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1. Full Text Coronavirus Main Proteinase ($3CL^{pro}$) Structure: Basis for Design of Anti-SARS Drugs
by Kanchan Anand and John Ziebuhr and Parvesh Wadhwani and Jeroen R. Mesters and Rolf Hilgenfeld
Science, ISSN 0036-8075, 6/2003, Volume 300, Issue 5626, pp. 1763 - 1767
A novel coronavirus has been identified as the causative agent of severe acute respiratory syndrome (SARS). The viral main proteinase (M , also called ), which... 
Enzymes | Molecules | Coronavirus | Atoms | SARS | Reports | Dimers | Polyproteins | SARS virus | Monomers | Crystal structure | VIRUS-ENCODED PROTEINASES | 229E 3C-LIKE PROTEINASE | MULTIDISCIPLINARY SCIENCES | PROTEASES | Cysteine Endopeptidases - chemistry | Coronavirus 229E, Human - enzymology | Humans | Cysteine Proteinase Inhibitors - metabolism | Molecular Sequence Data | Crystallography, X-Ray | Cysteine Endopeptidases - metabolism | Pyrrolidinones - metabolism | Pyrrolidinones - pharmacology | Drug Design | Amino Acid Chloromethyl Ketones - metabolism | Cysteine Proteinase Inhibitors - chemistry | Binding Sites | Dimerization | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Transmissible gastroenteritis virus - enzymology | Catalytic Domain | Protein Structure, Secondary | Amino Acid Chloromethyl Ketones - chemistry | Isoxazoles - metabolism | Crystallization | Models, Molecular | Recombinant Proteins - chemistry | SARS Virus - drug effects | Antiviral Agents | Isoxazoles - chemistry | Severe Acute Respiratory Syndrome - drug therapy | Pyrrolidinones - chemistry | Isoxazoles - pharmacology | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation | SARS Virus - enzymology | Severe acute respiratory syndrome | Research | Coronaviruses | Proteins | Viruses | Drug therapy | Index Medicus
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2. Full Text Development of α-helical calpain probes by mimicking a natural protein-protein interaction
by Jo, Hyunil and Meinhardt, Nataline and Wu, Yibing and Kulkarni, Swapnil and Hu, Xiaozhen and Low, Kristin E and Davies, Peter L and Degrado, William F and Greenbaum, Doron C
Journal of the American Chemical Society, ISSN 0002-7863, 10/2012, Volume 134, Issue 42, pp. 17704 - 17713
We have designed a highly specific inhibitor of calpain by mimicking a natural protein-protein interaction between calpain and its endogenous inhibitor... 
CIRCULAR-DICHROISM | SOLID-PHASE SYNTHESIS | PEPTIDOMIMETIC COMPOUNDS | CONFORMATIONAL PROPERTIES | BIOLOGICAL-ACTIVITY | INHIBITORY-ACTIVITY | SHORT PEPTIDES | CROSS-LINKING | SECONDARY STRUCTURE | HYDROGEN-BOND SURROGATE | CHEMISTRY, MULTIDISCIPLINARY | Calcium-Binding Proteins - chemistry | Calpain - metabolism | Protein Structure, Secondary | Models, Molecular | Structure-Activity Relationship | Calpain - chemistry | Calcium-Binding Proteins - chemical synthesis | Cysteine Proteinase Inhibitors - pharmacology | Cysteine Proteinase Inhibitors - chemical synthesis | Protein Binding | Cysteine Proteinase Inhibitors - chemistry | Molecular Structure | Calcium-Binding Proteins - pharmacology | Calpain - antagonists & inhibitors | Index Medicus
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3. Full Text Falcipain inhibitors: Optimization studies of the 2-pyrimidinecarbonitrile lead series
by Coterón, Jose M and Catterick, David and Castro, Julia and Chaparro, María J and Díaz, Beatriz and Fernández, Esther and Ferrer, Santiago and Gamo, Francisco J and Gordo, Mariola and Gut, Jiri and De Las Heras, Laura and Legac, Jennifer and Marco, Maria and Miguel, Juan and Muñoz, Vicente and Porras, Esther and De La Rosa, Juan C and Ruiz, Jose R and Sandoval, Elena and Ventosa, Pilar and Rosenthal, Philip J and Fiandor, Jose M
Journal of Medicinal Chemistry, ISSN 0022-2623, 08/2010, Volume 53, Issue 16, pp. 6129 - 6152
Falcipain-2 and falcipain-3 are papain-family cysteine proteases of the malaria parasite Plasmodium falciparum that are responsible for host hemoglobin... 
ARYL BROMIDES | CYSTEINE PROTEASE | CHEMISTRY, MEDICINAL | NITRILES | PLASMODIUM-FALCIPARUM | CATHEPSIN-K | MALARIA PARASITES | EXPRESSION | BINDING | PROTEINASE | HEMOGLOBINASE | Cysteine Endopeptidases - chemistry | Plasmodium falciparum - enzymology | Recombinant Proteins - chemistry | Structure-Activity Relationship | Plasmodium falciparum - drug effects | Antimalarials - pharmacology | Cysteine Endopeptidases - metabolism | Protozoan Proteins - metabolism | Cysteine Proteinase Inhibitors - pharmacology | Antimalarials - chemistry | Cysteine Proteinase Inhibitors - chemical synthesis | Cysteine Proteinase Inhibitors - chemistry | Protozoan Proteins - chemistry | Antimalarials - chemical synthesis | Index Medicus
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4. Full Text Purification and characterization of two cysteine proteinase inhibitors from silkworm, Bombyx mori
by Yang, Huan and Li, Jianwei and Liu, Qing and Zhang, Ziyu and Gong, Jing and Hou, Yong
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 09/2018, Volume 503, Issue 4, pp. 3108 - 3113
Cysteine proteinase inhibitors from silkworm are selective inhibitors with low molecular weight and regulate cathepsin L-like cysteine proteinase activity,... 
Structure and activity | Cysteine proteinase inhibitors | Purification | Silkworm | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | PROTEASE INHIBITORS | PROPEPTIDE REGIONS | BIOPHYSICS | IN-VIVO | CTLA-2-ALPHA | GENOME-WIDE SURVEY | EXPRESSION | SWISS-MODEL REPOSITORY | CATHEPSIN-B | Recombinant Proteins - metabolism | Amino Acid Sequence | Bombyx - chemistry | Enzyme Stability | Cysteine Proteinase Inhibitors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Cathepsin L - metabolism | Recombinant Proteins - isolation & purification | Bombyx - metabolism | Animals | Cysteine Proteinase Inhibitors - isolation & purification | Insect Proteins - chemistry | Cysteine Proteinase Inhibitors - chemistry | Protein Conformation | Insect Proteins - isolation & purification | Insect Proteins - metabolism | Cysteine | Surface active agents | Analysis | Escherichia coli | Genomics | Sulfates | Cystine | Index Medicus
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5. Full Text Characterization of a novel endogenous cysteine proteinase inhibitor, trichocystatin-3 (TC-3), localized on the surface of Trichomonas vaginalis
by Sánchez-Rodríguez, Diana Belén and Ortega-López, Jaime and Cárdenas-Guerra, Rosa Elena and Reséndiz-Cardiel, Gerardo and Chávez-Munguía, Bibiana and Lagunes-Guillen, Anel and Arroyo, Rossana
International Journal of Biochemistry and Cell Biology, ISSN 1357-2725, 09/2018, Volume 102, pp. 87 - 100
is a flagellated protist responsible for human trichomoniasis. has three genes encoding for endogenous cysteine proteinase (CP) inhibitors, known as... 
Trichomonas vaginalis | Cytotoxicity | Trichocystatin-3 | Surface protein | Cystatin-like CP endogenous inhibitor | Golgi complex | HEMOLYSIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IRON | BINDING PROTEIN | IDENTIFICATION | CYSTATINS | PROTEASES | CELL BIOLOGY | EPITHELIAL-CELLS | CATHEPSIN-L | CYTOADHERENCE | Amino Acid Sequence | Trichomonas vaginalis - metabolism | Protein Structure, Secondary | Humans | Cysteine Proteinase Inhibitors - metabolism | Models, Molecular | Cysteine Proteinase Inhibitors - chemistry | Cytoplasm - metabolism | Trichomonas vaginalis - cytology | Protein Transport | Cysteine | Proteases | Recombinant proteins | Mass spectrometry | Cystine | Index Medicus
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6. Full Text A fragment-based method to discover irreversible covalent inhibitors of cysteine proteases
by Kathman, Stefan G and Xu, Ziyang and Statsyuk, Alexander V
Journal of Medicinal Chemistry, ISSN 0022-2623, 06/2014, Volume 57, Issue 11, pp. 4969 - 4974
A novel fragment-based drug discovery approach is reported which irreversibly tethers drug-like fragments to catalytic cysteines. We attached an electrophile... 
REACTIVITY | SITE | CHEMISTRY, MEDICINAL | ACID | DRUG DISCOVERY | ESTERS | Rhinovirus - enzymology | Vinyl Compounds - chemistry | Acrylates - chemistry | Sulfonamides - chemistry | Ubiquitin-Specific Proteases - antagonists & inhibitors | Humans | Models, Molecular | Viral Proteins - antagonists & inhibitors | Structure-Activity Relationship | Acrylamides - chemistry | Small Molecule Libraries | Sulfones - chemistry | Papain - antagonists & inhibitors | Drug Design | Cysteine Proteinase Inhibitors - chemistry | Ubiquitin-Conjugating Enzymes - antagonists & inhibitors | Antiparasitic Agents - chemistry | Papain - chemistry | Index Medicus | Brief
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7. Full Text Quantitative analyses of aggregation, autofluorescence, and reactivity artifacts in a screen for inhibitors of a thiol protease
by Jadhav, Ajit and Ferreira, Rafaela S and Klumpp, Carleen and Mott, Bryan T and Austin, Christopher P and Inglese, James and Thomas, Craig J and Maloney, David J and Shoichet, Brian K and Simeonov, Anton
Journal of Medicinal Chemistry, ISSN 0022-2623, 2010, Volume 53, Issue 1, pp. 37 - 51
The perceived and actual burden of false positives in high-throughput screening has received considerable attention; however, few studies exist on the... 
LIBRARIES | POTENT | CHEMISTRY, MEDICINAL | MECHANISM | FALSE POSITIVES | HIGH-THROUGHPUT SCREEN | TRYPANOSOMA-CRUZI | PROMISCUOUS INHIBITORS | ASSAYS | INFECTION | IDENTIFICATION | Bacterial Proteins - antagonists & inhibitors | Cysteine Endopeptidases | Detergents - pharmacology | Drug Evaluation, Preclinical - methods | Protozoan Proteins - antagonists & inhibitors | Fluorescence | Structure-Activity Relationship | Artifacts | Cysteine Proteinase Inhibitors - pharmacology | Cysteine Proteinase Inhibitors - analysis | beta-Lactamases | Cysteine Proteinase Inhibitors - chemistry | beta-Lactamase Inhibitors | High-Throughput Screening Assays - methods | Index Medicus
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8. Full Text Conformational flexibility and allosteric regulation of cathepsin K
by Novinec, Marko and Kovačič, Lidija and Lenarĉič, Brigita and Baici, Antonio
Biochemical Journal, ISSN 0264-6021, 07/2010, Volume 429, Issue 2, pp. 379 - 389
The human cysteine peptidase cathepsin K is a key enzyme in bone homoeostasis and other physiological functions. In the present study we investigate the... 
Substrate inhibition | Chondroitin sulfate | Heparin | Conformational change | Dermatan sulfate | Non-essential activation | substrate inhibition | chondroitin sulfate | BIOCHEMISTRY & MOLECULAR BIOLOGY | non-essential activation | conformational change | DEFICIENCY | heparin | HEPARIN-LIKE GLYCOSAMINOGLYCANS | dermatan sulfate | INHIBITION | SULFATE | LYSOSOMAL ENZYMES | PURIFICATION | COLLAGENOLYTIC ACTIVITY | PROTEINS | EXPRESSION | PROTEASE | Allosteric Regulation | Humans | Protein Conformation - drug effects | Cysteine Proteinase Inhibitors - metabolism | Substrate Specificity | Tryptophan - chemistry | Glycosaminoglycans - chemistry | Cattle | Cathepsin K - blood | Cysteine Proteinase Inhibitors - chemistry | Cathepsin K - antagonists & inhibitors | Cysteine Proteinase Inhibitors - physiology | Glycosaminoglycans - pharmacology | Recombinant Proteins - metabolism | Elastin - metabolism | Recombinant Proteins - antagonists & inhibitors | Glycosaminoglycans - metabolism | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Spectrometry, Fluorescence | Enzyme Activation - drug effects | Collagen - metabolism | Animals | Cathepsin K - metabolism | Cathepsin K - chemistry | Kinetics | In Vitro Techniques | Hydrogen-Ion Concentration | Index Medicus
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9. Full Text Development of peptidomimetics with a vinyl sulfone warhead as irreversible falcipain-2 inhibitors
by Ettari, Roberta and Nizi, Emanuela and Di Francesco, Maria Emilia and Dude, Marie-Adrienne and Pradel, Gabriele and Vičík, Radim and Schirmeister, Tanja and Micale, Nicola and Grasso, Silvana and Zappalà, Maria
Journal of Medicinal Chemistry, ISSN 0022-2623, 02/2008, Volume 51, Issue 4, pp. 988 - 996
This paper describes the synthesis of a new class of peptidomimetic cysteine protease inhibitors based on a 1,4-benzodiazepine scaffold and on an electrophilic... 
LACTATE-DEHYDROGENASE | HEMOGLOBIN | CYSTEINE PROTEASE FALCIPAIN-2 | EPOXIDES | CROSS-METATHESIS | DESIGN | CHEMISTRY, MEDICINAL | PLASMODIUM-FALCIPARUM | SUBSTRATE | SCAFFOLDS | CATALYSTS | Cysteine Endopeptidases - chemistry | Plasmodium falciparum - enzymology | Benzodiazepines - chemical synthesis | Stereoisomerism | Humans | Cathepsin B - chemistry | Structure-Activity Relationship | Plasmodium falciparum - drug effects | Sulfones - pharmacology | Carbamates - chemistry | Molecular Mimicry | Cysteine Endopeptidases - metabolism | Sulfones - chemistry | Cysteine Proteinase Inhibitors - chemical synthesis | Cysteine Proteinase Inhibitors - chemistry | Antimalarials - chemical synthesis | Carbamates - pharmacology | Cathepsins - antagonists & inhibitors | Sulfones - chemical synthesis | Cathepsins - chemistry | Cathepsin L | Recombinant Proteins - antagonists & inhibitors | Benzodiazepines - pharmacology | Peptides - chemistry | Cathepsin B - antagonists & inhibitors | Recombinant Proteins - chemistry | Antimalarials - pharmacology | Carbamates - chemical synthesis | Animals | Cysteine Proteinase Inhibitors - pharmacology | Antimalarials - chemistry | Benzodiazepines - chemistry | Kinetics | Index Medicus
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10. Full Text Design, Synthesis, and Evaluation of Novel Prodrugs of Transition State Inhibitors of Norovirus 3CL Protease
by Galasiti Kankanamalage, Anushka C and Kim, Yunjeong and Rathnayake, Athri D and Alliston, Kevin R and Butler, Michelle M and Cardinale, Steven C and Bowlin, Terry L and Groutas, William C and Chang, Kyeong-Ok
Journal of Medicinal Chemistry, ISSN 0022-2623, 07/2017, Volume 60, Issue 14, pp. 6239 - 6248
Ester and carbamate prodrugs of aldehyde bisulfite adduct inhibitors were synthesized in order to improve their pharmacokinetic and pharmacodynamic properties.... 
CHEMISTRY, MEDICINAL | BIOLOGY | CHEMISTRY | INFECTION | PROTEINASES | NORWALK VIRUS | GASTROENTERITIS | DISCOVERY | CHALLENGES | FOODBORNE | ANTIVIRALS | Stereoisomerism | Humans | Microsomes, Liver - metabolism | Aza Compounds - pharmacology | Prodrugs - chemistry | Structure-Activity Relationship | Blood Proteins - metabolism | Carbamates - chemistry | Esters - chemical synthesis | Pyrrolidines - pharmacology | Cysteine Endopeptidases - metabolism | Antiviral Agents - chemistry | Esters - chemistry | Cysteine Proteinase Inhibitors - chemical synthesis | Cysteine Proteinase Inhibitors - chemistry | Norovirus - drug effects | Carbamates - pharmacology | Cell Line | Antiviral Agents - pharmacology | Aza Compounds - chemical synthesis | Aza Compounds - chemistry | Models, Molecular | Viral Proteins - antagonists & inhibitors | Pyrrolidines - chemistry | Hydrolysis | Carbamates - chemical synthesis | Animals | Pyrrolidines - chemical synthesis | Cysteine Proteinase Inhibitors - pharmacology | Antiviral Agents - chemical synthesis | Prodrugs - chemical synthesis | Protein Binding | Mice | Prodrugs - pharmacology | Esters - pharmacology | Index Medicus
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11. Full Text Development of new cathepsin b inhibitors: Combining bioisosteric replacements and structure-based design to explore the structure-activity relationships of nitroxoline derivatives
by Sosič, Izidor and Mirković, Bojana and Arenz, Katharina and Štefane, Bogdan and Kos, Janko and Gobec, Stanislav
Journal of Medicinal Chemistry, ISSN 0022-2623, 01/2013, Volume 56, Issue 2, pp. 521 - 533
Human cathepsin B has many house-keeping functions, such as protein turnover in lysosomes. However, dysregulation of its activity is associated with numerous... 
CELLS | IN-VITRO | BINDING MODE | CHEMISTRY, MEDICINAL | OCCLUDING LOOP | ESCHERICHIA-COLI | EXTRACELLULAR-MATRIX | CYSTEINE CATHEPSINS | CANCER | RAY CRYSTAL-STRUCTURE | Nitroquinolines - chemistry | Cathepsin B - antagonists & inhibitors | Cysteine Proteinase Inhibitors - chemistry | Structure-Activity Relationship | Cysteine Proteinase Inhibitors - pharmacology | Index Medicus
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12. Full Text Ru(ii) polypyridyl complexes as photocages for bioactive compounds containing nitriles and aromatic heterocycles
by Li, Ao and Turro, Claudia and Kodanko, Jeremy J
Chemical Communications, ISSN 1359-7345, 2/2018, Volume 54, Issue 11, pp. 128 - 129
Photocaging allows for precise spatiotemporal control over the release of biologically active compounds with light. Most photocaged molecules employ organic... 
RUTHENIUM(II) COMPLEXES | VISIBLE-LIGHT | PHOTODYNAMIC THERAPY | CYTOCHROME-P450 ENZYMES | PHOTOCHEMICAL CONTROL | PROSTATE-CANCER | CYSTEINE CATHEPSINS | PHOTOREMOVABLE PROTECTING GROUPS | DENSITY-FUNCTIONAL THEORY | CHEMISTRY, MULTIDISCIPLINARY | MANGANESE NITROSYL | Coordination Complexes - radiation effects | Nitriles - radiation effects | Pyridines - chemistry | Humans | Pyridines - chemical synthesis | Cysteine Proteinase Inhibitors - radiation effects | Coordination Complexes - chemistry | Ruthenium - chemistry | Pyridines - radiation effects | Light | Nitriles - chemistry | Cell Line, Tumor | Coordination Complexes - chemical synthesis | Drug Liberation | Cysteine Proteinase Inhibitors - chemistry | Cytochrome P-450 Enzyme Inhibitors - chemistry | Molecular Structure | Steroid 17-alpha-Hydroxylase - chemistry | Cytochrome P-450 Enzyme Inhibitors - radiation effects | Cathepsins - antagonists & inhibitors | Solid phase synthesis | Protease inhibitors | Aromatic compounds | Nitriles | Ligands | Active control | Functional groups | Biological activity | Index Medicus
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13. Full Text Synthesis, biological evaluation and molecular modeling of a novel series of fused 1,2,3-triazoles as potential anti-coronavirus agents
by Karypidou, Konstantina and Ribone, Sergio R and Quevedo, Mario A and Persoons, Leentje and Pannecouque, Christophe and Helsen, Christine and Claessens, Frank and Dehaen, Wim
Bioorganic and Medicinal Chemistry Letters, ISSN 0960-894X, 11/2018, Volume 28, Issue 21, pp. 3472 - 3476
Synthesis and biological evaluation of a novel library of fused 1,2,3-triazole derivatives are described. The in-house developed multicomponent reaction based... 
3CL protease | Coronavirus | Biological evaluation | Respiratory syndrome | 1,2,3-triazole | DESIGN | CHEMISTRY, MEDICINAL | CHEMISTRY, ORGANIC | IDENTIFICATION | PNEUMONIA | ACUTE RESPIRATORY SYNDROME | DISCOVERY | 3CL PROTEASE INHIBITORS | KETONES | SYNDROME-CORONAVIRUS | ARYL | PROTEINASE | Cysteine Endopeptidases - chemistry | Triazoles - chemistry | Humans | Cysteine Proteinase Inhibitors - metabolism | Structure-Activity Relationship | Antiviral Agents - metabolism | Viral Proteins - metabolism | Microbial Sensitivity Tests | Cysteine Endopeptidases - metabolism | Antiviral Agents - chemistry | Coronavirus - drug effects | Cysteine Proteinase Inhibitors - chemical synthesis | Cysteine Proteinase Inhibitors - chemistry | Triazoles - chemical synthesis | Molecular Structure | Antiviral Agents - pharmacology | Catalytic Domain | Viral Proteins - chemistry | Viral Proteins - antagonists & inhibitors | Triazoles - pharmacology | Triazoles - metabolism | Cysteine Proteinase Inhibitors - pharmacology | Antiviral Agents - chemical synthesis | Cell Line, Tumor | Protein Binding | Molecular Docking Simulation | Antiviral agents | Chymotrypsin | Chemotherapy | Proteases | Triazoles | Analysis | Cancer | Index Medicus
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14. Full Text Identification of a new class of nonpeptidic inhibitors of cruzain
by Brak, Katrien and Doyle, Patricia S and McKerrow, James H and Ellman, Jonathan A
Journal of the American Chemical Society, ISSN 0002-7863, 05/2008, Volume 130, Issue 20, pp. 6404 - 6410
Cruzain is the major cysteine protease of Trypanosoma cruzi, which is the causative agent of Chagas disease and is a promising target for the development of... 
IRREVERSIBLE INHIBITORS | POTENT | DESIGN | ACTIVITY SCREENING METHOD | TRYPANOSOMA-CRUZI | CYSTEINE PROTEASE INHIBITORS | PROTEINASES | RAPID IDENTIFICATION | ACYLOXYMETHYL KETONES | CHEMISTRY, MULTIDISCIPLINARY | CATHEPSIN-S | Cysteine Endopeptidases - chemistry | Coumarins - metabolism | Protozoan Proteins - antagonists & inhibitors | Cysteine Proteinase Inhibitors - metabolism | Molecular Sequence Data | Coumarins - chemistry | Structure-Activity Relationship | Sulfones - pharmacology | Trypanosoma cruzi - enzymology | Macrophages - parasitology | Cysteine Endopeptidases - metabolism | Protozoan Proteins - metabolism | Sulfones - chemistry | Triazoles | Drug Design | Cysteine Proteinase Inhibitors - chemistry | Protozoan Proteins - chemistry | Cathepsins - chemistry | Ketones - pharmacology | Amino Acid Sequence | Sulfones - metabolism | Sequence Alignment | Animals | Cathepsins - metabolism | Cysteine Proteinase Inhibitors - pharmacology | Ketones - chemistry | Trypanosoma cruzi - drug effects | Mice | Ketones - metabolism | Cathepsins - pharmacology | Cysteine | Enzyme inhibitors | Chagas' disease | Research | Chemical properties | Proteases | Index Medicus | Cruzain | protease inhibitor | Chagas’ disease | aryloxymethyl ketone
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15. Full Text Selective Targeting of Tumor and Stromal Cells By a Nanocarrier System Displaying Lipidated Cathepsin B Inhibitor
by Mikhaylov, G and Klimpel, D and Schaschke, N and Mikac, U and Vizovisek, M and Fonovic, M and Turk, V and Turk, Boris and Vasiljeva, Olga
Angewandte Chemie International Edition, ISSN 1433-7851, 09/2014, Volume 53, Issue 38, pp. 10077 - 10081
Cathepsin B (CtsB) is a lysosomal cysteine proteinase that is specifically translocated to the extracellular milieu during cancer progression. The development... 
theranostics | cancer | drug delivery | tumor microenvironment | cathepsin B | Cathepsin B | Drug delivery | Tumor microenvironment | Theranostics | Cancer | cathepsin B | THERAPY | MICROENVIRONMENT | CYSTEINE CATHEPSINS | CHEMISTRY, MULTIDISCIPLINARY | PROTEASES | DELIVERY | Cell Survival - drug effects | Mammary Neoplasms, Experimental - diagnosis | Neoplastic Stem Cells - drug effects | Cathepsin B - antagonists & inhibitors | Cathepsin B - metabolism | Doxorubicin - chemistry | Structure-Activity Relationship | Drug Carriers - chemistry | Drug Delivery Systems | Dose-Response Relationship, Drug | Animals | Cysteine Proteinase Inhibitors - pharmacology | Cysteine Proteinase Inhibitors - chemical synthesis | Cell Line, Tumor | Nanostructures - chemistry | Neoplastic Stem Cells - pathology | Cysteine Proteinase Inhibitors - chemistry | Female | Mice | Molecular Structure | Cell Transformation, Neoplastic - drug effects | Cell Transformation, Neoplastic - pathology | Doxorubicin - pharmacology | Mammary Neoplasms, Experimental - drug therapy | Index Medicus | Communications
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16. Full Text Synthesis and structure-activity relationship study of potent trypanocidal thio semicarbazone inhibitors of the trypanosomal cysteine protease cruzain
by Du, Xiaohui and Guo, Chun and Hansell, Elizabeth and Doyle, Patricia S and Caffrey, Conor R and Holler, Tod P and McKerrow, James H and Cohen, Fred E
Journal of Medicinal Chemistry, ISSN 0022-2623, 06/2002, Volume 45, Issue 13, pp. 2695 - 2707
American trypanosomiasis, or Chagas' disease, is the leading cause of heart disease in Latin America. Currently there is an urgent need to develop... 
ARREST | DESIGN | CHEMISTRY, MEDICINAL | VINYL SULFONES | SPECIFICITY | DETERMINANTS | CHAGAS-DISEASE | ANTICONVULSANT ACTIVITIES | 5-NITRO-2-FURALDEHYDE | AGENTS | DERIVATIVES | Cysteine Endopeptidases | Protozoan Proteins - antagonists & inhibitors | Models, Molecular | Thiosemicarbazones - chemical synthesis | Trypanocidal Agents - chemistry | Structure-Activity Relationship | Trypanosoma cruzi - enzymology | Thiosemicarbazones - chemistry | Animals | Trypanocidal Agents - pharmacology | Cysteine Proteinase Inhibitors - pharmacology | Cysteine Proteinase Inhibitors - chemical synthesis | Trypanocidal Agents - chemical synthesis | Cysteine Proteinase Inhibitors - chemistry | Thiosemicarbazones - pharmacology | Index Medicus
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17. Full Text A comparative study of warheads for design of cysteine protease inhibitors
by Silva, Daniel G and Ribeiro, Jean F.R and De Vita, Daniela and Cianni, Lorenzo and Franco, Caio Haddad and Freitas-Junior, Lucio H and Moraes, Carolina Borsoi and Rocha, Josmar R and Burtoloso, Antonio C.B and Kenny, Peter W and Leitão, Andrei and Montanari, Carlos A
Bioorganic & Medicinal Chemistry Letters, ISSN 0960-894X, 11/2017, Volume 27, Issue 22, pp. 5031 - 5035
The effects on potency of cruzain inhibition of replacing a nitrile group with alternative warheads were explored. The oxime was almost an order of magnitude... 
Oxime | Covalent inhibitor | Nitrile | Warhead | Cysteine protease | Aldehyde | CHEMISTRY, MEDICINAL | DRUG DISCOVERY | CHEMISTRY, ORGANIC | POTENT | NITRILE INHIBITORS | CATHEPSIN-K | PAPAIN | Cysteine Endopeptidases - chemistry | Catalytic Domain | Cysteine Endopeptidases - metabolism | Drug Design | Nitriles - chemistry | Cysteine Proteinase Inhibitors - metabolism | Cysteine Proteinase Inhibitors - chemistry | Cathepsin L - metabolism | Structure-Activity Relationship | Kinetics | Cathepsin L - chemistry | Dipeptides - chemistry | Cysteine | Protease inhibitors | Comparative analysis | Proteases | Cystine | Index Medicus
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18. Full Text Structures of falcipain-2 and falcipain-3 bound to small molecule inhibitors: Implications for substrate specificity
by Kerr, Iain D and Lee, Ji H and Pandey, Kailash C and Harrison, Amanda and Sajid, Mohammed and Rosenthal, Philip J and Brinen, Linda S
Journal of Medicinal Chemistry, ISSN 0022-2623, 02/2009, Volume 52, Issue 3, pp. 852 - 857
Falcipain-2 and falcipain-3 are critical hemoglobinases of Plasmodium falciparum, the most virulent human malaria parasite. We have determined the 2.9 angstrom... 
HEMOGLOBIN | CYSTEINE PROTEASE FALCIPAIN-2 | CHEMISTRY, MEDICINAL | EVOLUTION | GENE | DRUG DISCOVERY | PARASITE PLASMODIUM-FALCIPARUM | HYDROLYSIS | MALARIA PARASITE | PROTEINASE | SOFTWARE | Cysteine Endopeptidases - chemistry | Plasmodium falciparum - enzymology | Catalytic Domain | Animals | Crystallization | Models, Molecular | Substrate Specificity | Crystallography, X-Ray | Cysteine Proteinase Inhibitors - chemistry | Kinetics | Leupeptins - chemistry | Index Medicus
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