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Nature, ISSN 0028-0836, 06/2015, Volume 522, Issue 7557, pp. 450 - 454
The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by... 
E3 LIGASE | SPINDLE CHECKPOINT | ANAPHASE-PROMOTING COMPLEX | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | MITOTIC REGULATION | EM STRUCTURE DETERMINATION | CRYO-EM | ELECTRON-MICROSCOPY | CONJUGATING ENZYME | CHAIN ELONGATION | Phosphorylation | Ubiquitin - ultrastructure | Cadherins - metabolism | Humans | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitin - metabolism | Cell Cycle Proteins - ultrastructure | Substrate Specificity | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Structure-Activity Relationship | Anaphase-Promoting Complex-Cyclosome - ultrastructure | Protein Subunits - metabolism | Ubiquitin-Conjugating Enzymes - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cell Cycle Proteins - chemistry | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Ubiquitination | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Cadherins - chemistry | Cytoskeletal Proteins - metabolism | Lysine - metabolism | Anaphase-Promoting Complex-Cyclosome - chemistry | Cadherins - ultrastructure | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Catalytic Domain | F-Box Proteins - metabolism | Apc3 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | F-Box Proteins - chemistry | Cell Cycle Proteins - metabolism | Ubiquitin - chemistry | Models, Molecular | Ubiquitin-Conjugating Enzymes - ultrastructure | Cytoskeletal Proteins - chemistry | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Cryoelectron Microscopy | F-Box Proteins - ultrastructure | Ubiquitin-Conjugating Enzymes - metabolism | Protein Binding | Protein Subunits - chemistry | Apc10 Subunit, Anaphase-Promoting Complex-Cyclosome - chemistry | Anaphase-Promoting Complex-Cyclosome - metabolism | Apc11 Subunit, Anaphase-Promoting Complex-Cyclosome - metabolism | Apc1 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Apc8 Subunit, Anaphase-Promoting Complex-Cyclosome - ultrastructure | Ubiquitin | Physiological aspects | Structure | Ubiquitin-proteasome system | Ligases | Proteins | Peptides | Molecular structure | Cyclin-dependent kinases | Cell division | Kinases | Gene expression
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 04/2010, Volume 285, Issue 17, pp. 12497 - 12503
Cry toxins produced by Bacillus thuringiensis have been recognized as pore-forming toxins whose primary action is to lyse midgut epithelial cells in their... 
LYMANTRIA-DISPAR | LARVAL MIDGUT | AMINOPEPTIDASE-N-RECEPTOR | CYT TOXINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DOMAIN-II | DELTA-ENDOTOXIN | HELIOTHIS-VIRESCENS | BRUSH-BORDER MEMBRANE | BINDING-PROTEINS | OLIGOMERIC PRE-PORE | Insecticides - chemistry | Bacillus thuringiensis - chemistry | Cadherins - metabolism | Hemolysin Proteins - genetics | Protein Multimerization | Alkaline Phosphatase - metabolism | Bacterial Proteins - chemistry | Manduca - genetics | Mutation, Missense | Hemolysin Proteins - chemistry | Bacillus thuringiensis - genetics | Endotoxins - chemistry | Alkaline Phosphatase - chemistry | Aminopeptidases - chemistry | Cadherins - chemistry | Larva - enzymology | Cadherins - genetics | Aminopeptidases - metabolism | Bacillus thuringiensis - physiology | Insect Proteins - metabolism | Endotoxins - metabolism | Protein Structure, Tertiary | Aminopeptidases - genetics | Alkaline Phosphatase - genetics | Endotoxins - genetics | Larva - metabolism | Bacterial Proteins - genetics | Insect Proteins - genetics | Animals | Insecticides - metabolism | Insect Proteins - chemistry | Protein Binding | Bacterial Proteins - metabolism | Hemolysin Proteins - metabolism | Manduca - enzymology | Index Medicus | Membrane Proteins | Protein Structure and Folding | Receptor Structure-Function | Bacterial Toxins | Receptor | Bacillus thuringiensis | Cry1Ab Toxin | Alkaline Phosphatase | Phosphatase | Aminopeptidase | Insect
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 2386 - 9
Cry1A insecticidal toxins bind sequentially to different larval gut proteins facilitating oligomerization, membrane insertion and pore formation. Cry1Ac... 
MANDUCA-SEXTA | TRICHOPLUSIA-NI | ALKALINE-PHOSPHATASE | CABBAGE-LOOPER | MULTIDISCIPLINARY SCIENCES | PRE-PORE | INSECT RESISTANCE | HELICOVERPA-ARMIGERA LARVAE | PORE FORMATION | FIELD-EVOLVED RESISTANCE | MODIFIED BT TOXINS | Insecticides - chemistry | Hemolysin Proteins - pharmacology | Microvilli - chemistry | Hemolysin Proteins - genetics | Protein Multimerization | Bacterial Proteins - chemistry | Cell-Derived Microparticles - chemistry | Hemolysin Proteins - chemistry | Cell Membrane - chemistry | Larva - drug effects | Endotoxins - chemistry | Biological Control Agents - chemistry | Protein Engineering | Multidrug Resistance-Associated Proteins - genetics | Cell Membrane - metabolism | Cell-Derived Microparticles - metabolism | Larva - chemistry | Biological Control Agents - metabolism | Insect Proteins - metabolism | Cell Membrane - drug effects | Endotoxins - metabolism | Endotoxins - genetics | Insecticide Resistance | Larva - metabolism | Bacterial Proteins - genetics | Multidrug Resistance-Associated Proteins - chemistry | Insect Proteins - genetics | Microvilli - drug effects | Bacterial Proteins - pharmacology | Manduca - drug effects | Animals | Insecticides - metabolism | Microvilli - metabolism | Insect Proteins - chemistry | Protein Isoforms | Protein Binding | Bacterial Proteins - metabolism | Mutation | Multidrug Resistance-Associated Proteins - metabolism | Endotoxins - pharmacology | Hemolysin Proteins - metabolism | Moths - drug effects | Oligomerization | Cry1Ac toxin | Membrane vesicles | Toxins | Cadherin | ABC transporter | Western blotting
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2009, Volume 106, Issue 38, pp. 16233 - 16238
Carbonic anhydrase (CA) IX is a plasma membrane-associated member of the α-CA enzyme family, which is involved in solid tumor acidification. It is a marker of... 
Enzymes | Molecules | Active sites | Memory interference | Crystals | Cell adhesion | Hypoxia | Dimers | Crystal structure | Tumors | CA-IX | ISOZYMES | PROTEIN-TYROSINE-PHOSPHATASES | MULTIDISCIPLINARY SCIENCES | RESOLUTION | INTRACELLULAR PH | EXTRACELLULAR DOMAIN | E-CADHERIN | PROTON-TRANSFER | HYPOXIA | REFINED STRUCTURE | Protons | Carbon Dioxide - chemistry | Carbonic Anhydrases - genetics | Humans | Protein Multimerization | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Carbonic Anhydrases - chemistry | Antigens, Neoplasm - chemistry | Carbonic Anhydrases - metabolism | Disulfides - chemistry | Enzyme Inhibitors - chemistry | Drug Design | Water - chemistry | Antigens, Neoplasm - metabolism | Bicarbonates - chemistry | Carbonic Anhydrase IX | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Antigens, Neoplasm - genetics | Catalytic Domain | Carbon Dioxide - metabolism | Enzyme Inhibitors - metabolism | Crystallization | Enzyme Inhibitors - pharmacology | Water - metabolism | Models, Molecular | Neoplasms - enzymology | Recombinant Proteins - chemistry | Neoplasms - drug therapy | Sequence Homology, Amino Acid | Bicarbonates - metabolism | Protein Conformation | Kinetics | Neoplasms - pathology | Hydrogen-Ion Concentration | Structure | Biological Sciences
Journal Article
Journal Article
CELL, ISSN 0092-8674, 05/2001, Volume 105, Issue 3, pp. 391 - 402
Journal Article
Biochemistry, ISSN 0006-2960, 02/2010, Volume 49, Issue 6, pp. 1236 - 1247
Usher syndrome is the major cause of deaf/blindness in the world. It is a genetic heterogeneous disorder, with nine genes already identified as causative for... 
HARMONIN USH1C | SYNDROME TYPE 1F | SENSORY HAIR-CELLS | MOLECULAR LINKS | MYOSIN-VIIA | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYNDROME-TYPE IIA | GENE-PRODUCTS | TIP-LINK | SYNDROME TYPE-1 | PHOTORECEPTOR CELLS | Protein Precursors - chemistry | Humans | Multiprotein Complexes - genetics | Nerve Tissue Proteins - chemistry | Multiprotein Complexes - biosynthesis | Trachea - ultrastructure | Cattle | Protein Isoforms - chemistry | Cadherins - chemistry | Carrier Proteins - chemistry | Cadherins - genetics | Trachea - chemistry | Extracellular Matrix Proteins - chemistry | Protein Precursors - genetics | Respiratory Mucosa - cytology | Trachea - cytology | Membrane Proteins - genetics | Extracellular Matrix Proteins - genetics | Cell Fractionation - methods | Recombinant Proteins - chemistry | Protein Structure, Tertiary - genetics | Recombinant Proteins - genetics | Nerve Tissue Proteins - genetics | Respiratory Mucosa - ultrastructure | Protein Transport - genetics | Carrier Proteins - genetics | Multiprotein Complexes - chemistry | Animals | Membrane Proteins - chemistry | Protein Isoforms - biosynthesis | Respiratory Mucosa - chemistry | Transport Vesicles - genetics | Transport Vesicles - chemistry | Mice | Receptors, G-Protein-Coupled - genetics | Receptors, G-Protein-Coupled - chemistry | Transport Vesicles - ultrastructure | Protein Isoforms - genetics | Proteins | Analysis | Physiological aspects | Photoreceptors | Chemical properties | Structure | Trachea
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3145 - 3157
A disintegrin and metalloprotease 10 (ADAM10) is a ubiquitously expressed transmembrane metalloprotease that cleaves the extracellular regions from its... 
ACTIVATION | ANGIOGENESIS | endothelial cell | INTEGRIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | COMPLEXES | CELL-SURFACE | shedding | cell surface enzyme | ADAM | ADHESION | MICRODOMAINS | TspanC8 | N-cadherin | tetraspanin | platelet | COMPONENT | metalloprotease | GPVI | DOMAINS | EXPRESSION | Endothelium, Vascular - cytology | Amyloid Precursor Protein Secretases - genetics | Human Umbilical Vein Endothelial Cells - metabolism | Humans | Tetraspanins - chemistry | Substrate Specificity | Recombinant Fusion Proteins - metabolism | Blood Platelets - cytology | Proteolysis | Human Umbilical Vein Endothelial Cells - cytology | Surface Properties | Cell Membrane - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Tetraspanins - genetics | Tetraspanins - metabolism | Peptide Fragments - genetics | Tetraspanin-29 - chemistry | Cell Line | Peptide Fragments - metabolism | ADAM Proteins - chemistry | Membrane Proteins - genetics | Cells, Cultured | ADAM10 Protein | Recombinant Fusion Proteins - chemistry | Amyloid Precursor Protein Secretases - chemistry | Protein Transport | Cell Membrane - enzymology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Peptide Fragments - chemistry | Animals | Membrane Proteins - chemistry | Blood Platelets - metabolism | Endothelium, Vascular - metabolism | Mice | Protein Processing, Post-Translational | Enzyme Activation | ADAM Proteins - genetics | Tetraspanin-29 - metabolism | Tetraspanin-29 - genetics | Cell Biology
Journal Article
Journal Article