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Molecular Cell, ISSN 1097-2765, 09/2016, Volume 63, Issue 5, pp. 781 - 795
Mutations in the human autophagy gene cause the multisystem disorder Vici syndrome. Here we demonstrated that EPG5 is a Rab7 effector that determines the... 
RAB effector | LC3 | autophagosome maturation | epg-5 | SNARE | MEMBRANE-FUSION | LYSOSOME FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MACHINERY | MECHANISMS | SYNTAXIN 17 | MATURATION | VESICLE | C. ELEGANS | HOPS COMPLEX | CELL BIOLOGY | Microtubule-Associated Proteins - genetics | Microtubule-Associated Proteins - metabolism | Humans | Cataract - pathology | Qb-SNARE Proteins - metabolism | R-SNARE Proteins - metabolism | Caenorhabditis elegans Proteins - metabolism | Qb-SNARE Proteins - genetics | rab GTP-Binding Proteins - genetics | Endosomes - metabolism | Lysosomes - metabolism | Qc-SNARE Proteins - metabolism | Agenesis of Corpus Callosum - genetics | Endosomes - ultrastructure | Qa-SNARE Proteins - genetics | Autophagy - genetics | Synaptosomal-Associated Protein 25 - genetics | rab GTP-Binding Proteins - metabolism | Agenesis of Corpus Callosum - metabolism | Amino Acid Sequence | Caenorhabditis elegans - metabolism | Membrane Fusion | Signal Transduction | Caenorhabditis elegans - genetics | R-SNARE Proteins - genetics | Gene Expression Regulation | Autophagosomes - metabolism | Cataract - metabolism | Agenesis of Corpus Callosum - pathology | Autophagosomes - ultrastructure | Lysosomes - ultrastructure | Proteins - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Proteins - metabolism | Qa-SNARE Proteins - metabolism | Protein Binding | Qc-SNARE Proteins - genetics | Cataract - genetics | Synaptosomal-Associated Protein 25 - metabolism | HeLa Cells | Caenorhabditis elegans Proteins - genetics | Yuan (China)
Journal Article
Nature, ISSN 0028-0836, 07/2015, Volume 523, Issue 7562, pp. 555 - 560
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 06/2016, Volume 41, Issue 6, pp. 478 - 490
Two types of sequences, proline-rich domains (PRDs) and the WASP-homology 2 (WH2) domain, are found in most actin filament nucleation and elongation factors... 
PROMOTING FACTOR | ATP-ACTIN | CORDON-BLEU | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | RICKETTSIA SCA2 | ARP2/3 COMPLEX | SYNDAPIN I | MUSCLE-CELLS | BACTERIAL EFFECTOR VOPL | FILAMENT NUCLEATION | Autoantigens - metabolism | Cytoskeletal Proteins - genetics | Actin-Related Protein 2-3 Complex - ultrastructure | Humans | Actins - metabolism | Fetal Proteins - metabolism | Autoantigens - genetics | Drosophila melanogaster - genetics | Actins - genetics | Drosophila melanogaster - metabolism | Actin-Related Protein 2-3 Complex - metabolism | Cell Nucleus - metabolism | Actins - chemistry | Cytoskeletal Proteins - metabolism | Microfilament Proteins - metabolism | Protein Interaction Domains and Motifs | Nuclear Proteins - genetics | Microfilament Proteins - genetics | Amino Acid Sequence | Microfilament Proteins - chemistry | Bacteria - metabolism | Actin Cytoskeleton - metabolism | Protein Structure, Secondary | Polymerization | Nuclear Proteins - metabolism | Autoantigens - chemistry | Cytoskeletal Proteins - chemistry | Nuclear Proteins - chemistry | Bacteria - genetics | Sequence Homology, Amino Acid | Sequence Alignment | Animals | Cell Nucleus - genetics | Fetal Proteins - genetics | Actin Cytoskeleton - ultrastructure | Fetal Proteins - chemistry | Physiological aspects | Muscle proteins | Actin | Protein-protein interactions | Protein binding
Journal Article
Molecular Cell, ISSN 1097-2765, 2005, Volume 20, Issue 6, pp. 939 - 949
The death-inducing signaling complex (DISC) comprising Fas, Fas-associated death domain (FADD), and caspase-8/10 is assembled via homotypic associations... 
RECEPTOR SIGNALS | APOPTOSIS | INDUCED-PROXIMITY MODEL | BIOCHEMISTRY & MOLECULAR BIOLOGY | NMR STRUCTURE | DEATH-EFFECTOR DOMAIN | CASPASE ACTIVATION | CONTAINING PROTEIN | SIGNALING COMPLEX DISC | CELL-DEATH | PYRIN DOMAIN | CELL BIOLOGY | Caspase 8 | Humans | Multiprotein Complexes | Molecular Sequence Data | Crystallography, X-Ray | Intracellular Signaling Peptides and Proteins - metabolism | fas Receptor - metabolism | Viral Proteins - metabolism | Death Domain Receptor Signaling Adaptor Proteins | Caspases - metabolism | Molluscum contagiosum virus - genetics | Caspase 10 | fas Receptor - genetics | Intracellular Signaling Peptides and Proteins - genetics | Amino Acid Sequence | Caspases - genetics | Viral Proteins - chemistry | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | Models, Molecular | Viral Proteins - genetics | Fas-Associated Death Domain Protein | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - metabolism | Tumor Necrosis Factor Receptor-Associated Peptides and Proteins - chemistry | Sequence Alignment | Animals | Intracellular Signaling Peptides and Proteins - chemistry | Adaptor Proteins, Signal Transducing - genetics | Molluscum contagiosum virus - chemistry | Protein Conformation | CASP8 and FADD-Like Apoptosis Regulating Protein | Apoptosis - physiology | Mutation | Adaptor Proteins, Signal Transducing - metabolism | Proteins | Oligomers | Structure | Crystals
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2016, Volume 64, Issue 2, pp. 236 - 250
Caspase-8 activation can be triggered by death receptor-mediated formation of the death-inducing signaling complex (DISC) and by the inflammasome adaptor ASC.... 
caspase-8 | DED | MC159 | cFLIP | DISC | Fas | death domain | FADD | vFLIP | filament | APOPTOSIS | ACTIVATION | IMMUNE-SYSTEM | INHIBITION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | UNIFIED MODEL | EFFECTOR DOMAIN | CELL-DEATH | CELL BIOLOGY | Death Domain Receptor Signaling Adaptor Proteins - chemistry | Apoptosis - drug effects | Cytoskeletal Proteins - genetics | Humans | Caspase 8 - metabolism | Caspase 8 - chemistry | CASP8 and FADD-Like Apoptosis Regulating Protein - chemistry | Death Domain Receptor Signaling Adaptor Proteins - genetics | Recombinant Fusion Proteins - metabolism | Viral Proteins - metabolism | Caspase 8 - genetics | Transfection | Cytoskeletal Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | CASP8 and FADD-Like Apoptosis Regulating Protein - metabolism | Death Effector Domain | Fas-Associated Death Domain Protein - genetics | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | CASP8 and FADD-Like Apoptosis Regulating Protein - genetics | Jurkat Cells | Viral Proteins - chemistry | Fas-Associated Death Domain Protein - metabolism | Viral Proteins - genetics | fas Receptor - pharmacology | Cytoskeletal Proteins - chemistry | Recombinant Fusion Proteins - chemistry | Plasmids - metabolism | Fas-Associated Death Domain Protein - chemistry | Cryoelectron Microscopy | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | CARD Signaling Adaptor Proteins | Plasmids - chemistry | Protein Binding | Recombinant Fusion Proteins - genetics | Death Domain Receptor Signaling Adaptor Proteins - metabolism | Autoimmunity | Medical colleges | Skin diseases | Molecular biology | Analysis | Index Medicus
Journal Article
The FEBS Journal, ISSN 1742-464X, 07/2016, Volume 283, Issue 14, pp. 2690 - 2700
B‐cell lymphoma 2 (BCL‐2) family proteins mediate mitochondrial apoptosis by regulating mitochondrial outer membrane permeabilization (MOMP), which leads to... 
pro‐apoptotic; sensitizer | direct activator | BH3‐only | derepressor | mitochondrial apoptosis | effector | mitochondrial outer membrane permeabilization | anti‐apoptotic | B‐cell lymphoma 2 | Derepressor | Anti-apoptotic | Mitochondrial outer membrane permeabilization | Pro-apoptotic; sensitizer | Mitochondrial apoptosis | Direct activator | Effector | B-cell lymphoma 2 | BH3-only | anti-apoptotic | pro-apoptotic; sensitizer | DNA-BINDING DOMAIN | MITOCHONDRIAL OUTER-MEMBRANE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROMOTE APOPTOSIS | DIRECT ACTIVATION | sensitizer | CELL-DEATH | BAX ACTIVATION | CHANGES CONFORMATION | pro-apoptotic | PROLYL ISOMERASE PIN1 | PEPTIDE COMPLEX | Signal Transduction | Tumor Suppressor Protein p53 - antagonists & inhibitors | Humans | Protein Multimerization | Tumor Suppressor Protein p53 - metabolism | bcl-2-Associated X Protein - metabolism | Models, Molecular | Permeability | Mitochondrial Membranes - metabolism | bcl-X Protein - chemistry | Proto-Oncogene Proteins c-bcl-2 - metabolism | Animals | Models, Biological | Protein Conformation | Proto-Oncogene Proteins c-bcl-2 - chemistry | Protein Interaction Domains and Motifs | Tumor Suppressor Protein p53 - chemistry | Apoptosis - physiology | bcl-X Protein - metabolism | Tumor proteins | Protein-protein interactions | Protein binding | Apoptosis | Proteins | Lymphomas
Journal Article
Cellular Signalling, ISSN 0898-6568, 2006, Volume 18, Issue 5, pp. 579 - 591
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2016, Volume 11, Issue 12, p. e0167145
RAS effectors specifically interact with the GTP-bound form of RAS in response to extracellular signals and link them to downstream signaling pathways. The... 
R-RAS | KRAS MUTATIONS | H-RAS | PHOSPHOINOSITIDE 3-OH KINASE | K-RAS | N-RAS | GTPASE-ACTIVATING PROTEINS | MULTIDISCIPLINARY SCIENCES | SWITCH I-REGION | PHOSPHOLIPASE-C-EPSILON | HYPERVARIABLE REGION | Proto-Oncogene Proteins p21(ras) - genetics | Humans | Phosphatidylinositol 3-Kinases - metabolism | GTP Phosphohydrolases - chemistry | ral Guanine Nucleotide Exchange Factor - chemistry | Proto-Oncogene Proteins p21(ras) - chemistry | Protein Domains | Carrier Proteins - chemistry | Membrane Proteins - metabolism | Proto-Oncogene Proteins p21(ras) - metabolism | Binding, Competitive | Amino Acid Sequence | Protein Structure, Secondary | Signal Transduction | Membrane Proteins - genetics | Phosphatidylinositol 3-Kinases - chemistry | Models, Molecular | Binding Sites - genetics | Monomeric GTP-Binding Proteins - genetics | ral Guanine Nucleotide Exchange Factor - genetics | Phosphatidylinositol 3-Kinases - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Carrier Proteins - metabolism | Class I Phosphatidylinositol 3-Kinases | GTP Phosphohydrolases - metabolism | Membrane Proteins - chemistry | Monomeric GTP-Binding Proteins - metabolism | GTP Phosphohydrolases - genetics | Monomeric GTP-Binding Proteins - chemistry | Protein Binding | Kinetics | ral Guanine Nucleotide Exchange Factor - metabolism | Structure | Analysis | Crystals | Protein binding | Binding | Fluorescence polarization | GTP | Hot spots | Fluorescence | Amino acids | Biochemistry | Kinases | Gene expression | K-Ras protein | Proteins | Studies | Signal transduction | Signaling | Cell growth | Next-generation sequencing | Isoforms | Cell cycle | Effectors | Mutation | Molecular biology | Cancer | Crystal structure | Structure-function relationships
Journal Article