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1994, Methods in enzymology, ISBN 0121821455, Volume 244., xxi, 765
Book
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
Journal Article
Nature, ISSN 0028-0836, 04/2015, Volume 520, Issue 7546, pp. 186 - 191
Journal Article
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
Journal Article
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
Journal Article
2000, Advances in experimental medicine and biology, ISBN 0306463830, Volume 477
eBook
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
Journal Article
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
Journal Article
Biochemical Journal, ISSN 0264-6021, 03/2009, Volume 418, Issue 2, pp. 379 - 390
Journal Article
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
Journal Article