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1. Full Text Novel Prodrug-Like Fusion Toxin with Protease-Sensitive Bioorthogonal PEGylation for Tumor Targeting
by Stefan, Nikolas and Zimmermann, Martina and Simon, Manuel and Zangemeister-Wittke, Uwe and Plückthun, Andreas
Bioconjugate Chemistry, ISSN 1043-1802, 12/2014, Volume 25, Issue 12, pp. 2144 - 2156
Highly potent biotoxins like Pseudomonas exotoxin A (ETA) are attractive payloads for tumor targeting. However, despite replacement of the natural cell-binding... 
RECOMBINANT IMMUNOTOXIN | ANIMAL TOXICITY | DRUG-DELIVERY | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, ORGANIC | ANKYRIN REPEAT PROTEINS | B-CELL EPITOPES | ANTITUMOR-ACTIVITY | CHEMISTRY, MULTIDISCIPLINARY | CANCER-THERAPY | POLYETHYLENE-GLYCOL | PSEUDOMONAS EXOTOXIN | PENETRATING PEPTIDES | Cell Adhesion Molecules - chemistry | Cysteine Endopeptidases - chemistry | Recombinant Fusion Proteins - pharmacology | Area Under Curve | Humans | Half-Life | Polyethylene Glycols - chemistry | Prodrugs - chemistry | Antigens, Neoplasm - chemistry | Viral Proteins - metabolism | Epithelial Cell Adhesion Molecule | Cysteine Endopeptidases - metabolism | Drug Design | Female | Antineoplastic Agents - pharmacokinetics | Antineoplastic Agents - pharmacology | Binding Sites | ADP Ribose Transferases - chemistry | Exotoxins - chemistry | Click Chemistry | Viral Proteins - chemistry | Mice, Inbred C57BL | Ankyrin Repeat | Virulence Factors - chemistry | Recombinant Fusion Proteins - chemistry | Antineoplastic Agents - chemistry | Bacterial Toxins - chemistry | Animals | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Prodrugs - pharmacology | Index Medicus
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2. Full Text Conjugated Polymer‐Coated Bacteria for Multimodal Intracellular and Extracellular Anticancer Activity
by Zhu, Chunlei and Yang, Qiong and Lv, Fengting and Liu, Libing and Wang, Shu
Advanced Materials, ISSN 0935-9648, 02/2013, Volume 25, Issue 8, pp. 1203 - 1208
Multifunctional cationic conjugated polyelectrolyte (CP)‐coated bacteria are fabricated for drug loading, delivery and release with multimodal anticancer... 
toxin loading and release | bacteria | imaging | conjugated polymers | anticancer | POLYELECTROLYTES | PHYSICS, CONDENSED MATTER | PHYSICS, APPLIED | MICROSPHERES | MATERIALS SCIENCE, MULTIDISCIPLINARY | ESCHERICHIA-COLI | CONTROLLED-RELEASE | CHEMISTRY, PHYSICAL | NANOSCIENCE & NANOTECHNOLOGY | CHEMISTRY, MULTIDISCIPLINARY | CANCER-THERAPY | DELIVERY | NANOPARTICLES | IMMUNOTOXIN | ASSEMBLIES | EXPRESSION | Polymyxin B - chemistry | ADP Ribose Transferases - toxicity | Cell Survival - drug effects | Bacteria - chemistry | Cations - chemistry | Reactive Oxygen Species - metabolism | Exotoxins - chemistry | Humans | Bacterial Toxins - toxicity | Virulence Factors - chemistry | Antineoplastic Agents - chemistry | Electrolytes - chemistry | Escherichia coli - chemistry | Bacterial Toxins - chemistry | Antineoplastic Agents - toxicity | Polymyxin B - toxicity | Light | Cell Line, Tumor | Exotoxins - toxicity | Polymers - chemistry | ADP Ribose Transferases - chemistry | Virulence Factors - toxicity | Bacteria | Care and treatment | Polymer industry | Polymers | Cancer
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3. Full Text Sortase enzyme-mediated generation of site-specifically conjugated antibody drug conjugates with high In Vitro and In Vivo potency
by Beerli, Roger R and Hell, Tamara and Merkel, Anna S and Grawunder, Ulf
PLoS ONE, ISSN 1932-6203, 07/2015, Volume 10, Issue 7, p. e0131177
Antibody drug conjugates (ADCs) have recently been proven to be highly potent anti-tumor drugs, typically exceeding the efficacy of conventional monoclonal... 
RECOMBINANT IMMUNOTOXIN | IMMUNOGENICITY | MULTIDISCIPLINARY SCIENCES | PURIFICATION | SURFACE-PROTEINS | STAPHYLOCOCCUS-AUREUS | ANTITUMOR-ACTIVITY | MONOCLONAL-ANTIBODIES | FRAGMENTATION | CANCER-THERAPY | PROTEIN LIGATION | Cysteine Endopeptidases - chemistry | Staphylococcus aureus - enzymology | Aminoacyltransferases - immunology | Receptor, ErbB-2 - genetics | Humans | Bacterial Proteins - chemistry | Ovarian Neoplasms - pathology | Ki-1 Antigen - immunology | Maytansine - pharmacology | Immunoconjugates - immunology | Immunoconjugates - pharmacology | Antibodies, Monoclonal, Humanized - pharmacology | Protein Engineering | Maytansine - chemistry | Female | Antineoplastic Agents - pharmacology | Bacterial Proteins - immunology | Receptor, ErbB-2 - antagonists & inhibitors | Receptor, ErbB-2 - immunology | Oligopeptides - chemistry | Ovarian Neoplasms - drug therapy | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | Aminoacyltransferases - chemistry | Antineoplastic Agents - immunology | Maytansine - analogs & derivatives | Antibodies, Monoclonal - pharmacology | Oligopeptides - immunology | Antineoplastic Agents - chemistry | Immunoconjugates - chemistry | Staphylococcus aureus - chemistry | Xenograft Model Antitumor Assays | Animals | Mice, Nude | Ki-1 Antigen - antagonists & inhibitors | Mice | Antibodies, Monoclonal, Humanized - immunology | Cysteine Endopeptidases - immunology | Maytansine - immunology | Trastuzumab | Antibodies, Monoclonal, Humanized - chemistry | Ki-1 Antigen - genetics | Ovarian Neoplasms - immunology | Monoclonal antibodies | Enzymes | Cysteine | Peptides | Biopharmaceutics | Drugs | Conjugates | Addition polymerization | Ovarian carcinoma | Clinical trials | Pentaglycine | Cancer therapies | Molecular weight | Ovarian cancer | Proteins | Tubulin | CD30 antigen | Xenografts | Medical research | Immunoglobulins | Polypeptides | Cloning | Polymerization | Breast cancer | ErbB-2 protein | Substrates | Chemotherapy | Lysine | Heavy chains | Toxins | Conjugation | Sortase | Tumors
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4. Full Text Fungal ribotoxins: molecular dissection of a family of natural killers
by Lacadena, Javier and Álvarez-García, Elisa and Carreras-Sangrà, Nelson and Herrero-Galán, Elías and Alegre-Cebollada, Jorge and García-Ortega, Lucía and Oñaderra, Mercedes and Gavilanes, José G and Martínez del Pozo, Álvaro
FEMS Microbiology Reviews, ISSN 0168-6445, 03/2007, Volume 31, Issue 2, pp. 212 - 237
Abstract RNase T1 is the best known representative of a large family of ribonucleolytic proteins secreted by fungi, mostly Aspergillus and Penicillium species.... 
Aspf1 | immunotoxin | filamentous fungi | sarcin | RNase | Immunotoxin | Sarcin | Filamentous fungi | RIBOSOME-INACTIVATING PROTEIN | PROTEIN ALPHA-SARCIN | PSEUDOMONAS EXOTOXIN-A | MICROBIOLOGY | RIBONUCLEOLYTIC TOXIN RESTRICTOCIN | T-CELL IMMUNOTOXIN | YEAST PICHIA-PASTORIS | AMINO-ACID-SEQUENCE | ALLERGIC BRONCHOPULMONARY ASPERGILLOSIS | RICIN A-CHAIN | CONSTITUENT-PEPTIDE CHAINS | Fungal Proteins - chemistry | Amino Acid Sequence | Endoribonucleases - chemistry | Endoribonucleases - metabolism | Mycotoxins - chemistry | Ribonucleases - chemistry | Aspergillus - chemistry | Ribosomes - chemistry | Molecular Sequence Data | Fungi - chemistry | Ribonucleases - metabolism | Allergens - metabolism | Penicillium - chemistry | Allergens - chemistry | Immunotoxins - metabolism | Immunotoxins - chemistry | Mycotoxins - metabolism | Fungal Proteins - metabolism | RNA - metabolism
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5. Full Text Designing the Furin-Cleavable Linker in Recombinant Immunotoxins Based on Pseudomonas Exotoxin A
by Weldon, John E and Skarzynski, Martin and Therres, Jamy A and Ostovitz, Joshua R and Zhou, Hong and Kreitman, Robert J and Pastan, Ira
Bioconjugate Chemistry, ISSN 1043-1802, 06/2015, Volume 26, Issue 6, pp. 1120 - 1128
Recombinant immunotoxins (RITs) are fusion proteins that join antibodies to protein toxins for targeted cell killing. RITs aimed with Pseudomonas exotoxin A... 
TARGET | LOW IMMUNOGENICITY | TOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, ORGANIC | INFUSION | CYTOTOXIC ACTIVITY | CHEMISTRY, MULTIDISCIPLINARY | RESISTANT | PHASE-I TRIAL | LEUKEMIA | ANTI-MESOTHELIN IMMUNOTOXIN | CAT-8015 | Recombinant Fusion Proteins - pharmacology | Humans | Immunotoxins - pharmacology | Recombinant Fusion Proteins - metabolism | Exotoxins - metabolism | Antineoplastic Agents - metabolism | Immunotoxins - metabolism | Immunotoxins - chemistry | Antineoplastic Agents - pharmacology | ADP Ribose Transferases - chemistry | ADP Ribose Transferases - metabolism | Furin - metabolism | Amino Acid Sequence | Cell Survival - drug effects | Exotoxins - chemistry | Leukemia - drug therapy | Models, Molecular | Exotoxins - pharmacology | Virulence Factors - chemistry | Recombinant Fusion Proteins - chemistry | Antineoplastic Agents - chemistry | Bacterial Toxins - chemistry | Bacterial Toxins - metabolism | Bacterial Toxins - pharmacology | ADP Ribose Transferases - pharmacology | Cell Line, Tumor | Virulence Factors - metabolism | Virulence Factors - pharmacology | Index Medicus
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6. Full Text Mild Method for Succinimide Hydrolysis on ADCs: Impact on ADC Potency, Stability, Exposure, and Efficacy
by Tumey, L. Nathan and Charati, Manoj and He, Tao and Sousa, Eric and Ma, Dangshe and Han, Xiaogang and Clark, Tracey and Casavant, Jeff and Loganzo, Frank and Barletta, Frank and Lucas, Judy and Graziani, Edmund I
Bioconjugate Chemistry, ISSN 1043-1802, 10/2014, Volume 25, Issue 10, pp. 1871 - 1880
The stability of the connection between the antibody and the toxin can have a profound impact on ADC safety and efficacy. There has been increasing evidence in... 
ANTIBODY-DRUG CONJUGATE | LINKER STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, ORGANIC | MICE | CHEMISTRY, MULTIDISCIPLINARY | IMMUNOCONJUGATE | Immunotoxins - blood | Drug Stability | Humans | Sulfides - chemistry | Succinimides - chemistry | Neoplasms - drug therapy | Hydrolysis | Animals | Immunotoxins - therapeutic use | Cell Line, Tumor | Immunotoxins - chemistry | Mice | Protein Stability | Neoplasms - pathology
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7. Full Text Disulfide-Linked Antibody−Maytansinoid Conjugates: Optimization of In Vivo Activity by Varying the Steric Hindrance at Carbon Atoms Adjacent to the Disulfide Linkage
by Kellogg, Brenda A and Garrett, Lisa and Kovtun, Yelena and Lai, Katharine C and Leece, Barbara and Miller, Michael and Payne, Gillian and Steeves, Rita and Whiteman, Kathleen R and Widdison, Wayne and Xie, Hongsheng and Singh, Rajeeva and Chari, Ravi V. J and Lambert, John M and Lutz, Robert J
Bioconjugate Chemistry, ISSN 1043-1802, 04/2011, Volume 22, Issue 4, pp. 717 - 727
In this report, we describe the synthesis of a panel of disulfide-linked huC242 (anti-CanAg) antibody maytansinoid conjugates (AMCs), which have varying levels... 
XENOGRAFT MODELS | DRUG CONJUGATE | SOLID TUMORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, ORGANIC | MULTIPLE-MYELOMA CELLS | CANTUZUMAB MERTANSINE | CANCER | CHEMISTRY, MULTIDISCIPLINARY | IMMUNOCONJUGATE | RICIN-A-CHAIN | PHASE-I | IMMUNOTOXINS | Antibodies - chemistry | Colonic Neoplasms - drug therapy | Humans | Molecular Conformation | Disulfides - blood | Antineoplastic Agents - chemistry | Mice, Inbred Strains | Mice, SCID | Maytansine - pharmacology | Carbon - chemistry | Colonic Neoplasms - metabolism | Antibodies - pharmacology | Xenograft Model Antitumor Assays | Animals | Disulfides - chemistry | Antineoplastic Agents - blood | Maytansine - chemistry | Antibodies - blood | Disulfides - pharmacology | Antineoplastic Agents - pharmacology | Mice | Maytansine - blood
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8. Full Text A guide to taming a toxin – recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer
by Weldon, John E and Pastan, Ira
The FEBS Journal, ISSN 1742-464X, 12/2011, Volume 278, Issue 23, pp. 4683 - 4700
Pseudomonas exotoxin A (PE) is a highly toxic protein secreted by the opportunistic pathogen Pseudomonas aeruginosa. The modular structure and corresponding... 
cancer therapy | intracellular trafficking | recombinant immunotoxins | moxetumomab pasudotox | Pseudomonas exotoxin A | antibody conjugates | ELONGATION FACTOR-II | DISULFIDE-STABILIZED FV | BIOCHEMISTRY & MOLECULAR BIOLOGY | B-CELL EPITOPES | DIPHTHERIA-TOXIN | GROWTH-FACTOR-ALPHA | IN-VIVO | ENDOPLASMIC-RETICULUM | CONSERVED FRAMEWORK REGIONS | ANTI-MESOTHELIN IMMUNOTOXIN | ENDOGENOUS ADP-RIBOSYLATION | ADP Ribose Transferases - immunology | Immunotoxins - immunology | Exotoxins - chemistry | Recombinant Fusion Proteins - pharmacology | Bacterial Toxins - immunology | Exotoxins - immunology | Humans | Exotoxins - pharmacology | Virulence Factors - chemistry | Virulence Factors - immunology | Recombinant Fusion Proteins - chemistry | Immunotoxins - pharmacology | Recombinant Fusion Proteins - metabolism | Bacterial Toxins - chemistry | Neoplasms - therapy | Pseudomonas aeruginosa - pathogenicity | Bacterial Toxins - pharmacology | Neoplasms - immunology | Pseudomonas aeruginosa - metabolism | ADP Ribose Transferases - pharmacology | Immunotoxins - chemistry | Protein Conformation | ADP Ribose Transferases - chemistry | Virulence Factors - pharmacology | Care and treatment | Drug therapy | Antibody-toxin conjugates | Cancer | Index Medicus
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9. Full Text Functional characterization of sticholysin I and W111C mutant reveals the sequence of the actinoporin's pore assembly
by Antonini, Valeria and Pérez-Barzaga, Victor and Bampi, Silvia and Pentón, David and Martínez, Diana and Serra, Mauro Dalla and Tejuca, Mayra
PLoS ONE, ISSN 1932-6203, 10/2014, Volume 9, Issue 10, pp. e110824 - e110824
The use of pore-forming toxins in the construction of immunotoxins against tumour cells is an alternative for cancer therapy. In this protein family one of the... 
MODEL MEMBRANES | PROTEIN | MECHANISM | CYTOLYSIN EQUINATOXIN-II | SEA-ANEMONE | MULTIDISCIPLINARY SCIENCES | FORMING TOXIN | CONSTRUCTION | ANEMONE STICHODACTYLA-HELIANTHUS | LIPID-MEMBRANES | INSIGHTS | Hemolysis | Protein Structure, Tertiary | Protein Structure, Secondary | Humans | Organic Chemicals - chemistry | Sea Anemones - genetics | Recombinant Proteins - chemistry | Ions | Electric Conductivity | Cysteine - chemistry | Permeability | Phosphatidylcholines - chemistry | Sea Anemones - chemistry | Erythrocytes - drug effects | Cryoelectron Microscopy | Lipids - chemistry | Liposomes - chemistry | Animals | Adsorption | Immunotoxins - chemistry | Lipid Bilayers - chemistry | Mutation | Index Medicus
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10. Full Text Preparation and characterization of PE38KDEL-loaded anti-HER2 nanoparticles for targeted cancer therapy
by Chen, Huaiwen and Gao, Jie and Lu, Ying and Kou, Geng and Zhang, He and Fan, Li and Sun, Zhiguo and Guo, Yajun and Zhong, Yanqiang
Journal of Controlled Release, ISSN 0168-3659, 2008, Volume 128, Issue 3, pp. 209 - 216
The clinical use of immunotoxins is severely limited by nonspecific toxicity. To overcome this limitation, PE38KDEL was used as a model protein toxin to... 
Nanoparticles | rhuMAbHER2 | Immunotoxins | PLGA | Targeted delivery | VASCULAR LEAK SYNDROME | L-ASPARAGINASE | CELLS | MEMBRANE ANTIGEN | targeted delivery | MONOCLONAL-ANTIBODY | CHEMISTRY, MULTIDISCIPLINARY | CELLULAR UPTAKE | IN-VITRO | nanoparticles | IMMUNOLIPOSOMES | PROSTATE-CANCER | PHARMACOLOGY & PHARMACY | immunotoxins | ANTICANCER DRUGS | ADP Ribose Transferases - toxicity | Antibody Specificity | Breast Neoplasms - immunology | Humans | Immunotoxins - pharmacology | Glycolates - chemistry | Endocytosis | Time Factors | Surface Properties | Receptor, ErbB-2 - immunology | Immunoglobulin Fab Fragments | Antibodies, Monoclonal - chemistry | ADP Ribose Transferases - metabolism | Virulence Factors - toxicity | Cell Survival - drug effects | Exotoxins - chemistry | Antibodies, Monoclonal - pharmacology | Polyglycolic Acid | Recombinant Proteins - chemistry | Breast Neoplasms - drug therapy | Bacterial Toxins - chemistry | Particle Size | Mice, Nude | Cell Line, Tumor | Exotoxins - toxicity | Virulence Factors - metabolism | Mice | Mice, Inbred BALB C | Antibodies, Monoclonal - metabolism | Bacterial Toxins - toxicity | Exotoxins - metabolism | Drug Carriers | Antineoplastic Agents - metabolism | Dose-Response Relationship, Drug | Immunotoxins - metabolism | Inhibitory Concentration 50 | Female | Immunotoxins - chemistry | Antineoplastic Agents - pharmacology | ADP Ribose Transferases - chemistry | Lactic Acid | Virulence Factors - chemistry | Recombinant Proteins - pharmacology | Antineoplastic Agents - chemistry | Xenograft Model Antitumor Assays | Bacterial Toxins - metabolism | Animals | Breast Neoplasms - pathology | Medical colleges | Care and treatment | Transmission electron microscopes | Drugstores | Antineoplastic agents | Antimitotic agents | Analysis | Monoclonal antibodies | Chemical properties | Antibody-toxin conjugates | Health aspects | Cancer | Index Medicus
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11. Full Text Hindered Disulfide Bonds to Regulate Release Rate of Model Drug from Mesoporous Silica
by Nadrah, Peter and Maver, Uroš and Jemec, Anita and Tišler, Tatjana and Bele, Marjan and Dražić, Goran and Benčina, Mojca and Pintar, Albin and Planinšek, Odon and Gaberšček, Miran
ACS Applied Materials & Interfaces, ISSN 1944-8244, 05/2013, Volume 5, Issue 9, pp. 3908 - 3915
With the advancement of drug delivery systems based on mesoporous silica nanoparticles (MSNs), a simple and efficient method regulating the drug release... 
controlled release | mesoporous silica | nanoparticles | drug delivery | redox | SYSTEM | PORE-SIZE | ZEBRAFISH | STRATEGY | MATERIALS SCIENCE, MULTIDISCIPLINARY | NANOSCIENCE & NANOTECHNOLOGY | FUNCTIONALIZATION | RESPONSIVE CONTROLLED-RELEASE | IN-VIVO | IMMUNOTOXINS | INTRACELLULAR CONTROLLED-RELEASE | Fluorescent Dyes - chemistry | Fluorescent Dyes - pharmacokinetics | Models, Chemical | Nanoparticles - chemistry | Oxidation-Reduction | Silicon Dioxide - chemistry | Delayed-Action Preparations - chemistry | Drug Carriers - toxicity | Zebrafish | Rhodamines - pharmacokinetics | Nanoparticles - toxicity | Drug Carriers - chemistry | Animals | beta-Cyclodextrins - chemistry | Disulfides - chemistry | Embryo, Nonmammalian | Rhodamines - chemistry | Toxicity Tests
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12. Full Text Guided Molecular Missiles for Tumor-Targeting Chemotherapy—Case Studies Using the Second-Generation Taxoids as Warheads
by Ojima, Iwao
Accounts of Chemical Research, ISSN 0001-4842, 01/2008, Volume 41, Issue 1, pp. 108 - 119
A long-standing problem in cancer chemotherapy is the lack of tumor-specific treatments. Traditional chemotherapy relies on the premise that rapidly... 
Taxoids - chemistry | Fluorescent Dyes - chemistry | Fluorescent Dyes - pharmacokinetics | Drug Carriers - therapeutic use | Biotin - pharmacokinetics | Humans | Antibodies, Monoclonal - therapeutic use | Drug Carriers - chemistry | Neoplasms - drug therapy | Biotin - chemistry | Taxoids - therapeutic use | Animals | Immunotoxins - therapeutic use | Nanotubes, Carbon - chemistry | Drug Design | Immunotoxins - chemistry | Immunotoxins - pharmacokinetics | Drug Carriers - pharmacokinetics | Antibodies, Monoclonal - chemistry | Antimitotic agents | Drugs | Drug delivery systems | Chemotherapy | Usage | Product development | Research | Antineoplastic agents | Vehicles | Cancer
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13. Full Text Increasing the antitumor effect of an EpCAM-targeting fusion toxin by facile click PEgylation
by Simon, Manuel and Stefan, Nikolas and Borsig, Lubor and Pleuckthun, Andreas and Zangemeister-Wittke, Uwe
Molecular Cancer Therapeutics, ISSN 1535-7163, 02/2014, Volume 13, Issue 2, pp. 375 - 385
Fusion toxins used for cancer-related therapy have demonstrated short circulation half-lives, which impairs tumor localization and, hence, efficacy. Here, we... 
HALF-LIFE | CELL-ADHESION MOLECULE | ANKYRIN REPEAT PROTEIN | ONCOLOGY | DARPINS | ANTIBODY | CHEMICAL-MODIFICATION | POLYETHYLENE-GLYCOL | PSEUDOMONAS EXOTOXIN | IMMUNOTOXINS | ANTIGEN | Cell Adhesion Molecules - chemistry | Neoplasms - metabolism | Surface Plasmon Resonance | Cell Adhesion Molecules - genetics | Virulence Factors - genetics | Recombinant Fusion Proteins - pharmacology | Humans | Polyethylene Glycols - chemistry | Antigens, Neoplasm - chemistry | Epithelial Cell Adhesion Molecule | MCF-7 Cells | Bacterial Toxins - genetics | Female | Antineoplastic Agents - pharmacokinetics | Antineoplastic Agents - pharmacology | ADP Ribose Transferases - chemistry | Antigens, Neoplasm - genetics | Cell Survival - drug effects | Exotoxins - chemistry | Click Chemistry | Electrophoresis, Polyacrylamide Gel | Virulence Factors - chemistry | Recombinant Fusion Proteins - chemistry | Antineoplastic Agents - chemistry | Bacterial Toxins - chemistry | Neoplasms - drug therapy | HT29 Cells | Xenograft Model Antitumor Assays | ADP Ribose Transferases - genetics | Animals | Tumor Burden - drug effects | Mice, Nude | Recombinant Fusion Proteins - pharmacokinetics | Exotoxins - genetics | Cell Line, Tumor | Neoplasms - pathology
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14. Full Text Removing T-cell epitopes with computational protein design
by Chris King and Esteban N. Garza and Ronit Mazor and Jonathan L. Linehan and Ira Pastan and Marion Pepper and David Baker
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 6/2014, Volume 111, Issue 23, pp. 8577 - 8582
Immune responses can make protein therapeutics ineffective or even dangerous. We describe a general computational protein design method for reducing... 
T lymphocytes | Immune response | Immunodominant epitopes | Exotoxins | Medical treatment | Alleles | T lymphocyte epitopes | Epitopes | Genetic mutation | Epics | Biotherapeutics | Immunotoxin | Deimmunization | Machine learning | Rosetta | biotherapeutics | MULTIDISCIPLINARY SCIENCES | ANTIBODY | deimmunization | ALGORITHMS | machine learning | IDENTIFICATION | GREEN FLUORESCENT PROTEIN | REDUCED IMMUNOGENICITY | THERAPEUTIC PROTEINS | immunotoxin | OPTIMIZATION | PHASE-I | Virulence Factors - genetics | Protein Engineering - methods | Humans | Molecular Sequence Data | Epitopes, T-Lymphocyte - genetics | Green Fluorescent Proteins - genetics | Virulence Factors - immunology | HLA Antigens - genetics | Support Vector Machine | Flow Cytometry | Bacterial Toxins - genetics | Immunotoxins - chemistry | Epitopes, T-Lymphocyte - immunology | Green Fluorescent Proteins - chemistry | ADP Ribose Transferases - chemistry | Protein Structure, Tertiary | ADP Ribose Transferases - immunology | Immunization | Immunotoxins - immunology | Exotoxins - chemistry | Bacterial Toxins - immunology | Exotoxins - immunology | Mice, Inbred C57BL | HLA Antigens - immunology | Models, Molecular | Spectrometry, Fluorescence | Virulence Factors - chemistry | Bacterial Toxins - chemistry | Proteins - immunology | Proteins - genetics | Sequence Homology, Amino Acid | ADP Ribose Transferases - genetics | Immunotoxins - genetics | Animals | Green Fluorescent Proteins - immunology | Exotoxins - genetics | Cell Line, Tumor | Mice | Computer-Aided Design | Proteins - chemistry | Microbiological research | Protein research | Peptides | Research | Pseudomonas | T cells | Health aspects | Index Medicus | Biological Sciences | Physical Sciences
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