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Journal Article
Journal Article
Journal Article
Nature (London), ISSN 0028-0836, 2014, Volume 505, Issue 7481, pp. 112 - 116
Eukaryotic ribosomes are assembled by a complex pathway that extends from the nucleolus to the cytoplasm and is powered by many energy-consuming enzymes(1-3).... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Potassium - metabolism | Ribosomes - metabolism | Cytoplasm - metabolism | Ribosomal Proteins - metabolism | GTP Phosphohydrolases - chemistry | Saccharomyces cerevisiae - metabolism | Ribosomes - secretion | Saccharomyces cerevisiae Proteins - secretion | Cell Nucleus - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Cell Nucleus - secretion | ATPases Associated with Diverse Cellular Activities | Ribosome Subunits, Large, Eukaryotic - chemistry | RNA-Binding Proteins - chemistry | Ribosomes - chemistry | Adenosine Triphosphatases - metabolism | Models, Molecular | Protein Structure, Tertiary - genetics | Saccharomyces cerevisiae Proteins - genetics | Mutation - genetics | Saccharomyces cerevisiae - cytology | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Genes, Lethal - genetics | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | RNA-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Biological research | Physiological aspects | Guanosine triphosphatase | Adenosine triphosphatase | Biology, Experimental | Proteins | Yeast | Atoms & subatomic particles | Biosynthesis | Mutation | Binding sites | Methods | Index Medicus
Journal Article
The Journal of biological chemistry, ISSN 0021-9258, 01/2016, Volume 291, Issue 3, pp. 1014 - 1027
The majority of biosynthetic secretory proteins initiate their journey through the endomembrane system from specific sub-domains of the endoplasmic reticulum.... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Vesicular Transport Proteins - metabolism | Caenorhabditis elegans Proteins - chemistry | Humans | Membrane Microdomains - ultrastructure | Endoplasmic Reticulum - ultrastructure | GTP Phosphohydrolases - chemistry | Caenorhabditis elegans - physiology | ras GTPase-Activating Proteins - genetics | Vesicular Transport Proteins - antagonists & inhibitors | RNA Interference | ras GTPase-Activating Proteins - metabolism | Enzyme Inhibitors - pharmacology | COP-Coated Vesicles - metabolism | Recombinant Proteins - chemistry | Guanylyl Imidodiphosphate - pharmacology | Receptor Protein-Tyrosine Kinases - metabolism | Monomeric GTP-Binding Proteins - antagonists & inhibitors | Caenorhabditis elegans - ultrastructure | GTP Phosphohydrolases - metabolism | GTP Phosphohydrolases - genetics | Models, Biological | Monomeric GTP-Binding Proteins - chemistry | GTPase-Activating Proteins - genetics | Mutation | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Membrane Microdomains - metabolism | Caenorhabditis elegans Proteins - metabolism | Endoplasmic Reticulum - metabolism | Guanosine Triphosphate - metabolism | GTP Phosphohydrolases - antagonists & inhibitors | GTPase-Activating Proteins - metabolism | Microscopy, Atomic Force | Organelle Shape - drug effects | Recombinant Proteins - metabolism | COP-Coated Vesicles - ultrastructure | GTPase-Activating Proteins - antagonists & inhibitors | Vesicular Transport Proteins - genetics | COP-Coated Vesicles - drug effects | Monomeric GTP-Binding Proteins - genetics | Animals | Caenorhabditis elegans - drug effects | Caenorhabditis elegans Proteins - antagonists & inhibitors | Monomeric GTP-Binding Proteins - metabolism | Receptor Protein-Tyrosine Kinases - genetics | Membrane Microdomains - drug effects | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Amino Acid Substitution | Index Medicus | COPII | membrane transport | endoplasmic reticulum (ER) | GTPase | membrane bilayer | Cell Biology
Journal Article
by Wang, X and Su, B and Lee, H.-g and Li, X and Perry, G and Smith, M. A and Zhu, X
The Journal of neuroscience, ISSN 1529-2401, 07/2009, Volume 29, Issue 28, pp. 9090 - 9103
Journal Article