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Structures of translationally inactive mammalian ribosomes
by
Murray, Jason
, Yip, Matthew CJ
, Brown, Alan
, Baird, Matthew R
, Shao, Sichen
in
Amino Acid Sequence
/ Anemia
/ Animals
/ Binding Sites
/ Biochemistry
/ Biological response modifiers
/ Blood
/ Brown, Alan
/ Cell differentiation
/ Datasets
/ EDTA
/ electron cryomicroscopy
/ Erythrocytes
/ Gene expression
/ Genes
/ HEK293 Cells
/ Hemoglobin
/ Humans
/ in vitro reconstitution
/ Interferon
/ Kinases
/ Mammals
/ Mammals - metabolism
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Messenger RNA
/ Models, Molecular
/ Molecular Conformation
/ Mutation
/ Novels
/ Peptide Elongation Factor 2 - metabolism
/ Physiological aspects
/ Protein Binding
/ Protein Biosynthesis
/ Protein interaction
/ Proteins
/ Rabbits
/ Reticulocytes
/ Reticulocytes - metabolism
/ ribosome
/ Ribosomes
/ Ribosomes - metabolism
/ Ribosomes - ultrastructure
/ RNA
/ RNA, Transfer - metabolism
/ RNA-Binding Proteins - chemistry
/ RNA-Binding Proteins - metabolism
/ Structural Biology and Molecular Biophysics
/ Structure (Literature)
/ Transfer RNA
/ Translation
/ Translation (Genetics)
/ Translations
/ tRNA
2018
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Structures of translationally inactive mammalian ribosomes
by
Murray, Jason
, Yip, Matthew CJ
, Brown, Alan
, Baird, Matthew R
, Shao, Sichen
in
Amino Acid Sequence
/ Anemia
/ Animals
/ Binding Sites
/ Biochemistry
/ Biological response modifiers
/ Blood
/ Brown, Alan
/ Cell differentiation
/ Datasets
/ EDTA
/ electron cryomicroscopy
/ Erythrocytes
/ Gene expression
/ Genes
/ HEK293 Cells
/ Hemoglobin
/ Humans
/ in vitro reconstitution
/ Interferon
/ Kinases
/ Mammals
/ Mammals - metabolism
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Messenger RNA
/ Models, Molecular
/ Molecular Conformation
/ Mutation
/ Novels
/ Peptide Elongation Factor 2 - metabolism
/ Physiological aspects
/ Protein Binding
/ Protein Biosynthesis
/ Protein interaction
/ Proteins
/ Rabbits
/ Reticulocytes
/ Reticulocytes - metabolism
/ ribosome
/ Ribosomes
/ Ribosomes - metabolism
/ Ribosomes - ultrastructure
/ RNA
/ RNA, Transfer - metabolism
/ RNA-Binding Proteins - chemistry
/ RNA-Binding Proteins - metabolism
/ Structural Biology and Molecular Biophysics
/ Structure (Literature)
/ Transfer RNA
/ Translation
/ Translation (Genetics)
/ Translations
/ tRNA
2018
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Do you wish to request the book?
Structures of translationally inactive mammalian ribosomes
by
Murray, Jason
, Yip, Matthew CJ
, Brown, Alan
, Baird, Matthew R
, Shao, Sichen
in
Amino Acid Sequence
/ Anemia
/ Animals
/ Binding Sites
/ Biochemistry
/ Biological response modifiers
/ Blood
/ Brown, Alan
/ Cell differentiation
/ Datasets
/ EDTA
/ electron cryomicroscopy
/ Erythrocytes
/ Gene expression
/ Genes
/ HEK293 Cells
/ Hemoglobin
/ Humans
/ in vitro reconstitution
/ Interferon
/ Kinases
/ Mammals
/ Mammals - metabolism
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Messenger RNA
/ Models, Molecular
/ Molecular Conformation
/ Mutation
/ Novels
/ Peptide Elongation Factor 2 - metabolism
/ Physiological aspects
/ Protein Binding
/ Protein Biosynthesis
/ Protein interaction
/ Proteins
/ Rabbits
/ Reticulocytes
/ Reticulocytes - metabolism
/ ribosome
/ Ribosomes
/ Ribosomes - metabolism
/ Ribosomes - ultrastructure
/ RNA
/ RNA, Transfer - metabolism
/ RNA-Binding Proteins - chemistry
/ RNA-Binding Proteins - metabolism
/ Structural Biology and Molecular Biophysics
/ Structure (Literature)
/ Transfer RNA
/ Translation
/ Translation (Genetics)
/ Translations
/ tRNA
2018
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Structures of translationally inactive mammalian ribosomes
Journal Article
Structures of translationally inactive mammalian ribosomes
2018
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Overview
The cellular levels and activities of ribosomes directly regulate gene expression during numerous physiological processes. The mechanisms that globally repress translation are incompletely understood. Here, we use electron cryomicroscopy to analyze inactive ribosomes isolated from mammalian reticulocytes, the penultimate stage of red blood cell differentiation. We identify two types of ribosomes that are translationally repressed by protein interactions. The first comprises ribosomes sequestered with elongation factor 2 (eEF2) by SERPINE mRNA binding protein 1 (SERBP1) occupying the ribosomal mRNA entrance channel. The second type are translationally repressed by a novel ribosome-binding protein, interferon-related developmental regulator 2 (IFRD2), which spans the P and E sites and inserts a C-terminal helix into the mRNA exit channel to preclude translation. IFRD2 binds ribosomes with a tRNA occupying a noncanonical binding site, the ‘Z site’, on the ribosome. These structures provide functional insights into how ribosomal interactions may suppress translation to regulate gene expression.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ Anemia
/ Animals
/ Biological response modifiers
/ Blood
/ Datasets
/ EDTA
/ Genes
/ Humans
/ Kinases
/ Mammals
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Mutation
/ Novels
/ Peptide Elongation Factor 2 - metabolism
/ Proteins
/ Rabbits
/ ribosome
/ RNA
/ RNA-Binding Proteins - chemistry
/ RNA-Binding Proteins - metabolism
/ Structural Biology and Molecular Biophysics
/ tRNA
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