosome.The role of membranes and membrane trafficking in RNA localization.Identification of Non-Coding RNAs in the Candida parapsilosis Species Group.Noncanoncial signal recognition particle RNAs in a major eukaryotic phylum revealed by purification of SRP from the human pathogen Cryptococcus neoformans Regulation of Srpr Expression by miR-330-5p Controls Proliferation of Mouse Epidermal Keratinocyte Alu element-containing RNAs maintain nucleolar structure and function.Mutation of RNA Pol III subunit rpc2/polr3b Leads to Deficiency of Subunit Rpc11 and disrupts zebrafish digestive development.Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversities correlated with long disordered regions.The LiaFSR system regulates the cell envelope stress response in Streptococcus mutans.A nascent polypeptide domain that can regulate translation elongation.Conserved tertiary base pairing ensures proper RNA folding and efficient assembly of the signal recognition particle Alu domain.Golgi bypass: skirting around the heart of classical secretion.No-go decay: a quality control mechanism for RNA in translation.Cryo-electron microscopy of ribosomal complexes in cotranslational folding, targeting, and translocation.The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Anti-tumor effect of lentivirus-mediated gene transfer of alphastatin on human glioma.Structure of the E. coli signal recognition particle bound to a translating ribosome.

P2860

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P2860

Structure, function and evolution of the signal recognition particle.

http://www.wikidata.org/entity/Q35174625

description

2003 nî lūn-bûn

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2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Structure, function and evolution of the signal recognition particle.

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Structure, function and evolution of the signal recognition particle.

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label

Structure, function and evolution of the signal recognition particle.

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Structure, function and evolution of the signal recognition particle.

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prefLabel

Structure, function and evolution of the signal recognition particle.

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Structure, function and evolution of the signal recognition particle.

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The EMBO Journal

P1476

Structure, function and evolution of the signal recognition particle.

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P2093

Andreas Kuglstatter

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

Elena Menichelli

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

Kiyoshi Nagai

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

P2860

Getting on target: the archaeal signal recognition particle

Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting

RNA tertiary interactions in the large ribosomal subunit: the A-minor motif

The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane

Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein

The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor

Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP

Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding

Structure of the phylogenetically most conserved domain of SRP RNA.

Crystal structure of the ribonucleoprotein core of the signal recognition particle

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10.1093/EMBOJ/CDG337

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12853463

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165607

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