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1. Proteolytic enzymes
: serine and cysteine peptidases
by Barrett, Alan J
1994, Methods in enzymology, ISBN 0121821455, Volume 244., xxi, 765
Enzymes protéolytiques
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2. Proteolytic enzymes
: aspartic and metallo peptidases
by Barrett, Alan J
1995, Methods in enzymology, ISBN 0121821498, Volume 248, xxxi, 873
Metalloproteases | Aspartic Acid Proteases | Peptide Hydrolases | Peptidase | Metalloproteinases | Aspartic proteinases
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3. Full Text The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis
by Beers, Eric P and Jones, Alan M and Dickerman, Allan W
Phytochemistry, ISSN 0031-9422, 01/2004, Volume 65, Issue 1, pp. 43 - 58
The Arabidopsis thaliana genome has over 550 protease sequences representing all five catalytic types: serine, cysteine, aspartic acid, metallo and threonine... 
Arabidopsis thaliana | Cysteine protease | Crucifereae | Papain | Serine protease | Aspartic protease | Subtilisin | Pepsin | Cysteine Endopeptidases - chemistry | Amino Acid Sequence | Aspartic Acid Endopeptidases - chemistry | Arabidopsis - enzymology | Molecular Sequence Data | Serine Endopeptidases - chemistry | Aspartic Acid Endopeptidases - genetics | Phylogeny | Sequence Alignment | Cysteine Endopeptidases - metabolism | Aspartic Acid Endopeptidases - metabolism | Cysteine Endopeptidases - genetics | Databases, Protein | Serine Endopeptidases - genetics | Serine Endopeptidases - metabolism | Genetic Structures | Embryonic development | Thiols | Genomics | Family | Thrombin | Amino acids | Cellular signal transduction | Index Medicus
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4. Full Text Multiple Associated Proteins Regulate Proteasome Structure and Function
by Leggett, David S and Hanna, John and Borodovsky, Anna and Crosas, Bernat and Schmidt, Marion and Baker, Rohan T and Walz, Thomas and Ploegh, Hidde and Finley, Daniel
Molecular Cell, ISSN 1097-2765, 2002, Volume 10, Issue 3, pp. 495 - 507
We have identified proteins that are abundant in affinity-purified proteasomes, but absent from proteasomes as previously defined because elevated salt... 
YEAST | COMPLEX | DOMAIN | DOA4 DEUBIQUITINATING ENZYME | PATHWAY | UBIQUITIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | 26S PROTEASOME | IDENTIFICATION | SACCHAROMYCES-CEREVISIAE | CORE PARTICLE | CELL BIOLOGY | Cysteine Endopeptidases - chemistry | Ligases - isolation & purification | Ligases - genetics | Multienzyme Complexes - metabolism | Proteasome Endopeptidase Complex | Recombinant Fusion Proteins - metabolism | Protein Subunits - metabolism | Saccharomyces cerevisiae - metabolism | Salts - chemistry | Cysteine Endopeptidases - metabolism | Protein Subunits - isolation & purification | Adenosine Triphosphate - metabolism | Saccharomyces cerevisiae Proteins - isolation & purification | Binding Sites | Endopeptidases - isolation & purification | Protein Subunits - genetics | Multienzyme Complexes - ultrastructure | Endopeptidases - metabolism | Ligases - metabolism | Saccharomyces cerevisiae Proteins - genetics | Canavanine - metabolism | Multienzyme Complexes - chemistry | Proteins - genetics | Ubiquitin-Protein Ligases | Endopeptidases - genetics | Proteins - metabolism | Cysteine Endopeptidases - isolation & purification | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Recombinant Fusion Proteins - genetics | Cysteine Endopeptidases - ultrastructure | Multienzyme Complexes - isolation & purification | Index Medicus
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5. Full Text In vivo genome editing using Staphylococcus aureus Cas9
by Ran, F. Ann and Cong, Le and Yan, Winston X and Scott, David A and Gootenberg, Jonathan S and Kriz, Andrea J and Zetsche, Bernd and Shalem, Ophir and Wu, Xuebing and Makarova, Kira S and Koonin, Eugene V and Sharp, Phillip A and Zhang, Feng
Nature, ISSN 0028-0836, 04/2015, Volume 520, Issue 7546, pp. 186 - 191
The RNA-guided endonuclease Cas9 has emerged as a versatile genom-editing platform. However, the size of the commonly used Cas9 from Streptococcus pyogenes... 
NUCLEASE SPECIFICITY | IMMUNITY | OFF-TARGET SITES | DNA CLEAVAGE | ENDONUCLEASE | GENE | CRISPR RNA | MULTIDISCIPLINARY SCIENCES | SEQUENCE | SYSTEMS | GUIDE RNA | Staphylococcus aureus - enzymology | Cholesterol - blood | Genome - genetics | Substrate Specificity | Male | Proprotein Convertases - genetics | Proprotein Convertases - biosynthesis | Base Sequence | Serine Endopeptidases - genetics | Proprotein Convertases - blood | Genetic Engineering - methods | Staphylococcus aureus - genetics | Gene Targeting | Serine Endopeptidases - deficiency | Serine Endopeptidases - biosynthesis | CRISPR-Associated Proteins - genetics | Liver - metabolism | Mice, Inbred C57BL | Cholesterol - metabolism | Proprotein Convertases - deficiency | Animals | CRISPR-Associated Proteins - metabolism | Serine Endopeptidases - blood | Liver - physiology | Mice | Proprotein Convertase 9 | Enzymes | Usage | Genetic engineering | Genetic aspects | Methods | Staphylococcus aureus | Bacteria | Genomes | Biomedical research | Molecular weight | Index Medicus
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6. Full Text A cryptic protease couples deubiquitination and degradation by the proteasome
by Cohen, Robert E and Yao, Tingting
Nature, ISSN 0028-0836, 09/2002, Volume 419, Issue 6905, pp. 403 - 407
The 26S proteasome is responsible for most intracellular proteolysis in eukaryotes. Efficient substrate recognition relies on conjugation of substrates with... 
REGULATORY PARTICLE | SIGNAL | DOMAIN | THERMODYNAMICS | GENE | UBIQUITIN | ENZYMES | MULTIDISCIPLINARY SCIENCES | SACCHAROMYCES-CEREVISIAE | ATP | Cysteine Endopeptidases - chemistry | Protein Subunits | Drug Resistance, Multiple | Peptide Hydrolases - genetics | Saccharomyces cerevisiae - genetics | Zinc - metabolism | Molecular Sequence Data | Multienzyme Complexes - metabolism | Proteasome Endopeptidase Complex | Trans-Activators - chemistry | Cell Cycle Proteins - chemistry | Genes, Lethal | Endopeptidases - chemistry | Cysteine Endopeptidases - metabolism | Cattle | Protein Denaturation | Cell Cycle Proteins - genetics | Ovomucin - chemistry | Genes, Fungal - genetics | Ubiquitins - metabolism | Peptide Hydrolases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Endopeptidases - metabolism | Ovomucin - metabolism | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Multienzyme Complexes - genetics | Saccharomyces cerevisiae Proteins - genetics | Blotting, Western | Peptide Hydrolases - chemistry | Macromolecular Substances | Multienzyme Complexes - chemistry | Animals | Endopeptidases - genetics | Cysteine Endopeptidases - genetics | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Adenosine Triphosphatases - chemistry | Trans-Activators - metabolism | Adenosine Triphosphatases - genetics | Protein Processing, Post-Translational | Kinetics | Saccharomyces cerevisiae Proteins - chemistry | Cellular biology | Molecules | Biochemistry | Index Medicus
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7. Full Text Production, characterization, gene cloning, and nematocidal activity of the extracellular protease from Stenotrophomonas maltophilia N4
by Jankiewicz, Urszula and Larkowska, Ewa and Swiontek Brzezinska, Maria
Journal of Bioscience and Bioengineering, ISSN 1389-1723, 06/2016, Volume 121, Issue 6, pp. 614 - 618
A rhizosphere strain of the bacterium N4 secretes the serine protease PN4, whose molecular mass is approximately 42 kDa. The optimal temperature for the enzyme... 
Stenotrophomonas maltophilia | Serine protease | Nematocidal activity | Biocontrol | FOOD SCIENCE & TECHNOLOGY | BREVIBACILLUS-LATEROSPORUS G4 | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | NEMATODES | ENZYMES | PURIFICATION | PATHOGENIC FACTOR | SERINE-PROTEASE | CHITINASE | BIOLOGICAL-CONTROL | BACILLUS | STRAIN | Temperature | Molecular Weight | Bacterial Proteins - chemistry | Molecular Sequence Data | Serine Endopeptidases - pharmacology | Substrate Specificity | Endopeptidases - chemistry | Stenotrophomonas maltophilia - genetics | Cloning, Molecular | Serine Endopeptidases - genetics | Protein Domains | Antinematodal Agents - metabolism | Antinematodal Agents - pharmacology | Rhabditida - drug effects | Amino Acid Sequence | Endopeptidases - metabolism | Bacterial Proteins - genetics | Enzyme Stability | Serine Endopeptidases - chemistry | Antinematodal Agents - chemistry | Bacterial Proteins - pharmacology | Animals | Caenorhabditis elegans - drug effects | Endopeptidases - genetics | Bacterial Proteins - metabolism | Serine Endopeptidases - metabolism | Endopeptidases - pharmacology | Hydrogen-Ion Concentration | Stenotrophomonas maltophilia - enzymology | Keratin | Protease inhibitors | Casein | Cloning | Genes | Thrombin | Amino acids | Genetic aspects | Enzymes | Biological control | Albumin | Pests | Biocides | Zinc compounds | Index Medicus
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8. Full Text Cellular peptidases in immune functions and diseases 2
by Ansorge, Siegfried and Langner, Jürgen
2000, Advances in experimental medicine and biology, ISBN 0306463830, Volume 477
physiology | Peptide Hydrolases | Peptidase | Immunology | Pathophysiology | Endopeptidases
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9. Full Text Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum
by Grainger, Munira and Powers, James C and Ponder, Elizabeth L and Yuan, Fang and Fonovi, Urša Pe ar and Fonovi, Marko and Phillips, Carolyn I and Bogyo, Matthew and Yeoh, Sharon and Arastu-Kapur, Shirin
Nature Chemical Biology, ISSN 1552-4450, 03/2008, Volume 4, Issue 3, pp. 203 - 213
Newly replicated Plasmodium falciparum parasites escape from host erythrocytes through a tightly regulated process that is mediated by multiple classes of... 
CYSTEINE PROTEASE | PARASITOPHOROUS VACUOLE | VINYL SULFONES | STREPTOLYSIN-O | MEROZOITES | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL INVASION | I CATHEPSIN-C | SERINE-PROTEASE | SUBTILISIN-LIKE PROTEASE-1 | ANTIGEN | Cysteine Endopeptidases - chemistry | Plasmodium falciparum - enzymology | Parasitic Sensitivity Tests | Protozoan Proteins - antagonists & inhibitors | Stereoisomerism | Humans | Molecular Conformation | Subtilisins - chemistry | Plasmodium falciparum - drug effects | Cysteine Endopeptidases - drug effects | Sulfones - pharmacology | Serine Endopeptidases - drug effects | Dose-Response Relationship, Drug | Antigens, Protozoan - metabolism | Protease Inhibitors - pharmacology | Antigens, Protozoan - drug effects | Cysteine Endopeptidases - metabolism | Protozoan Proteins - metabolism | Isocoumarins - pharmacology | Sulfones - chemistry | Malaria, Falciparum - metabolism | Protozoan Proteins - chemistry | Subtilisins - metabolism | Plasmodium falciparum - physiology | Peptides - chemistry | Protease Inhibitors - chemistry | Serine Endopeptidases - chemistry | Subtilisins - antagonists & inhibitors | Peptides - pharmacology | Host-Parasite Interactions - drug effects | Malaria, Falciparum - parasitology | Animals | Small Molecule Libraries | Erythrocytes - metabolism | Serine Endopeptidases - metabolism | Erythrocytes - parasitology | Isocoumarins - chemistry | Biochemistry | Biomedical research | Parasites | Malaria | Proteases | Erythrocytes | Index Medicus
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10. Full Text IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
by Johansson, Björn P and Björck, Lars and von Pawel-Rammingen, Ulrich and Institutionen för experimentell medicinsk vetenskap and Department of Experimental Medical Science and Lund University and Infektionsmedicin and Lunds universitet and Division of Infection Medicine (BMC)
The EMBO Journal, ISSN 0261-4189, 04/2002, Volume 21, Issue 7, pp. 1607 - 1615
Recent work from several laboratories has demonstrated that proteolytic mechanisms significantly contribute to the molecular interplay between Streptococcus... 
Streptococcus pyogenes | cysteine proteinase | immunoglobulin | virulence | Immunoglobulin | Virulence | Cysteine proteinase | PYOGENES STRAINS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SURFACE-PROTEINS | IGG | BINDING PROTEIN | CELL BIOLOGY | GROUP-A STREPTOCOCCI | GRAM-POSITIVE BACTERIA | M1 PROTEIN | GENE | TOXIC-SHOCK-SYNDROME | EXPRESSION | Neutrophils - cytology | Immunoglobulin Fc Fragments - metabolism | Humans | Integrins - isolation & purification | Molecular Sequence Data | Substrate Specificity | Integrins - metabolism | Cysteine Endopeptidases - metabolism | Immunoglobulin Fc Fragments - immunology | Immunoglobulin G - immunology | Antibodies, Bacterial - metabolism | Amino Acid Sequence | Cell Line | Genes, Bacterial | Gene Expression | Streptococcus pyogenes - immunology | Integrins - immunology | Cells, Cultured | Phagocytosis - immunology | Integrins - classification | Animals | Cysteine Endopeptidases - isolation & purification | Streptococcus pyogenes - enzymology | Antibodies, Bacterial - immunology | Bacterial Proteins - metabolism | Mice | Cysteine Endopeptidases - classification | Cysteine Endopeptidases - immunology | Immunoglobulin G - metabolism | Index Medicus | Bacterial | Cysteine Endopeptidases : metabolism | Integrins : isolation & purification | Support | Genes | Antibodies | Fc : immunology | Cysteine Endopeptidases : immunology | Cysteine Endopeptidases : isolation & purification | Integrins : classification | Immunoglobulin G : metabolism | Biochemistry and Molecular Biology | Cultured | Biologi | Natural Sciences | Streptococcus pyogenes : enzymology | Human | Biological Sciences | Immunoglobulins | Integrins : metabolism | Bacterial : metabolism | Integrins : immunology | Bacterial Proteins : metabolism | Cells | Phagocytosis : immunology | Cysteine Endopeptidases : classification | Streptococcus pyogenes : immunology | Naturvetenskap | Biokemi och molekylärbiologi | Animal | Neutrophils : cytology | Bacterial : immunology | Fc : metabolism | Immunoglobulin G : immunology | Non-U.S. Gov't
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11. 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 | Index Medicus
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12. Full Text Purification and stability characteristics of an alkaline serine protease from a newly isolated Haloalkaliphilic bacterium sp. AH-6
by Dodia, M S and Rawal, C M and Bhimani, H G and Joshi, R H and Khare, S K and Singh, S P
Journal of Industrial Microbiology & Biotechnology, ISSN 1367-5435, 2/2008, Volume 35, Issue 2, pp. 121 - 131
An alkaline protease secreting Haloalkaliphilic bacterium (Gene bank accession number EU118361) was isolated from the Saurashtra Coast in Western India. The... 
Biochemistry, general | Biotechnology | Chemistry | Genetic Engineering | Purification | Microbiology | Microbial Genetics and Genomics | Bioinformatics | Haloalkaliphiles | Alkaline protease | Salt-dependent thermostability | SULFUR-OXIDIZING BACTERIA | SODA LAKES | THIOALKALIVIBRIO | BIOCHEMICAL-CHARACTERIZATION | HALOPHILIC MICROORGANISMS | NATRIALBA-MAGADII | ARCHAEON NATRONOCOCCUS-OCCULTUS | ENZYME | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | purification | salt-dependent thermostability | SP-NOV | alkaline protease | BACILLUS-PUMILUS | Coenzymes - pharmacology | Temperature | Molecular Weight | Sodium Chloride - pharmacology | Bacterial Proteins - chemistry | Molecular Sequence Data | DNA, Bacterial - chemistry | DNA, Ribosomal - chemistry | Endopeptidases - chemistry | Serine Endopeptidases - genetics | Bacteria - classification | Chromatography, Liquid | Phenylmethylsulfonyl Fluoride - pharmacology | DNA, Ribosomal - genetics | Endopeptidases - isolation & purification | Detergents - pharmacology | Endopeptidases - metabolism | Calcium - pharmacology | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Enzyme Stability | Serine Endopeptidases - chemistry | Bacteria - genetics | Sequence Analysis, DNA | India | Bacteria - isolation & purification | DNA, Bacterial - genetics | Endopeptidases - genetics | Environmental Microbiology | RNA, Ribosomal, 16S - genetics | Bacteria - enzymology | Bacterial Proteins - metabolism | Serine Endopeptidases - metabolism | Serine Endopeptidases - isolation & purification | Bacterial Proteins - isolation & purification | Hydrogen-Ion Concentration | Prothrombin | Serine | Studies | Bacteria | Proteases | Temperature effects | Index Medicus
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