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Journal Article
Nature medicine, ISSN 1546-170X, 10/2014, Volume 20, Issue 11, pp. 1254 - 1262
Journal Article
Journal Article
Nature (London), ISSN 1476-4687, 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... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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
Molecular cell, ISSN 1097-2765, 09/2002, Volume 10, Issue 3, pp. 495 - 507
Journal Article
Nature chemical biology, ISSN 1552-4469, 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... 
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | 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