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Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2016, Volume 113, Issue 36, pp. 10061 - 10066
The supramolecular cargo procollagen is loaded into coat protein complex II (COPII)-coated carriers at endoplasmic reticulum (ER) exit sites by the receptor... 
Coat protein | Procollagen | Vesicle traffic | COLLAGEN SECRETION | COMPLEX | PROTEIN | vesicle traffic | RECOGNITION | MECHANISM | MULTIDISCIPLINARY SCIENCES | TANGO1 | EXPORT | procollagen | coat protein | TRANSPORT | REVEALS | Vesicular Transport Proteins - metabolism | Humans | Endoplasmic Reticulum - metabolism | Aryl Hydrocarbon Receptor Nuclear Translocator - chemistry | Crystallography, X-Ray | Aryl Hydrocarbon Receptor Nuclear Translocator - metabolism | Neoplasm Proteins - metabolism | Antigens, Neoplasm - chemistry | Antigens, Neoplasm - metabolism | Protein Interaction Domains and Motifs | Neoplasm Proteins - genetics | Binding Sites | COP-Coated Vesicles - genetics | Recombinant Proteins - metabolism | Antigens, Neoplasm - genetics | Protein Conformation, alpha-Helical | Gene Expression | Procollagen - genetics | Procollagen - chemistry | Vesicular Transport Proteins - genetics | COP-Coated Vesicles - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Vesicular Transport Proteins - chemistry | Procollagen - metabolism | Recombinant Proteins - genetics | Monomeric GTP-Binding Proteins - genetics | COP-Coated Vesicles - chemistry | Amino Acid Motifs | Protein Transport | Monomeric GTP-Binding Proteins - metabolism | Protein Conformation, beta-Strand | Monomeric GTP-Binding Proteins - chemistry | Protein Binding | Aryl Hydrocarbon Receptor Nuclear Translocator - genetics | Biological Sciences
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 4/2009, Volume 185, Issue 2, pp. 305 - 321
Autophagy, an intracellular degradative pathway, maintains cell homeostasis under normal and stress conditions. Nascent double-membrane autophagosomes... 
Starvation | Transferrins | 3T3 cells | Small interfering RNA | HeLa cells | Antibodies | CHO cells | Endosomes | Golgi apparatus | P branes | CORE MACHINERY | TRANSPORT | UNFOLDED PROTEIN RESPONSE | MULTIVESICULAR BODIES | MEMBRANE | EPSILON-COP | ENDOCYTIC PATHWAYS | BETA-COP | CELL MUTANT | GOLGI-COMPLEX | CELL BIOLOGY | Mannose-Binding Lectins - metabolism | RNA, Small Interfering - genetics | Membrane Glycoproteins - metabolism | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Humans | Ubiquitin - metabolism | Autophagy - physiology | Coat Protein Complex I - metabolism | Recombinant Fusion Proteins - metabolism | Endosomes - metabolism | Protein Subunits - metabolism | Lysosomal-Associated Membrane Protein 1 - genetics | Membrane Proteins - metabolism | Protein Subunits - genetics | Biomarkers - metabolism | Cell Line | Membrane Proteins - genetics | Lysosomal-Associated Membrane Protein 2 - genetics | Phagosomes - metabolism | Ubiquitin - genetics | Coat Protein Complex I - genetics | Membrane Glycoproteins - genetics | Animals | Mannose-Binding Lectins - genetics | Adaptor Proteins, Signal Transducing - genetics | Recombinant Fusion Proteins - genetics | Golgi Apparatus - metabolism | Lysosomal-Associated Membrane Protein 1 - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Transferrin - metabolism | Lysosomal-Associated Membrane Protein 2 - metabolism | RNA, Small Interfering - metabolism | Ubiquitin | Gas vesicles | Physiological aspects | Research | Phagocytosis
Journal Article
FEBS Letters, ISSN 0014-5793, 11/2015, Volume 589, Issue 22, pp. 3343 - 3353
Autophagy is an intracellular degradation system that, as a basic mechanism it delivers cytoplasmic components to the lysosomes in order to maintain adequate... 
Autophagosome biogenesis | Rab GTPase | Autophagosome–lysosome fusion | Autophagy | SNAP receptor | GTP | PAS | PtdIns3P | sequestosome 1 | TRAPP | LRRK1 | mechanistic target of rapamycin | 200 kD focal adhesion kinase family-interacting protein | unc-51 like autophagy activating kinase 1 | GAS-containing autophagosome-like vacuoles | FYCO1 | guanosine diphosphate | GDP | WD-repeat-interacting phosphoinositide proteins | CMA | guanosine nucleotide exchange factor | STX | AMD | mTOR | LC3 | GTPase activating protein | N-ethyl-maleimide-sensitive factor | NSF | endoplasmic reticulum exit sites | chaperone-mediated autophagy | autophagy-related protein | phosphatidylinositol 3-phosphate | light chain 3 | coat protein complex II | phagophore assembly site | Huntington disease | PKA | GEF | cAMP-dependent protein kinase | transport protein particle | GAP | NS4B | soluble N-ethyl-maleimide attachment proteins | FIP200 | GAS | MVB | AMPK | HCV | PIK3C3 | ULK1 | ERES | epidermal growth factor | SQSTM1 | class III phosphatidylinositol 3 kinase | AMP-activated protein kinase | FYVE and coiled-coil domain-containing 1 | SNARE | vacuolar protein sorting | COPII | non-structural protein 4B | age-related macular degeneration of the eye | multivesicular body | VPS | leucine-rich repeat kinase 1 | recycling endosome | WIPI | EGF | guanosine triphosphate | molecular weight | SNAP | Syntaxin | Streptococcus | phosphatidylethanolamine | ATG | GcAVs | Group A | Hepatitis C virus | DFCP1 | endoplasmic reticulum | double FYVE domain-containing protein 1 | Autophagosome-lysosome fusion | OXIDATIVE STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLASMA-MEMBRANE | RAB24 GTPASE | SMALL GTPASE | NEGATIVE REGULATOR | CELL BIOLOGY | MEMBRANE-FUSION | PROMOTES AUTOPHAGY | LONGIN DOMAIN | BIOPHYSICS | MULTIVESICULAR BODIES | WIPI PROTEINS | rab GTP-Binding Proteins - metabolism | Animals | Proteins - metabolism | Biological Transport | Humans | Intracellular Space - metabolism | SNARE Proteins - metabolism | Proteins
Journal Article
Virus Research, ISSN 0168-1702, 2006, Volume 122, Issue 1, pp. 127 - 136
Journal Article
Cell, ISSN 0092-8674, 08/2003, Volume 114, Issue 4, pp. 497 - 509
Journal Article
Molecular Cell, ISSN 1097-2765, 2009, Volume 34, Issue 3, pp. 344 - 353
The YidC/Oxa1/Alb3 family of membrane proteins facilitates the insertion and assembly of membrane proteins in bacteria, mitochondria, and chloroplasts. Here we... 
RNA | PF3 COAT PROTEIN | PERIPLASMIC DOMAIN | ESCHERICHIA-COLI YIDC | MEMBRANE-PROTEIN INSERTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SIGNAL RECOGNITION PARTICLE | ELECTRON-MICROSCOPY | ENDOPLASMIC-RETICULUM | CONDUCTING CHANNEL | SEC-INDEPENDENT FUNCTION | CELL BIOLOGY | Protein Biosynthesis | Bacterial Proteins - chemistry | Ribosomes - metabolism | Mitochondrial Proteins - genetics | Electron Transport Complex IV - chemistry | Electron Transport Complex IV - metabolism | Multiprotein Complexes - metabolism | Membrane Transport Proteins - genetics | Mitochondrial Proteins - metabolism | Protein Structure, Quaternary | Membrane Transport Proteins - metabolism | Cysteine - metabolism | Nuclear Proteins - genetics | Dimerization | Oxidation-Reduction | Bacterial Proteins - genetics | Models, Molecular | Escherichia coli Proteins - metabolism | Nuclear Proteins - metabolism | Cysteine - chemistry | Electron Transport Complex IV - genetics | Nuclear Proteins - chemistry | Membrane Transport Proteins - chemistry | SEC Translocation Channels | Ribosomes - genetics | Mitochondrial Proteins - chemistry | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Proteins - metabolism | Escherichia coli Proteins - chemistry | Cysteine | Crosslinked polymers | Ribosomal proteins | Water quality | Mitochondrial DNA | Monomers | Tunnels | Membrane proteins
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2010, Volume 107, Issue 14, pp. 6292 - 6297
Bluetongue virus (BTV) is transmitted by blood-feeding insects (Culicoides sp.) and causes hemorrhagic diseases in livestock. BTV is a nonenveloped,... 
Proteins | Capsid proteins | Double stranded RNA | Maps | Rotavirus | Viruses | Amino acids | Trimers | Infections | Bluetongue virus | Sialic acid-binding protein | dsRNA virus structure | Membrane penetration protein | Cryo-electron microscopy | CAPSID PROTEIN | RECONSTRUCTION | MULTIDISCIPLINARY SCIENCES | membrane penetration protein | HIV-1 GP41 | FUNCTIONAL-CHARACTERIZATION | RICE-DWARF-VIRUS | ATOMIC-STRUCTURE | ELECTRON CRYOMICROSCOPY | MEMBRANE-PENETRATION PROTEIN | CELL ENTRY | EXPRESSION | cryo-electron microscopy | sialic acid-binding protein | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Cricetinae | Viral Fusion Proteins - metabolism | Protein Structure, Secondary | Capsid Proteins - metabolism | Humans | Protein Multimerization | Bluetongue virus - chemistry | Models, Molecular | Molecular Sequence Data | N-Acetylneuraminic Acid - metabolism | Capsid Proteins - ultrastructure | Cryoelectron Microscopy | N-Acetylneuraminic Acid - chemistry | Animals | Viral Fusion Proteins - chemistry | Virus Replication | Capsid Proteins - chemistry | Protein Structure, Quaternary | Viral Fusion Proteins - ultrastructure | Bluetongue virus - metabolism | Binding Sites | RNA viruses | Usage | Viral proteins | Physiological aspects | Genetic aspects | Research | Electron microscopy | Structure | Health aspects | Transcription | Double-stranded RNA | Amino acid sequence | Data processing | Genomes | Hemorrhagic disease | Peptide mapping | Bluetongue | Capsids | Coats | Infection | Microscopy | Influenza | Virions | Cell adhesion | Coat protein | Livestock | Fusion protein | Gene mapping | Core particles | Sugar | Biological Sciences
Journal Article