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science & technology (579) 579
life sciences & biomedicine (449) 449
animals (428) 428
humans (388) 388
single-domain antibodies - genetics (249) 249
single-domain antibodies - immunology (232) 232
single-domain antibodies - chemistry (219) 219
biochemistry & molecular biology (216) 216
antibodies (198) 198
proteins (184) 184
single-domain antibodies - metabolism (158) 158
mice (147) 147
amino acid sequence (128) 128
nanobody (128) 128
science & technology - other topics (126) 126
immunology (121) 121
antigens (116) 116
multidisciplinary sciences (116) 116
protein binding (112) 112
molecular sequence data (104) 104
biotechnology & applied microbiology (101) 101
viral antibodies (100) 100
immunoglobulins (99) 99
single-domain antibody (93) 93
phage display (86) 86
gene expression (83) 83
models, molecular (81) 81
peptide library (81) 81
single-domain antibodies - pharmacology (80) 80
camelids, new world (78) 78
research (74) 74
biotechnology (72) 72
enzyme-linked immunosorbent assay (72) 72
cell line, tumor (71) 71
biochemical research methods (69) 69
vhh (69) 69
medicine (68) 68
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science (67) 67
single domain antibody (67) 67
escherichia coli - genetics (66) 66
recombinant fusion proteins - genetics (66) 66
single-domain antibodies (66) 66
analysis (63) 63
binding sites (63) 63
research article (60) 60
microbiology (59) 59
recombinant proteins - genetics (58) 58
cancer (57) 57
immunization (57) 57
life sciences (57) 57
chemistry (56) 56
viruses (56) 56
physical sciences (55) 55
single-domain antibodies - isolation & purification (55) 55
cell biology (54) 54
health aspects (53) 53
male (53) 53
affinity (51) 51
camelids, new world - immunology (51) 51
protein engineering (51) 51
mutation (50) 50
protein conformation (50) 50
crystallography, x-ray (49) 49
antibody affinity (47) 47
cell line (46) 46
monoclonal antibodies (46) 46
nanobodies (46) 46
biology (45) 45
physiological aspects (44) 44
hek293 cells (43) 43
immunoglobulin heavy chains - genetics (43) 43
protein stability (43) 43
antibody specificity (42) 42
biochemistry (41) 41
escherichia coli (41) 41
surface plasmon resonance (41) 41
virology (40) 40
camelus (39) 39
epitopes - immunology (39) 39
immunotherapy (39) 39
recombinant proteins - immunology (39) 39
flow cytometry (38) 38
gene library (38) 38
recombinant proteins - chemistry (38) 38
single-domain antibodies - biosynthesis (38) 38
biology and life sciences (37) 37
recombinant fusion proteins - metabolism (37) 37
antibodies, neutralizing - immunology (36) 36
binding (36) 36
fluorescence (36) 36
protein structure, tertiary (36) 36
recombinant fusion proteins - immunology (36) 36
immunoglobulin heavy chains - immunology (35) 35
tumors (35) 35
biological and medical sciences (34) 34
camelus - immunology (34) 34
crystal structure (34) 34
escherichia coli - metabolism (34) 34
medicine, research & experimental (34) 34
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1. Full Text Nanobodies: Natural single-domain antibodies
by Muyldermans, Serge
Annual review of biochemistry, ISSN 0066-4154, 06/2013, Volume 82, Issue 1, pp. 775 - 797
Heavy-chain antibody | Camel | Llama | Single-domain antibody | Shark | VHH | Biotechnology | Antibodies - chemistry | Immunoglobulin Heavy Chains - chemistry | Antibody Affinity | Camelus - immunology | Single-Domain Antibodies - immunology | Camelids, New World | Animals | Single-Domain Antibodies - chemistry | Camelus - genetics | Antibodies - immunology | Antibodies - genetics | Immunoglobulin Heavy Chains - immunology | Immunoglobulin Heavy Chains - genetics | Viral antibodies | Antibodies | Dosage and administration | Research | Drug interactions | Protein binding | Antigens | Genes | Crystal structure | Index Medicus
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2. Full Text Modulating antibody‐dependent cellular cytotoxicity of epidermal growth factor receptor‐specific heavy‐chain antibodies through hinge engineering
by D'Eall, Calvin and Pon, Robert A and Rossotti, Martin A and Krahn, Natalie and Spearman, Maureen and Callaghan, Deborah and Faassen, Henk and Hussack, Greg and Stetefeld, Jörg and Butler, Michael and Durocher, Yves and Zhang, Jianbing and Henry, Kevin A and Tanha, Jamshid
Immunology and cell biology, ISSN 0818-9641, 07/2019, Volume 97, Issue 6, pp. 526 - 537
antibody engineering | antibody‐dependent cellular cytotoxicity (ADCC) | hinge | antibody | single‐domain antibody | epidermal growth factor receptor (EGFR) | Immunology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Immunotherapy - methods | ErbB Receptors - metabolism | Antibody-Dependent Cell Cytotoxicity | Breast Neoplasms - immunology | Adenocarcinoma - immunology | Humans | Antibody Affinity | Camelidae | Mutation - genetics | Breast Neoplasms - therapy | Antibodies, Monoclonal - genetics | Animals | Immunoglobulin G - genetics | Adenocarcinoma - therapy | ErbB Receptors - immunology | Protein Engineering | Cell Line, Tumor | Protein Binding | Recombinant Fusion Proteins - genetics | Female | Immunoglobulin Variable Region - genetics | Antibodies, Monoclonal - metabolism | Immunoglobulin Fc Fragments - genetics | Immunoglobulin Heavy Chains - genetics | Epidermal growth factor | Epidermal growth factor receptors | Tumor cells | Immunoglobulin G | Point mutation | Antibodies | Cytotoxicity | Epitopes | Index Medicus
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3. Full Text Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2
by Xiang, Yufei and Nambulli, Sham and Xiao, Zhengyun and Liu, Heng and Sang, Zhe and Duprex, W Paul and Schneidman-Duhovny, Dina and Zhang, Cheng and Shi, Yi
Science (American Association for the Advancement of Science), ISSN 0036-8075, 12/2020, Volume 370, Issue 6523, pp. 1479 - 1484
Escherichia coli | Humans | Neutralization Tests | Angiotensin-Converting Enzyme 2 - immunology | Receptors, Virus - genetics | Angiotensin-Converting Enzyme 2 - genetics | Single-Domain Antibodies - immunology | Antibodies, Neutralizing - immunology | Protein Domains | Angiotensin-Converting Enzyme 2 - chemistry | SARS-CoV-2 - immunology | Recombinant Proteins - chemistry | Antibody Affinity | Antibodies, Neutralizing - genetics | Recombinant Proteins - genetics | COVID-19 - therapy | Camelids, New World | Animals | Receptors, Virus - chemistry | Recombinant Proteins - immunology | Single-Domain Antibodies - chemistry | Antibodies, Neutralizing - chemistry | Antibodies, Viral - chemistry | Protein Binding | Receptors, Virus - immunology | Antibodies, Viral - immunology | Single-Domain Antibodies - genetics | Antibodies, Viral - genetics | Virus diseases | Severe acute respiratory syndrome | Analysis | Coronaviruses | Health aspects | Antigenic determinants | Protein binding | Bioengineering | Yeasts | Immunization | Pandemics | Yeast | Viral diseases | Proteins | Severe acute respiratory syndrome coronavirus 2 | Domains | COVID-19 | Respiratory diseases | Proteomics | Monoclonal antibodies | Neutralization | Index Medicus
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4. Full Text Exceptionally Potent and Broadly Cross-Reactive, Bispecific Multivalent HIV-1 Inhibitors Based on Single Human CD4 and Antibody Domains
by Weizao Chen and Yang Feng and Ponraj Prabakaran and Tianlei Ying and Yanping Wang and Jianping Sun and Camila D. S. Macedo and Zhongyu Zhu and Yuxian He and Victoria R. Polonis and Dimiter S. Dimitrov
Journal of Virology, ISSN 0022-538X, 01/2014, Volume 88, Issue 2, pp. 1125 - 1139
Life Sciences & Biomedicine | Science & Technology | Virology | Humans | Antibodies, Monoclonal - therapeutic use | Neutralization Tests | Single-Domain Antibodies - immunology | HIV Envelope Protein gp120 - immunology | HIV Infections - immunology | HIV Antibodies - immunology | Anti-HIV Agents - therapeutic use | HIV Antibodies - therapeutic use | Antibodies, Monoclonal - chemistry | Antibodies, Monoclonal - immunology | CD4 Antigens - genetics | CD4 Antigens - immunology | Single-Domain Antibodies - therapeutic use | HIV-1 - drug effects | HIV Infections - virology | HIV-1 - genetics | HIV Antibodies - chemistry | Cross Reactions | Antibodies, Monoclonal - genetics | Anti-HIV Agents - chemistry | HIV-1 - immunology | Single-Domain Antibodies - chemistry | HIV Infections - drug therapy | HIV Antibodies - genetics | Single-Domain Antibodies - genetics | Anti-HIV Agents - immunology | Index Medicus | Vaccines and Antiviral Agents
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5. Full Text Genetically engineered red cells expressing single domain camelid antibodies confer long-Term protection against botulinum neurotoxin
by Huang, Nai-Jia and Pishesha, Novalia and Mukherjee, Jean and Zhang, Sicai and Deshycka, Rhogerry and Sudaryo, Valentino and Dong, Min and Shoemaker, Charles B and Lodish, Harvey F
Nature communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 423 - 13
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Metalloendopeptidases - genetics | Antibodies, Neutralizing - administration & dosage | Botulinum Toxins, Type A - toxicity | Glycophorin - metabolism | Membrane Glycoproteins - metabolism | Single-Domain Antibodies - metabolism | Humans | Antibodies, Neutralizing - metabolism | Metalloendopeptidases - metabolism | Erythroid Precursor Cells - virology | Botulism - therapy | Botulism - etiology | Retroviridae - metabolism | Retroviridae - genetics | Erythroid Precursor Cells - transplantation | Erythrocyte Transfusion | Mice, Inbred C57BL | Genetic Vectors - metabolism | Glycophorin - genetics | Antibodies, Neutralizing - genetics | Single-Domain Antibodies - administration & dosage | Genetic Vectors - genetics | Membrane Glycoproteins - genetics | Animals | Genetic Engineering | Erythrocytes - virology | Erythrocytes - metabolism | Erythroid Precursor Cells - metabolism | Mice | Botulinum Toxins, Type A - metabolism | Single-Domain Antibodies - genetics | Infusion | Red blood cells | Blood circulation | Botulinum toxin type A | Blood cells | Erythrocytes | Antibodies | Neurotoxin A | Genetic engineering | Index Medicus
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6. Full Text Inhibition of HCV replication by humanized-single domain transbodies to NS4B
by Glab-ampai, Kittirat and Malik, Aijaz Ahmad and Chulanetra, Monrat and Thanongsaksrikul, Jeeraphong and Thueng-in, Kanyarat and Srimanote, Potjanee and Tongtawe, Pongsri and Chaicumpa, Wanpen
Biochemical and biophysical research communications, ISSN 0006-291X, 08/2016, Volume 476, Issue 4, pp. 654 - 664
Direct acting anti-HCV | Transbody | Hepatitis C virus | Humanized-nanobody | NS4B | qRT-PCR | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Hepacivirus - immunology | Virus Replication - genetics | Humans | Immunity, Innate - genetics | Hepacivirus - genetics | Antibodies, Monoclonal, Humanized - genetics | Antibodies, Monoclonal, Humanized - administration & dosage | Transfection | Antiviral Agents - chemistry | Computer Simulation | Carrier Proteins - administration & dosage | Carrier Proteins - chemistry | Hepacivirus - physiology | Antibodies, Viral - administration & dosage | Cell-Penetrating Peptides - chemistry | Viral Nonstructural Proteins - immunology | Cell Line | Cell-Penetrating Peptides - genetics | Models, Molecular | Recombinant Proteins - chemistry | Viral Nonstructural Proteins - genetics | Virus Replication - immunology | Recombinant Proteins - genetics | Single-Domain Antibodies - administration & dosage | Antiviral Agents - administration & dosage | Viral Nonstructural Proteins - physiology | Carrier Proteins - genetics | Recombinant Proteins - immunology | Single-Domain Antibodies - chemistry | Cell Surface Display Techniques | Antibodies, Viral - chemistry | Cell-Penetrating Peptides - administration & dosage | Single-Domain Antibodies - genetics | Virus Replication - physiology | Antibodies, Viral - genetics | Antibodies, Monoclonal, Humanized - chemistry | Proteins | Antiviral agents | Biological products | RNA | Escherichia coli | Hepatitis C | Health aspects | Protein binding | Index Medicus
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7. Full Text Neutralization of Clostridium difficile toxin A with single-domain antibodies targeting the cell receptor binding domain
by Hussack, Greg and Arbabi-Ghahroudi, Mehdi and Van Faassen, Henk and Songer, J. Glenn and Ng, Kenneth K.-S and MacKenzie, Roger and Tanha, Jamshid
The Journal of biological chemistry, ISSN 0021-9258, 03/2011, Volume 286, Issue 11, pp. 8961 - 8976
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Enterocolitis, Pseudomembranous - therapy | Protein Structure, Tertiary | Clostridioides difficile - immunology | Bacterial Toxins - immunology | Humans | Male | Antibodies, Neutralizing - genetics | Epitopes - genetics | Epitopes - immunology | Antibodies, Neutralizing - immunology | Camelids, New World | Enterotoxins - genetics | Animals | Single-Chain Antibodies - genetics | Enterotoxins - immunology | Antibodies, Bacterial - genetics | Enterocolitis, Pseudomembranous - immunology | Clostridioides difficile - genetics | Antibodies, Bacterial - immunology | Bacterial Toxins - genetics | Immunoglobulin Heavy Chains - immunology | Immunoglobulin Heavy Chains - genetics | Single-Chain Antibodies - immunology | Index Medicus | Protein Structure and Folding | Epitope Mapping | Toxin A | Immunology | Single-domain Antibody | Clostridium difficile | VHH | Antibodies | Toxins | Endotoxin
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8. Full Text Immunotoxin targeting glypican-3 regresses liver cancer via dual inhibition of Wnt signalling and protein synthesis
by Gao, Wei and Tang, Zhewei and Zhang, Yi-Fan and Feng, Mingqian and Qian, Min and Dimitrov, Dimiter S and Ho, Mitchell
Nature communications, ISSN 2041-1723, 03/2015, Volume 6, Issue 1, pp. 6536 - 6536
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Recombinant Fusion Proteins - immunology | Hepatoblastoma - genetics | Liver - pathology | Humans | Glypicans - antagonists & inhibitors | Antineoplastic Agents - administration & dosage | Liver - immunology | Liver - drug effects | Bacterial Toxins - genetics | Liver Neoplasms - pathology | Antibodies, Monoclonal - immunology | Gene Expression | Exotoxins - chemistry | Liver Neoplasms - genetics | Signal Transduction | Antineoplastic Agents - immunology | Bacterial Toxins - immunology | Exotoxins - immunology | Liver Neoplasms - immunology | Remission Induction | Bacterial Toxins - chemistry | Wnt Proteins - immunology | Exotoxins - genetics | Recombinant Fusion Proteins - genetics | Protein Biosynthesis - drug effects | Mice | Single-Domain Antibodies - genetics | Wnt Proteins - antagonists & inhibitors | Hepatoblastoma - immunology | Virulence Factors - genetics | Hepatoblastoma - drug therapy | Virulence Factors - immunology | Molecular Targeted Therapy | Single-Domain Antibodies - immunology | Wnt Proteins - genetics | Female | Immunotoxins - chemistry | Recombinant Fusion Proteins - administration & dosage | ADP Ribose Transferases - chemistry | Hepatoblastoma - pathology | ADP Ribose Transferases - immunology | Liver Neoplasms - drug therapy | Glypicans - immunology | Virulence Factors - chemistry | Antineoplastic Agents - chemistry | Glypicans - genetics | Hep G2 Cells | Xenograft Model Antitumor Assays | ADP Ribose Transferases - genetics | Antibodies, Monoclonal - genetics | Immunotoxins - genetics | Animals | Tumor Burden - drug effects | Index Medicus
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9. Full Text Comparative analysis of fusion tags used to functionalize recombinant antibodies
by Veggiani, Gianluca and Giabbai, Barbara and Semrau, Marta S and Medagli, Barbara and Riccio, Vincenzo and Bajc, Gregor and Storici, Paola and de Marco, Ario
Protein expression and purification, ISSN 1046-5928, 02/2020, Volume 166, pp. 105505 - 105505
Antibody functionalization | Fusion tags | Recombinant antibodies | Nanobodies | Sortase | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Biochemical Research Methods | Science & Technology | Binding, Competitive | Receptor, ErbB-2 - genetics | Oxidoreductases - genetics | Escherichia coli | Receptor, ErbB-2 - chemistry | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - chemistry | Oxidoreductases - chemistry | Genetic Vectors - genetics | Protein Disulfide-Isomerases - genetics | Single-Domain Antibodies - chemistry | Escherichia coli Proteins - genetics | Recombinant Fusion Proteins - genetics | Protein Disulfide-Isomerases - chemistry | Cysteine - metabolism | Protein Stability | Escherichia coli Proteins - chemistry | Green Fluorescent Proteins - chemistry | Single-Domain Antibodies - genetics | Index Medicus
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10. Full Text Comparative analysis of nanobody sequence and structure data
by Mitchell, Laura S and Colwell, Lucy J
Proteins, structure, function, and bioinformatics, ISSN 0887-3585, 07/2018, Volume 86, Issue 7, pp. 697 - 706
VH | antibody | framework | single domain antibody | heavy chain antibody | loop | VHH | HcAb | camelid | Biochemistry & Molecular Biology | Biophysics | Life Sciences & Biomedicine | Science & Technology | Antibody Specificity | Sequence Alignment | Single-Domain Antibodies - chemistry | Antibodies - chemistry | Antibodies - immunology | Models, Molecular | Antibodies - genetics | Protein Conformation | Structure-Activity Relationship | Binding Sites, Antibody | Single-Domain Antibodies - genetics | Viral antibodies | Antigens | Crystals | Antibodies | Comparative analysis | Structure | Protein binding | Proteins | Molecular chains | Crystal structure | Index Medicus
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