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1. Full Text Critical Role for Asparagine Endopeptidase in Endocytic Toll-like Receptor Signaling in Dendritic Cells
by Sepulveda, Fernando E and Maschalidi, Sophia and Colisson, Renaud and Heslop, Lea and Ghirelli, Cristina and Sakka, Emna and Lennon-Duménil, Ana-Maria and Amigorena, Sebastian and Cabanie, Lucien and Manoury, Bénédicte
Immunity, ISSN 1074-7613, 2009, Volume 31, Issue 5, pp. 737 - 748
Intracellular Toll-like receptor 3 (TLR3), TLR7, and TLR9 localize in endosomes and recognize single-stranded RNA and nucleotides from viruses and bacteria.... 
MOLIMMUNO | CELLIMMUNO | ACTIVATION | CATHEPSIN-L | CPG-DNA | MICE | TOLL-LIKE-RECEPTOR-9 | INVARIANT CHAIN | INHIBITORS | IMMUNOLOGY | EXPRESSION | ANTIGEN | Animals | Signal Transduction | Cathepsins - metabolism | Cysteine Endopeptidases - genetics | Dendritic Cells - immunology | Mice | Toll-Like Receptor 9 - metabolism | Cysteine Endopeptidases - physiology | Mice, Knockout | Asparagine | Cysteine | Nucleotides | Dendritic cells | RNA | Proteases | Proteins | Medical research | Mutagenesis | Molecular weight
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2. Full Text Modification in reverse: the SUMO proteases
by Mukhopadhyay, Debaditya and Dasso, Mary
Trends in Biochemical Sciences, ISSN 0968-0004, 2007, Volume 32, Issue 6, pp. 286 - 295
SUMOs (small ubiquitin-like modifiers) are ubiquitin-related proteins that become covalently conjugated to cellular target proteins that are involved in a... 
YEAST | CONJUGATION | SUBSTRATE-SPECIFICITY | TOPOISOMERASE-II | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR-PORE COMPLEX | MODIFIED PROTEINS | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | SUMOYLATION | Amino Acid Sequence | Humans | Gene Expression Regulation | Protein Transport - physiology | Ubiquitins - physiology | Cysteine Endopeptidases - physiology | Small Ubiquitin-Related Modifier Proteins - physiology | Repressor Proteins - physiology | Animals | Endopeptidases - genetics | Models, Biological | Peptide Hydrolases - physiology | Cysteine Endopeptidases - genetics | Saccharomyces cerevisiae Proteins - physiology | Endopeptidases - physiology | Evolution, Molecular | Proteins | Biochemistry | Metabolic conjugation | Chemical properties | Research | Analysis
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3. Full Text Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase
by Ewald, Sarah E and Engel, Alex and Lee, Jiyoun and Wang, Miqi and Bogyo, Matthew and Barton, Gregory M
Journal of Experimental Medicine, ISSN 0022-1007, 04/2011, Volume 208, Issue 4, pp. 643 - 651
Toll-like receptor (TLR) 9 requires proteolytic processing in the endolysosome to initiate signaling in response to DNA. However, recent studies conflict as to... 
MEDICINE, RESEARCH & EXPERIMENTAL | SITE | ACTIVATION | DNA | TLR9 | ANTIGEN PRESENTATION | TOLL-LIKE-RECEPTOR-9 | MICE | IMMUNOLOGY | Cell Line | Animals | Toll-Like Receptor 7 - metabolism | Membrane Glycoproteins - metabolism | Mice, Inbred C57BL | Mice | Nucleic Acids - metabolism | Cathepsins - physiology | Toll-Like Receptor 3 - metabolism | Toll-Like Receptor 9 - metabolism | Cysteine Endopeptidases - physiology | Dendritic Cells - metabolism | Brief Definitive Report
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4. Full Text Dynamic regulation of macroautophagy by distinctive ubiquitin-like proteins
by Klionsky, Daniel J and Schulman, Brenda A
Nature Structural and Molecular Biology, ISSN 1545-9993, 2014, Volume 21, Issue 4, pp. 336 - 345
Autophagy complements the ubiquitin-proteasome system in mediating protein turnover. Whereas the proteasome degrades individual proteins modified with... 
CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | LIR MOTIF | CELL BIOLOGY | ATG12-ATG5 CONJUGATE | MEMBRANE-BINDING | CROHN-DISEASE | BIOPHYSICS | STRUCTURAL BASIS | FAMILY INTERACTING MOTIF | AUTOPHAGOSOME FORMATION | ATG8-PE DECONJUGATION | GENOME-WIDE ASSOCIATION | Adaptor Proteins, Signal Transducing - chemistry | Microfilament Proteins - chemistry | Autophagy-Related Proteins | Humans | Microfilament Proteins - physiology | Ubiquitins - chemistry | Autophagy - physiology | Ubiquitins - physiology | Cysteine Endopeptidases - physiology | Proteasome Endopeptidase Complex - physiology | Autophagy-Related Protein 8 Family | Adaptor Proteins, Signal Transducing - physiology | Cysteine Endopeptidases - metabolism | Models, Biological | Proteolysis | Microfilament Proteins - metabolism | Adaptor Proteins, Signal Transducing - metabolism | Ubiquitins - metabolism | Physiological aspects | Autophagy (Cytology) | Cell research | Biosynthesis | Research | Ubiquitin-proteasome system | Proteins | Proteases | Autophagy
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5. Full Text Isocitrate-to-SENP1 signaling amplifies insulin secretion and rescues dysfunctional β cells
by Ferdaoussi, Mourad and Dai, Xiaoqing and Jensen, Mette V and Wang, Runsheng and Peterson, Brett S and Huang, Chao and Ilkayeva, Olga and Smith, Nancy and Miller, Nathanael and Hajmrle, Catherine and Spigelman, Aliya F and Wright, Robert C and Plummer, Gregory and Suzuki, Kunimasa and Mackay, James P and Van De Bunt, Martijn and Gloyn, Anna L and Ryan, Terence E and Norquay, Lisa D and Brosnan, M. Julia and Trimmer, Jeff K and Rolph, Timothy P and Kibbey, Richard G and Manning Fox, Jocelyn E and Colmers, William F and Shirihai, Orian S and Neufer, P. Darrell and Yeh, Edward T.H and Newgard, Christopher B and MacDonald, Patrick E
Journal of Clinical Investigation, ISSN 0021-9738, 10/2015, Volume 125, Issue 10, pp. 3847 - 3860
Insulin secretion from beta cells of the pancreatic islets of Langerhans controls metabolic homeostasis and is impaired in individuals with type 2 diabetes... 
GLUTATHIONE-REDUCTASE | MEDICINE, RESEARCH & EXPERIMENTAL | PANCREATIC B-CELLS | HUMAN ISLETS | TYPE-2 DIABETIC-PATIENTS | POTASSIUM CHANNELS | HUMAN ERYTHROCYTES | REGULATORY ROLE | AMPLIFYING PATHWAYS | N-ETHYLMALEIMIDE | DEPENDENT K+-CHANNELS | Humans | Secretory Vesicles - metabolism | Homeostasis | Male | Exocytosis - physiology | Recombinant Fusion Proteins - metabolism | Exocytosis - drug effects | Glutathione - pharmacology | RNA Interference | Islets of Langerhans - metabolism | HEK293 Cells | Islets of Langerhans - physiopathology | Cell Membrane - metabolism | NADP - metabolism | Insulin Secretion | Cysteine Endopeptidases | Insulin - pharmacology | Catalytic Domain | Signal Transduction | Mice, Inbred C57BL | Isocitrates - metabolism | Glucose - pharmacology | Endopeptidases - deficiency | Gene Knockout Techniques | Organ Specificity | Isocitrates - pharmacology | Isocitrate Dehydrogenase - physiology | Endopeptidases - biosynthesis | Insulin - metabolism | Animals | Diabetes Mellitus, Type 2 - physiopathology | Endopeptidases - genetics | Membrane Potentials | Glucose - metabolism | Sumoylation | Mice | Diabetes Mellitus, Type 2 - pathology | Endopeptidases - physiology
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6. Full Text Proteasomes and their kin: proteases in the machine age
by Pickart, Cecile M and Cohen, Robert E
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 03/2004, Volume 5, Issue 3, pp. 177 - 187
'Chambered proteases', including the eukaryotic 26S proteasome, use the energy of ATP to drive the unfolding and translocation of a polypeptide substrate into... 
20S PROTEASOME | ANGSTROM RESOLUTION | 26 S PROTEASOME | CRYSTAL-STRUCTURE | SUBUNIT-SPECIFIC DEGRADATION | ATP-DEPENDENT PROTEOLYSIS | POLYUBIQUITIN CHAINS | 19S REGULATORY COMPLEX | SACCHAROMYCES-CEREVISIAE | TRANS RECOGNITION | CELL BIOLOGY | Protein Structure, Tertiary | Endopeptidases - metabolism | Peptides - chemistry | Signal Transduction | Ubiquitin - metabolism | Multienzyme Complexes - metabolism | Structure-Activity Relationship | Bacterial Proteins - physiology | Microscopy, Electron | Proteasome Endopeptidase Complex | Cysteine Endopeptidases - physiology | Protein Folding | Protein Transport | Fungal Proteins - physiology | Cysteine Endopeptidases - metabolism | Models, Biological | Peptide Hydrolases - physiology | Multienzyme Complexes - physiology | Protein Binding | Protein Conformation
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7. Full Text Protease inhibitors: Current status and future prospects
by Leung, Donmienne and Abbenante, Giovanni and Fairlie, David P
Journal of Medicinal Chemistry, ISSN 0022-2623, 02/2000, Volume 43, Issue 3, pp. 305 - 341
Aspartic Acid Endopeptidases - physiology | Metalloendopeptidases - antagonists & inhibitors | Serine Proteinase Inhibitors - chemical synthesis | Aspartic Acid Endopeptidases - antagonists & inhibitors | Humans | Serine Endopeptidases - physiology | Models, Molecular | Protease Inhibitors - chemistry | Metalloendopeptidases - metabolism | Cysteine Endopeptidases - physiology | Protease Inhibitors - pharmacology | Animals | Cysteine Endopeptidases - metabolism | Serine Proteinase Inhibitors - chemistry | Aspartic Acid Endopeptidases - metabolism | Cysteine Proteinase Inhibitors - pharmacology | Cysteine Proteinase Inhibitors - chemical synthesis | Cysteine Proteinase Inhibitors - chemistry | Metalloendopeptidases - physiology | Protease Inhibitors - chemical synthesis | Serine Endopeptidases - metabolism | Serine Proteinase Inhibitors - pharmacology | CHEMISTRY, MEDICINAL | HEPATITIS-C VIRUS | SYNTHETIC THROMBIN INHIBITOR | HUMAN NEUTROPHIL ELASTASE | HUMAN-LEUKOCYTE ELASTASE | RHINOVIRUS 3C PROTEASE | NECROSIS-FACTOR-ALPHA | FACTOR XA INHIBITOR | MAST-CELL TRYPTASE | INTERLEUKIN-1-BETA CONVERTING-ENZYME | STRUCTURE-BASED DESIGN
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8. Full Text An Asparaginyl Endopeptidase Mediates in Vivo Protein Backbone Cyclization
by Ivana Saska and Amanda D. Gillon and Noriyuki Hatsugai and Ralf G. Dietzgen and Ikuko Hara-Nishimura and Marilyn A. Anderson and David J. Craik
Journal of Biological Chemistry, ISSN 0021-9258, 10/2007, Volume 282, Issue 40, pp. 29721 - 29728
Proteases can catalyze both peptide bond cleavage and formation, yet the hydrolysis reaction dominates in nature. This presents an interesting challenge for... 
CIRCULAR PROTEINS | CONCANAVALIN-A | FOLDING PATHWAYS | OLDENLANDIA-AFFINIS | MACROCYCLIC PEPTIDES | CYCLOTIDE KALATA B1 | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | PLANTS | CYSTINE KNOT | CELL-DEATH | Protein Structure, Tertiary | Amino Acid Sequence | Cyclotides - chemistry | Peptides - chemistry | Tobacco - metabolism | Gene Expression Regulation | Molecular Sequence Data | Cysteine Endopeptidases - physiology | Peptide Hydrolases - chemistry | Protein Folding | Hydrolysis | Sequence Homology, Amino Acid | Cysteine Endopeptidases - metabolism | Plant Proteins - chemistry | Protein Conformation | DNA, Complementary - metabolism
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9. Full Text Structural basis and specificity of human otubain 1-mediated deubiquitination
by Edelmann, Mariola J and Iphöfer, Alexander and Akutsu, Masato and Altun, Mikael and di Gleria, Katalin and Kramer, Holger B and Fiebiger, Edda and Dhe-Paganon, Sirano and Kessler, Benedikt M
Biochemical Journal, ISSN 0264-6021, 03/2009, Volume 418, Issue 2, pp. 379 - 390
OTUB (otubain) 1 is a human (deubiquitinating enzyme that is implicated in mediating lymphocyte antigen responsiveness, but whose Molecular function is... 
Ubiquitin | Interferon-stimulated gene 15 (ISG15) | Otubain 1 (OTUB1) | Deubiquitinating enzyme (DUB) | Neural-precursor-cell-expressed developmentally down-regulated 8 (NEDD8) | Small ubiquitin-related modifier (SUMO) | DOMAIN | PROTEIN | deubiquitinating enzyme (DUB) | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | otubain 1 (OTUB 1) | interferon-stimulated gene 15 (ISG15) | IDENTIFICATION | neural-precusor-cell-expressed developmentally down-regulated 8 (NEDD8) | ubiquitin | MASS-SPECTROMETRY | ENZYME | POLYUBIQUITIN CHAINS | small ubiquitin-related modifier (SUMO) | CYSTEINE PROTEASES | A20 | Cysteine Endopeptidases - chemistry | Endopeptidases - metabolism | Humans | Cells, Cultured | Models, Molecular | Substrate Specificity | Structure-Activity Relationship | Yeasts - enzymology | Cysteine Endopeptidases - physiology | Sequence Homology, Amino Acid | Endopeptidases - chemistry | Cysteine Endopeptidases - metabolism | Models, Biological | Protein Binding | Protein Conformation | Protein Processing, Post-Translational | Thiolester Hydrolases - chemistry | Ubiquitins - metabolism | Endopeptidases - physiology
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10. Full Text The proteasome: a suitable antineoplastic target
by Adams, Julian
Nature Reviews Cancer, ISSN 1474-175X, 05/2004, Volume 4, Issue 5, pp. 349 - 360
The proteasome is an abundant multi-enzyme complex that provides the main pathway for degradation of intracellular proteins in eukaryotic cells. As such, it... 
PS-341 INHIBITS GROWTH | ONCOLOGY | PHASE-I TRIAL | MOLECULAR-WEIGHT PROTEASES | REFRACTORY HEMATOLOGIC MALIGNANCIES | ANTIGEN PRESENTATION | DRUG-RESISTANCE | MULTICATALYTIC PROTEINASE COMPLEX | NF-KAPPA-B | MULTIPLE-MYELOMA CELLS | CHYMOTRYPSIN-LIKE ACTIVITY | Bortezomib | Humans | Multienzyme Complexes - antagonists & inhibitors | Proteasome Endopeptidase Complex | Cysteine Endopeptidases - physiology | Multienzyme Complexes - physiology | Signal Transduction - physiology | Antineoplastic Agents - pharmacology | Nuclear Proteins - physiology | Cell Transformation, Neoplastic - drug effects | Pyrazines - pharmacology | Cell Cycle Proteins - physiology | Boronic Acids - pharmacology | Endopeptidases - physiology | Antimitotic agents | Control | Physiological aspects | Dosage and administration | Genetic aspects | Cellular signal transduction | Research | Antineoplastic agents | Ubiquitin-proteasome system | Carcinogenesis | Risk factors
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11. Full Text Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation
by Elfriede Dall and Hans Brandstetter
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2013, Volume 110, Issue 27, pp. 10940 - 10945
The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its... 
Proteins | Oxygen | Active sites | Allosteric regulation | Memory interference | Substrate specificity | Electrostatics | Crystal structure | Integrins | Allostery | Electrostatic stability switch | Context-dependent activities | Death domain | substrate specificity | electrostatic stability switch | SITE | k(cat)-substrate specificity | INHIBITION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | TUMOR-ASSOCIATED MACROPHAGES | death domain | context-dependent activities | allostery | Cysteine Endopeptidases - chemistry | Amino Acid Sequence | Enzyme Precursors - chemistry | Humans | Catalytic Domain - genetics | Enzyme Precursors - genetics | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Signal Transduction - genetics | Cysteine Endopeptidases - physiology | Sequence Homology, Amino Acid | Enzyme Precursors - metabolism | Cysteine Endopeptidases - genetics | Protein Conformation | Signal Transduction - physiology | Enzyme Stability - genetics | Kinetics | Enzyme Activation - genetics | Hydrogen-Ion Concentration | Physiological aspects | Cysteine | Biosynthesis | Research | Proteases | Biological Sciences | kcat-substrate specificity
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