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Journal of Hepatology, ISSN 0168-8278, 2011, Volume 55, Issue 1, pp. 192 - 206
Journal Article
Antimicrobial agents and chemotherapy, ISSN 1098-6596, 2019, Volume 63, Issue 4
The combination of the hepatitis C virus (HCV) nonstructural protein 5A (NS5A) inhibitor elbasvir and the NS3/4A protease inhibitor grazoprevir is a potent... 
Atazanavir | Darunavir | Ritonavir | Lopinavir | Elbasvir | Grazoprevir | Virology | EFFICACY | DRUG-INTERACTIONS | MK-5172 | MICROBIOLOGY | RIBAVIRIN | COMBINATION | elbasvir | ATORVASTATIN | TREATMENT-NAIVE | lopinavir | virology | atazanavir | ritonavir | TREATMENT-EXPERIENCED PATIENTS | grazoprevir | GENOTYPE 1 INFECTION | PHARMACOLOGY & PHARMACY | darunavir | ELBASVIR/GRAZOPREVIR | Darunavir - pharmacokinetics | Antiviral Agents - pharmacokinetics | Hepatitis C - drug therapy | Humans | Middle Aged | Benzofurans - pharmacology | Male | Imidazoles - pharmacokinetics | Healthy Volunteers | Lopinavir - pharmacokinetics | Benzofurans - pharmacokinetics | HIV Protease Inhibitors - pharmacology | Quinoxalines - pharmacology | Young Adult | Atazanavir Sulfate - pharmacokinetics | Darunavir - pharmacology | Drug Interactions | HIV Protease Inhibitors - pharmacokinetics | Adult | Female | Ritonavir - pharmacology | Hepacivirus - drug effects | Antiviral Agents - pharmacology | Quinoxalines - pharmacokinetics | Lopinavir - pharmacology | HIV-1 - drug effects | Intracellular Signaling Peptides and Proteins - antagonists & inhibitors | Imidazoles - pharmacology | Ritonavir - pharmacokinetics | Atazanavir Sulfate - pharmacology | HIV Infections - drug therapy | Viral Nonstructural Proteins - antagonists & inhibitors | Index Medicus
Journal Article
PLoS pathogens, ISSN 1553-7374, 2012, Volume 8, Issue 7, p. e1002832
... boceprevir and telaprevir, which inhibit the viral NS3/4A protease. Despite extensive efforts to develop more potent next-generation protease inhibitors, however... 
WILD-TYPE | TELAPREVIR | RAPID VIRAL RESPONSE | ENZYMATIC-ACTIVITIES | PRECLINICAL PROFILE | MICROBIOLOGY | DISCOVERY | INTERFERON | REPLICATION | VIROLOGY | ANTIVIRAL EFFICACY | BOCEPREVIR | PARASITOLOGY | Hepatitis C - drug therapy | Proline - metabolism | Humans | Hepacivirus - genetics | Structure-Activity Relationship | Antiviral Agents - metabolism | Protease Inhibitors - pharmacology | Indoles - metabolism | Viral Nonstructural Proteins - chemistry | Antiviral Agents - chemistry | Lactams - pharmacology | Proline - pharmacology | Indoles - pharmacology | Protease Inhibitors - therapeutic use | Oligopeptides - chemistry | Hepacivirus - drug effects | Protein Structure, Tertiary | Antiviral Agents - pharmacology | Proline - analogs & derivatives | Sulfonamides - chemistry | Models, Molecular | Protease Inhibitors - chemistry | Protease Inhibitors - metabolism | Oligopeptides - metabolism | Sulfonamides - pharmacology | Lactams - metabolism | Proline - chemistry | Drug Resistance, Viral - genetics | Hepatitis C - virology | Sulfonamides - metabolism | Oligopeptides - pharmacology | Viral Nonstructural Proteins - antagonists & inhibitors | Indoles - chemistry | Lactams - chemistry | Virus diseases | Viral drug resistance | Research | Protease inhibitors | Properties | Observations | Hepatitis | Liver cancer | Liver diseases | Ligands | Genetic diversity | Drug resistance | Pharmaceutical industry | Cancer therapies | Viral infections
Journal Article
Cancer cell, ISSN 1535-6108, 2012, Volume 22, Issue 3, pp. 345 - 358
.... Here, we show that P5091 is an inhibitor of deubiquitylating enzyme USP7, which induces apoptosis in MM cells resistant to conventional and bortezomib therapies... 
DEUBIQUITINATING ENZYME | INACTIVATION | PROTEIN | THERAPY | ONCOLOGY | MDM2 | DEGRADATION | MECHANISMS | HAUSP | CANCER | P53 REGULATION | CELL BIOLOGY | Thiophenes - therapeutic use | Apoptosis - drug effects | Humans | Molecular Sequence Data | Antineoplastic Agents - therapeutic use | Pyrazines - therapeutic use | Thalidomide - pharmacology | Boronic Acids - therapeutic use | Antineoplastic Combined Chemotherapy Protocols - pharmacology | Protease Inhibitors - pharmacology | Thalidomide - analogs & derivatives | Multiple Myeloma - drug therapy | Dexamethasone - pharmacology | Antineoplastic Agents - pharmacology | Drug Therapy, Combination | Multiple Myeloma - enzymology | Protease Inhibitors - therapeutic use | Proto-Oncogene Proteins c-mdm2 - metabolism | Ubiquitin Thiolesterase - antagonists & inhibitors | Bortezomib | Cyclin-Dependent Kinase Inhibitor p21 - antagonists & inhibitors | Thiophenes - pharmacology | Random Allocation | Mice, SCID | Ubiquitin Thiolesterase - genetics | Xenograft Model Antitumor Assays | Dexamethasone - therapeutic use | Multiple Myeloma - pathology | Animals | Antineoplastic Combined Chemotherapy Protocols - therapeutic use | Neovascularization, Pathologic - drug therapy | Cell Line, Tumor | Mice | Thalidomide - therapeutic use | Pyrazines - pharmacology | Ubiquitin-Specific Peptidase 7 | Boronic Acids - pharmacology | Drug Resistance, Neoplasm - drug effects | Medical colleges | Dexamethasone | Proteases | Analysis | Multiple myeloma | Lymphomas | Apoptosis
Journal Article
Nature (London), ISSN 1476-4687, 2016, Volume 530, Issue 7589, pp. 233 - 236
.... In particular, proteasome inhibitors have been shown to be toxic for the malaria parasite Plasmodium falciparum at all stages of its life cycle(2-5... 
VISUALIZATION | FALCIPARUM MALARIA | MECHANISM | SPECIFICITY | ARTEMISININ RESISTANCE | MULTIDISCIPLINARY SCIENCES | VALIDATION | ELECTRON-MICROSCOPY | IDENTIFICATION | PARASITE | HUMAN 20S PROTEASOME | Plasmodium falciparum - enzymology | Plasmodium - enzymology | Plasmodium chabaudi - enzymology | Species Specificity | Humans | Proteasome Inhibitors - chemistry | Plasmodium - drug effects | Plasmodium falciparum - drug effects | Protein Subunits - metabolism | Dose-Response Relationship, Drug | Artemisinins - pharmacology | Plasmodium chabaudi - physiology | Drug Design | Plasmodium - growth & development | Female | Drug Resistance | Antimalarials - adverse effects | Catalytic Domain | Proteasome Inhibitors - pharmacology | Models, Molecular | Proteasome Endopeptidase Complex - chemistry | Proteasome Inhibitors - toxicity | Proteasome Inhibitors - adverse effects | Antimalarials - pharmacology | Cryoelectron Microscopy | Drug Synergism | Animals | Substrate Specificity - drug effects | Proteasome Endopeptidase Complex - ultrastructure | Antimalarials - chemistry | Plasmodium chabaudi - drug effects | Mice | Mice, Inbred BALB C | Protein Subunits - antagonists & inhibitors | Protein Subunits - chemistry | Antimalarials - toxicity | Enzyme Activation | Plasmodium falciparum - growth & development | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-proteasome system | Plasmodium | Health aspects | Proteins | Malaria | Protease inhibitors | Proteases | Erythrocytes | Ligands | Parasites | Drug dosages
Journal Article
Nature (London), ISSN 1476-4687, 2017, Volume 550, Issue 7677, pp. 481 - 486
Ubiquitination controls the stability of most cellular proteins, and its deregulation contributes to human diseases including cancer. Deubiquitinases remove... 
DEUBIQUITINATING ENZYME | CELLS | ACTIVATION | PATHWAY | MULTIDISCIPLINARY SCIENCES | CATALYTIC DOMAIN | UBIQUITIN SYSTEM | CANCER-THERAPY | GMP-SYNTHETASE | P53 | PROTEASES | Transcription, Genetic - drug effects | Pyrazoles - chemical synthesis | Pyrimidines - chemical synthesis | Ubiquitin-Specific Peptidase 7 - chemistry | Humans | Substrate Specificity | Crystallography, X-Ray | Proto-Oncogene Proteins c-mdm2 - chemistry | Ubiquitination - drug effects | Piperidines - pharmacology | Apoenzymes - metabolism | Female | Proto-Oncogene Proteins c-mdm2 - metabolism | Apoenzymes - antagonists & inhibitors | Pyrazoles - pharmacology | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Neoplasms - enzymology | Ubiquitin-Specific Peptidase 7 - antagonists & inhibitors | Pyrimidines - pharmacology | Ubiquitin-Specific Peptidase 7 - metabolism | Piperidines - chemical synthesis | Neoplasms - drug therapy | Xenograft Model Antitumor Assays | Animals | Apoenzymes - chemistry | Cell Line, Tumor | Cell Proliferation - drug effects | Mice | Neoplasms - pathology | Proteins | Structure | Proteases | Ligases | Cells | Crystals | Ubiquitin | Enzymes | MDM2 protein | Deregulation | Ubiquitin-specific proteinase | Transcription | p53 Protein | Kinases | Substrates | Degradation | Ubiquitination | Fingers & toes | DNA methylation | Control stability | Catalysis | Inhibition | Ubiquitin-protein ligase | Cancer | Crystal structure | Tumors
Journal Article