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1. Full Text Reprint of “On the Size of the Active Site in Proteases. I. Papain”
by Schechter, Israel
Biochemical and biophysical research communications, ISSN 0006-291X, 08/2012, Volume 425, Issue 3, pp. 497 - 502
Papain
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2. Full Text A mesoporous SiO.sub.2/dense SiO.sub.2/Fe.sub.3O.sub.4 multiply coated hollow microsphere: Synthesis and application on papain immobilization
by Li, Qunyan and Zhou, Yunlu and Ma, Kairui and Wei, Qi and Nie, Zuoren
Colloids and surfaces. A, Physicochemical and engineering aspects, ISSN 0927-7757, 12/2016, Volume 511, p. 239
Papain
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3. Full Text Porcine epidemic diarrhea virus papain-like protease 2 can be noncompetitively inhibited by 6-thioguanine
by Chu, Hsu-Feng and Chen, Chiao-Che and Moses, David C and Chen, Yau-Hung and Lin, Chao-Hsiung and Tsai, Ying-Chieh and Chou, Chi-Yuan
Antiviral research, ISSN 0166-3542, 10/2018, Volume 158, pp. 199 - 205
6-Thioguanine | Papain-like protease | Alpha coronavirus | PEDV | Noncompetitive inhibition | Pharmacology & Pharmacy | Life Sciences & Biomedicine | Science & Technology | Virology | Coronavirus Infections | Antiviral Agents - pharmacology | Thioguanine - pharmacology | Papain - isolation & purification | Protein Conformation - drug effects | Recombinant Proteins | Porcine epidemic diarrhea virus - genetics | Papain - genetics | Coronavirus - drug effects | Papain - antagonists & inhibitors | Porcine epidemic diarrhea virus - drug effects | Molecular Docking Simulation | Kinetics | Binding Sites - drug effects | Papain - chemistry | Ubiquitin | Epidemics | Antiviral agents | Severe acute respiratory syndrome | Diarrhea | Papain | Coronaviruses | Thioguanine | Chemotherapy | Swine | Catalysis | Health aspects | Cancer | Index Medicus | USP, ubiquitin-specific protease | Ubl, ubiquitin-like | PL1pro, papain-like protease 1 | SARS, severe acute respiratory syndrome | AUC, The abbreviations used are analytical ultracentrifugation | PLpro, papain-like protease | Ub-AFC, ubiquitin-7-amino-4-trifluoro-methyl-coumarin | 6MP, 6-mercaptopurine | DUB, deubiquitinating | PEDV, porcine epidemic diarrhea virus | nsp, non-structural protein | 6TG, 6-thioguanine | βME, β-mercaptoethanol | CoV, coronavirus | MERS, Middle East respiratory syndrome | PL2pro, papain-like protease 2 | SV, sedimentation velocity
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4. Full Text Fluorescence turn-on assay for detection of serum D-penicillamine based on papain@AuNCs-Cu.sup.2+ complex
by Chen, Yifan and Qiao, Juan and Liu, Qianrong and Zhang, Mingming and Qi, Li
Analytica chimica acta, ISSN 0003-2670, 10/2018, Volume 1026, p. 133
Fluorescence | Papain
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5. Full Text Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
by Lei, Jian and Kusov, Yuri and Hilgenfeld, Rolf
Antiviral research, ISSN 0166-3542, 01/2018, Volume 149, pp. 58 - 74
Papain-like protease | Innate immunity | Macrodomain | Ubiquitin-like domain | Nucleic-acid binding domain | Structural biology | Pharmacology & Pharmacy | Life Sciences & Biomedicine | Science & Technology | Virology | Amino Acid Sequence | Humans | Ubiquitin - chemistry | Ubiquitin - metabolism | Models, Molecular | Structure-Activity Relationship | Coronaviridae - metabolism | Viral Nonstructural Proteins - chemistry | Protein Binding | Protein Domains | Protein Conformation | Viral Nonstructural Proteins - metabolism | Glutamine - chemistry | Protein Interaction Domains and Motifs | Papain - metabolism | Coronaviridae - genetics | Papain - chemistry | Proteins | Phosphates | Antiviral agents | Severe acute respiratory syndrome | Papain | Nuclear magnetic resonance spectroscopy | B cells | Biological response modifiers | Health aspects | Protein binding | Index Medicus | IRF, interferon regulatory factor | RID, Ras-interacting domain | DMV, double-membrane vesicle | SUD, SARS-unique domain | Ubl, ubiquitin-like | N, nucleocapsid | MHV, mouse hepatitis virus | UTR, untranslated region | transcription complex | ADPr, ADP-ribose | 3Ecto, Nsp3 ectodomain | mISG15, mouse interferon-stimulated gene 15 | hISG15, human interferon-stimulated gene 15 | NF-κB, nuclear factor kappa-light-chain-enhancer of activated B cells | R.M.S.D., root-mean-square deviation | RTC, replication | ARTD, ADP-ribosyltransferases diphtheria toxin-like | GST, glutathione S-transferase | TM, transmembrane | TNF, tumor necrosis factor | TGEV, transmissible gastroenteritis virus | VEEV, Venezuelan equine encephalitis virus | SARS, severe acute respiratory syndrome | PLpro, papain-like protease | TRS, transcriptional regulatory sequence | DUB, deubiquitinating | MKRN, makorin ring finger protein | Ub, ubiquitin | NTD, N-terminal domain | HKU, Hong Kong University | PABP, poly(A)-binding protein | HVR, hypervariable region | RCHY1, RING finger and CHY zinc-finger domain-containing protein 1 | PARP, poly(ADP-ribose) polymerase | MDM2, mouse double minute 2 homolog | Mpro, main protease | ER, Endoplasmic Reticulum | 3CLpro, 3C-like protease | IL-6, Interleukin 6 | CM, convoluted membrane | ADRP, ADP-ribose-1″-phosphate phosphatase | βSM, betacoronavirus-specific marker | Nsp, non-structural protein | HEV, hepatitis E virus | MARylation, mono-ADP-ribosylation | MERS, Middle-East respiratory syndrome | IFN, interferon | USP, ubiquitin-specific protease | CHIKV, Chikungunya virus | DPUP, Domain Preceding Ubl2 and PL2pro | ORF, open reading frame | NAB, nucleic-acid binding domain | HCoV, human coronavirus | PARylation, poly-ADP-ribosylation | CoV, coronavirus | Mac, macrodomain | IBV, infectious bronchitis virus
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6. Full Text Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity
by Shin, Donghyuk and Mukherjee, Rukmini and Grewe, Diana and Bojkova, Denisa and Baek, Kheewoong and Bhattacharya, Anshu and Schulz, Laura and Widera, Marek and Mehdipour, Ahmad Reza and Tascher, Georg and Geurink, Paul P and Wilhelm, Alexander and van der Heden van Noort, Gerbrand J and Ovaa, Huib and Müller, Stefan and Knobeloch, Klaus-Peter and Rajalingam, Krishnaraj and Schulman, Brenda A and Cinatl, Jindrich and Hummer, Gerhard and Ciesek, Sandra and Dikic, Ivan
Nature (London), ISSN 0028-0836, 11/2020, Volume 587, Issue 7835, pp. 657 - 662
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | COVID-19 - immunology | Coronavirus Papain-Like Proteases - chemistry | Humans | Deubiquitinating Enzymes - antagonists & inhibitors | NF-kappa B - immunology | NF-kappa B - metabolism | Ubiquitins - chemistry | Interferons - immunology | SARS-CoV-2 - enzymology | Cytokines - chemistry | Ubiquitination | SARS-CoV-2 - drug effects | SARS-CoV-2 - immunology | Deubiquitinating Enzymes - metabolism | Ubiquitins - metabolism | Coronavirus Papain-Like Proteases - antagonists & inhibitors | COVID-19 - virology | Cytokines - metabolism | Coronavirus Papain-Like Proteases - metabolism | Models, Molecular | Immunity, Innate | SARS-CoV-2 - physiology | COVID-19 - drug therapy | Molecular Dynamics Simulation | Deubiquitinating Enzymes - chemistry | Animals | Interferon Regulatory Factor-3 - metabolism | Interferons - metabolism | Protein Binding | Mice | Ubiquitin | Proteinase | Viral diseases | Innate immunity | Viruses | Infections | Immunity | Middle East respiratory syndrome | COVID-19 | Proteins | Protease | Replicase | Substrate preferences | Post-translation | Preferences | Crystal structure | NF-κB protein | Enzymes | Immune response | Severe acute respiratory syndrome | Papain | Coronaviruses | Substrates | Severe acute respiratory syndrome coronavirus 2 | Disease transmission | Simulation | Respiratory diseases | Interferon | Polyproteins | Binding sites | Structural analysis | Structure-function relationships | Index Medicus
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7. Full Text MERS-CoV papain-like protease has deISGylating and deubiquitinating activities
by Mielech, Anna M and Kilianski, Andy and Baez-Santos, Yahira M and Mesecar, Andrew D and Baker, Susan C
Virology (New York, N.Y.), ISSN 0042-6822, 2013, Volume 450, pp. 64 - 70
Infectious Disease | Ubiquitin | MERS-CoV | PLpro | ISG15 | deISGylating activity | DUB activity | DeISGylating activity | Life Sciences & Biomedicine | Science & Technology | Virology | Ubiquitins - genetics | Humans | Coronaviridae Infections - virology | Molecular Sequence Data | Papain - genetics | Viral Proteins - metabolism | Ubiquitination | SARS Virus - genetics | Coronaviridae Infections - genetics | Cytokines - genetics | Ubiquitins - metabolism | Coronaviridae - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Coronaviridae - chemistry | Cytokines - metabolism | Viral Proteins - chemistry | Viral Proteins - genetics | Glycosylation | Coronaviridae Infections - metabolism | SARS Virus - enzymology | Papain - metabolism | Coronaviridae - enzymology | Papain - chemistry | Virus diseases | Papain | Index Medicus
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8. Full Text Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features
by Lei, Jian and Mesters, Jeroen R and Drosten, Christian and Anemüller, Stefan and Ma, Qingjun and Hilgenfeld, Rolf
Antiviral research, ISSN 0166-3542, 09/2014, Volume 109, Issue 1, pp. 72 - 82
Papain-like protease | MERS-CoV | Oxyanion hole | Deubiquitinase | Zinc finger | Antiviral drug design | Pharmacology & Pharmacy | Life Sciences & Biomedicine | Science & Technology | Virology | Antiviral agents | Viral diseases of the respiratory system and ent viral diseases | Infectious diseases | Pharmacology. Drug treatments | Viral diseases | Biological and medical sciences | Medical sciences | Human viral diseases | Antibiotics. Antiinfectious agents. Antiparasitic agents | Protein Structure, Tertiary | Amino Acid Sequence | Catalytic Domain | Viral Proteins - chemistry | Models, Molecular | Molecular Sequence Data | Viral Proteins - genetics | Crystallography, X-Ray | Viral Proteins - antagonists & inhibitors | Middle East Respiratory Syndrome Coronavirus - chemistry | Papain - genetics | Sequence Alignment | Middle East Respiratory Syndrome Coronavirus - genetics | Papain - antagonists & inhibitors | Middle East Respiratory Syndrome Coronavirus - enzymology | Papain - chemistry | Structure | Papain | Crystals | Index Medicus
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9. Full Text Development and in vivo evaluation of papain-functionalized nanoparticles
by Müller, Christiane and Perera, Glen and König, Verena and Bernkop-Schnürch, Andreas
European journal of pharmaceutics and biopharmaceutics, ISSN 0939-6411, 05/2014, Volume 87, Issue 1, pp. 125 - 131
Nanoparticles | In vivo | Papain | Proteolytic | Oral drug delivery | Mucus penetration | Life Sciences & Biomedicine | Pharmacology & Pharmacy | Science & Technology | Enzymes, Immobilized - chemistry | Enzymes, Immobilized - metabolism | Intestinal Mucosa - metabolism | Nanoparticles - chemistry | Rheology | Drug Carriers - chemical synthesis | Permeability | Rats, Sprague-Dawley | Drug Carriers - chemistry | Intestinal Absorption | Particle Size | Animals | Papain - pharmacokinetics | Enzymes, Immobilized - pharmacokinetics | Surface Properties | Drug Compounding | Drug Carriers - pharmacokinetics | In Vitro Techniques | Sus scrofa | Papain - metabolism | Papain - chemistry | Analysis | Index Medicus
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10. Full Text Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells
by Matsuyama, Shutoku and Matsuyama, Shutoku and