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Nature Biotechnology, ISSN 1087-0156, 04/2009, Volume 27, Issue 4, pp. 331 - 337
Journal Article
Chemical Science, ISSN 2041-6520, 12/2016, Volume 8, Issue 1, pp. 63 - 77
Recent advances in nanomedicine have shown that dramatic improvements in nanoparticle therapeutics and diagnostics can be achieved through the use of disease... 
IRON-OXIDE NANOPARTICLES | BREAST-CANCER | IN-VITRO | DRUG-DELIVERY | MESOPOROUS SILICA NANOPARTICLES | BLOCK-COPOLYMER MICELLES | SINGLE-DOMAIN ANTIBODIES | MAGNETIC NANOPARTICLES | CHEMISTRY, MULTIDISCIPLINARY | CARBON NANOTUBES | QUANTUM DOTS | Nanoparticles | Conjugates | Switches | Antibodies | Fragments | Ligands | Diagnostic systems | Nanostructure | Chemistry
Journal Article
Journal of Immunological Methods, ISSN 0022-1759, 08/2018, Volume 459, pp. 20 - 28
Journal Article
Process Biochemistry, ISSN 1359-5113, 08/2013, Volume 48, Issue 8, pp. 1242 - 1251
Journal Article
Protein Science, ISSN 0961-8368, 03/2002, Volume 11, Issue 3, pp. 500 - 515
A variety of techniques, including high‐pressure unfolding monitored by Fourier transform infrared spectroscopy, fluorescence, circular dichroism, and surface... 
CDR, complementary determining region | circular dichroism | IPTG, isopropyl β‐D‐thiogalactopyranoside | fluorescence | surface plasmon resonance | ANS, 8‐anilino‐1‐naphtalene‐sulfonic acid | protein folding | Fab, Fv, scFv, and dsFv, antigen‐binding fragment, variable fragment, single‐chain variable fragment, and disulphide stabilized variable fragment of conventional antibodies, respectively | GdmCl, guanidinium chloride | variable domain of immunoglobulin light chain | H, variable domain of camelid heavy‐chain antibody | FTIR, Fourier transform infrared | BSA, bovine serum albumin | csm, center of the spectral mass | MOPS, 3‐N‐morpholinopropanosulfonic acid | protein stability | high pressure | VH, variable domain of immunoglobulin heavy chain | HEPES, N‐(2‐hydroxyethyl)piperazine‐N′‐2‐ethanesulfonic acid | RU, resonance units | Fourier transform infrared spectroscopy | Camel heavy‐chain antibodies | IR, infrared | SPR, surface plasmon resonance | CD, circular dichroism | Protein folding | Fluorescence | Protein stability | Surface plasmon resonance | Camel heavy-chain antibodies | Circular dichroism | High pressure | HEAVY-CHAIN ANTIBODIES | HIGH-PRESSURE | MOLTEN GLOBULE STATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MONOCLONAL-ANTIBODY | V-H | TRANSFORM INFRARED-SPECTROSCOPY | BETA-LACTAMASE | FOURIER SELF-DECONVOLUTION | SECONDARY STRUCTURE | camel heavy-chain antibodies | Protein Structure, Tertiary | Amino Acid Sequence | Immunoglobulin Fragments - chemistry | Camelus | beta-Lactamases - immunology | Humans | Molecular Sequence Data | Spectrometry, Fluorescence | Hot Temperature | Spectroscopy, Fourier Transform Infrared | Protein Folding | Bacterial Proteins | Muramidase - immunology | Camelids, New World | Animals | Immunoglobulin Fragments - immunology | Protein Denaturation | Protein Conformation | Index Medicus
Journal Article
JOURNAL OF NUCLEAR MEDICINE, ISSN 0161-5505, 08/2015, Volume 56, Issue 8, pp. 1265 - 1271
Tumor-associated macrophages constitute a major component of the stroma of solid tumors, encompassing distinct subpopulations with different characteristics... 
ACTIVATION | camelid single-domain antibody fragment (sdAb) | SUBSETS | N-SUCCINIMIDYL | BIODISTRIBUTION | CANCER | F-18 | macrophage mannose receptor (MMR) | POSITRON-EMISSION-TOMOGRAPHY | NANOBODIES | tumor microenvironment | RADIOLOGY, NUCLEAR MEDICINE & MEDICAL IMAGING | PET | MICROENVIRONMENTS | PROGRESSION
Journal Article
Frontiers in Immunology, ISSN 1664-3224, 10/2017, Volume 8, pp. 1287 - 1287
The use of antibody-based therapeutics has proven very promising for clinical applications in cancer patients, with multiple examples of antibodies and... 
Molecular imaging | Nanobody | Antibody | Antibody fragments | Cancer therapy | Single-domain antibodies | HALF-LIFE | antibody | PENETRATION | MODELING ANALYSIS | nanobody | IMMUNOLOGY | molecular imaging | ALBUMIN-BINDING DOMAIN | CANCER | cancer therapy | antibody fragments | TRANSPORT | NEONATAL FC-RECEPTOR | AFFINITY | single-domain antibodies | SINGLE-CHAIN FV | DIFFUSION
Journal Article
MOLECULAR PHARMACEUTICS, ISSN 1543-8384, 11/2014, Volume 11, Issue 11, pp. 3965 - 3973
Engineered antibody fragments offer faster delivery with retained tumor specificity and rapid clearance from nontumor tissues. Here, we demonstrate that... 
minibody | MEDICINE, RESEARCH & EXPERIMENTAL | RADIOIMMUNOTHERAPY | EXTRACELLULAR DOMAIN | Cys-diabody | MEMBRANE ANTIGEN PSMA | CANCER | RADIOLABELED MONOCLONAL-ANTIBODIES | PSMA | INTERNALIZATION | 16-BETA-F-18-FLUORO-5-ALPHA-DIHYDROTESTOSTERONE | PHARMACOLOGY & PHARMACY | huJ591 | CARCINOEMBRYONIC ANTIGEN | EXPRESSION | PET
Journal Article