Nanobody Technology: A Versatile Toolkit for Microscopic Imaging, Protein–Protein Interaction Analysis, and Protein Function Exploration
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Hamers-Casterman, 1993, Naturally occurring antibodies devoid of light chains, Nature, 363, 446, 10.1038/363446a0
Muyldermans, 2013, Nanobodies: natural single-domain antibodies, Annual Review of Biochemistry, 775
Ghahroudi, 1997, Selection and identification of single domain antibody fragments from camel heavy-chain antibodies, FEBS Lett, 414, 521, 10.1016/s0014-5793(97)01062-4
Muyldermans, 2001, Single domain camel antibodies: current status, J Biotechnol, 74, 277, 10.1016/S1389-0352(01)00021-6
Van den Abbeele, 2010, A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction, Cell Mol Life Sci, 67, 1519, 10.1007/s00018-010-0266-1
Van Audenhove, 2013, Mapping cytoskeletal protein function in cells by means of nanobodies, Cytoskeleton (Hoboken), 70, 604, 10.1002/cm.21122
Beghein, 2016, A new survivin tracer tracks, delocalizes and captures endogenous survivin at different subcellular locations and in distinct organelles, Sci Rep, 6, 31177, 10.1038/srep31177
Maier, 2015, Real-time analysis of epithelial-mesenchmal transition using fluorescent single-domain antibodies, Sci Rep, 5, 13402, 10.1038/srep13402
Jullien, 2016, Chromatibody, a novel non-invasive molecular tool to explore and manipulate chromatin in living cells, J Cell Sci, 129, 2673, 10.1242/jcs.183103
De Genst, 2006, Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies, Proc Natl Acad Sci U S A, 103, 4586, 10.1073/pnas.0505379103
Desmyter, 1996, Crystal structure of a camel single-domain V-H antibody fragment in complex with lysozyme, Nat Struct Biol, 3, 803, 10.1038/nsb0996-803
Delanote, 2010, An alpaca single-domain antibody blocks filopodia formation by obstructing L-plastin-mediated F-actin bundling, FASEB J, 24, 105, 10.1096/fj.09-134304
Braun, 2016, Peptides in headlock – a novel high-affinity and versatile peptide-binding nanobody for proteomics and microscopy, Sci Rep, 6, 19211, 10.1038/srep19211
De Genst, 2010, Structure and properties of a complex of alpha-synuclein and a single-domain camelid antibody, J Mol Biol, 402, 326, 10.1016/j.jmb.2010.07.001
Thueng-in, 2012, Cell penetrable humanized-VH/VHH that inhibit RNA dependent RNA polymerase (NS5B) of HCV, PLoS One, 7, e49254, 10.1371/journal.pone.0049254
Van Impe, 2013, A nanobody targeting the F-actin capping protein CapG restrains breast cancer metastasis, Breast Cancer Res, 15, R116, 10.1186/bcr3585
Blanco-Toribio, 2010, Direct injection of functional single-domain antibodies from E. coli into human cells, PLoS One, 5, e15227, 10.1371/journal.pone.0015227
Van Audenhove, 2016, Nanobodies as versatile tools to understand, diagnose, visualize and treat cancer, EBioMedicine, 8, 40, 10.1016/j.ebiom.2016.04.028
Steeland, 2016, Nanobodies as therapeutics: big opportunities for small antibodies, Drug Discov Today, 21, 1076, 10.1016/j.drudis.2016.04.003
de Bruin, 2016, Highly specific and potently activating V gamma 9V delta 2-T cell specific nanobodies for diagnostic and therapeutic applications, Clin Immunol, 169, 128, 10.1016/j.clim.2016.06.012
Peyrassol, 2016, Development by genetic immunization of monovalent antibodies (nanobodies) behaving as antagonists of the human ChemR23 receptor, J Immunol, 196, 2893, 10.4049/jimmunol.1500888
Ries, 2012, A simple, versatile method for GFP-based super-resolution microscopy via nanobodies, Nat Methods, 9, 582, 10.1038/nmeth.1991
Chamma, 2016, Mapping the dynamics and nanoscale organization of synaptic adhesion proteins using monomeric streptavidin, Nat Commun, 7, 10773, 10.1038/ncomms10773
Platonova, 2015, Single-molecule microscopy of molecules tagged with GFP or RFP derivatives in mammalian cells using nanobody binders, Methods, 88, 89, 10.1016/j.ymeth.2015.06.018
Szymborska, 2013, Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging, Science, 341, 655, 10.1126/science.1240672
Mikhaylova, 2015, Resolving bundled microtubules using anti-tubulin nanobodies, Nat Commun, 6, 7933, 10.1038/ncomms8933
Pleiner, 2015, Nanobodies: site-specific labeling for super-resolution imaging, rapid epitope-mapping and native protein complex isolation, Elife, 4, e11349, 10.7554/eLife.11349
Massa, 2014, Site-specific labeling of cysteine-tagged camelid single-domain antibody-fragments for use in molecular imaging, Bioconjug Chem, 25, 979, 10.1021/bc500111t
Massa, 2016, Sortase A-mediated site-specific labeling of camelid single-domain antibody-fragments: a versatile strategy for multiple molecular imaging modalities, Contrast Media Mol Imaging, 11, 328, 10.1002/cmmi.1696
Antonatou, 2016, Singlet oxygen-induced furan oxidation for site-specific and chemoselective peptide ligation, Chemistry, 22, 8457, 10.1002/chem.201601113
Traenkle, 2015, Monitoring interactions and dynamics of endogenous beta-catenin with intracellular nanobodies in living cells, Mol Cell Proteomics, 14, 707, 10.1074/mcp.M114.044016
Van Overbeke, 2014, Chaperone nanobodies protect gelsolin against MT1-MMP degradation and alleviate amyloid burden in the gelsolin amyloidosis mouse model, Mol Ther, 22, 1768, 10.1038/mt.2014.132
Panza, 2015, Live imaging of endogenous protein dynamics in zebrafish using chromobodies, Development, 142, 1879, 10.1242/dev.118943
Huang, 2010, Breaking the diffraction barrier: super-resolution imaging of cells, Cell, 143, 1047, 10.1016/j.cell.2010.12.002
Huang, 2009, Super-resolution fluorescence microscopy, Annu Rev Biochem, 78, 993, 10.1146/annurev.biochem.77.061906.092014
Deschout, 2014, Precisely and accurately localizing single emitters in fluorescence microscopy, Nat Methods, 11, 253, 10.1038/nmeth.2843
Bates, 2007, Multicolor super-resolution imaging with photo-switchable fluorescent probes, Science, 317, 1749, 10.1126/science.1146598
Guignet, 2004, Reversible site-selective labeling of membrane proteins in live cells, Nat Biotechnol, 22, 440, 10.1038/nbt954
Popp, 2007, Sortagging: a versatile method for protein labeling, Nat Chem Biol, 3, 707, 10.1038/nchembio.2007.31
Huang, 2008, Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy, Science, 319, 810, 10.1126/science.1153529
Rothbauer, 2006, Targeting and tracing antigens in live cells with fluorescent nanobodies, Nat Methods, 3, 887, 10.1038/nmeth953
Herce, 2013, Visualization and targeted disruption of protein interactions in living cells, Nat Commun, 4, 2660, 10.1038/ncomms3660
Künzl, 2016, Receptor-mediated sorting of soluble vacuolar proteins ends at the trans-Golgi network/early endosome, Nat Plants, 2, 16017, 10.1038/nplants.2016.17
Drees, 2016, Engineered upconversion nanoparticles for resolving protein interactions inside living cells, Angew Chem Int Ed Engl, 55, 11668, 10.1002/anie.201603028
Shi, 2015, A strategy for dissecting the architectures of native macromolecular assemblies, Nat Methods, 12, 1135, 10.1038/nmeth.3617
Eyckerman, 2016, Trapping mammalian protein complexes in viral particles, Nat Commun, 7, 11416, 10.1038/ncomms11416
Roux, 2012, A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells, J Cell Biol, 196, 801, 10.1083/jcb.201112098
Lee, 2015, Hydrogen-deuterium exchange mass spectrometry for determining protein structural changes in drug discovery, Arch Pharm Res, 38, 1737, 10.1007/s12272-015-0584-9
Malito, 2013, Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen, Proc Natl Acad Sci U S A, 110, 3304, 10.1073/pnas.1222845110
Yan, 2016, Isomerization and oxidation in the complementarity-determining regions of a monoclonal antibody: a study of the modification-structure-function correlations by hydrogen-deuterium exchange mass spectrometry, Anal Chem, 88, 2041, 10.1021/acs.analchem.5b02800
Jensen, 2015, Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometry, Mol Cell Proteomics, 14, 148, 10.1074/mcp.M114.042044
Smits, 2016, Characterizing protein-protein interactions using mass spectrometry: challenges and opportunities, Trends Biotechnol, 34, 825, 10.1016/j.tibtech.2016.02.014
Otera, 2012, Pex5p imports folded tetrameric catalase by interaction with Pex13p, Traffic, 13, 1364, 10.1111/j.1600-0854.2012.01391.x
McNew, 1994, An oligomeric protein is imported into peroxisomes in-vivo, J Cell Biol, 127, 1245, 10.1083/jcb.127.5.1245
Glover, 1994, Saccharomyces cerevisiae peroxisomal thiolase is imported as a dimer, Proc Natl Acad Sci U S A, 91, 10541, 10.1073/pnas.91.22.10541
Yang, 2001, Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a partner, Dci1p, Eur J Cell Biol, 80, 126, 10.1078/0171-9335-00144
Islinger, 2009, Hitchhiking of Cu/Zn superoxide dismutase to peroxisomes – evidence for a natural piggyback import mechanism in mammals, Traffic, 10, 1711, 10.1111/j.1600-0854.2009.00966.x
Freitas, 2015, The peroxisomal protein import machinery displays a preference for monomeric substrates, Open Biol, 5, 140236, 10.1098/rsob.140236
Yates, 2005, Proteomics of organelles and large cellular structures, Nat Rev Mol Cell Biol, 6, 702, 10.1038/nrm1711
Wiese, 2007, Proteomics characterization of mouse kidney peroxisomes by tandem mass spectrometry and protein correlation profiling, Mol Cell Proteomics, 6, 2045, 10.1074/mcp.M700169-MCP200
Kikuchi, 2004, Proteomic analysis of rat liver peroxisome – presence of peroxisome-specific isozyme of Lon protease, J Biol Chem, 279, 421, 10.1074/jbc.M305623200
Newnham, 2015, Functional inhibition of β-catenin-mediated Wnt signaling by intracellular VHH antibodies, MAbs, 7, 180, 10.4161/19420862.2015.989023
Van Audenhove, 2014, Stratifying fascin and cortactin function in invadopodium formation using inhibitory nanobodies and targeted subcellular delocalization, FASEB J, 28, 1805, 10.1096/fj.13-242537
Van Audenhove, 2015, Fascin actin bundling controls podosome turnover and disassembly while cortactin is involved in podosome assembly by its SH3 domain in THP-1 macrophages and dendritic cells, Biochim Biophys Acta, 1853, 940, 10.1016/j.bbamcr.2015.01.003
Van Audenhove, 2016, Fascin rigidity and L-plastin flexibility cooperate in cancer cell invadopodia and filopodia, J Biol Chem, 291, 9148, 10.1074/jbc.M115.706937
Bertier, 2017, Inhibitory cortactin nanobodies delineate the role of NTA- and SH3-domain-specific functions during invadopodium formation and cancer cell invasion, FASEB J, 31, 2460, 10.1096/fj.201600810RR
Bethuyne, 2014, A nanobody modulates the p53 transcriptional program without perturbing its functional architecture, Nucleic Acids Res, 42, 12928, 10.1093/nar/gku962
Rasmussen, 2011, Structure of a nanobody-stabilized active state of the β(2) adrenoceptor, Nature, 469, 175, 10.1038/nature09648
Staus, 2014, Regulation of β(2)-adrenergic receptor function by conformationally selective single-domain intrabodies, Mol Pharmacol, 85, 472, 10.1124/mol.113.089516
Staus, 2016, Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation, Nature, 535, 448, 10.1038/nature18636
Caussinus, 2012, Fluorescent fusion protein knockout mediated by anti-GFP nanobody, Nat Struct Mol Biol, 19, 117, 10.1038/nsmb.2180
Shin, 2015, Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins, Sci Rep, 5, 14269, 10.1038/srep14269
Fulcher, 2016, An affinity-directed protein missile system for targeted proteolysis, Open Biol, 6, 10.1098/rsob.160255
Kromann-Hansen, 2016, A camelid-derived antibody fragment targeting the active site of a serine protease balances between inhibitor and substrate behavior, J Biol Chem, 291, 15156, 10.1074/jbc.M116.732503
Rudolph, 2016, Structural analysis of nested neutralizing and non-neutralizing B cell epitopes on ricin toxin’s enzymatic subunit, Proteins, 84, 1162, 10.1002/prot.25062
Rudolph, 2017, Structural analysis of single domain antibodies bound to a second neutralizing hot spot on ricin toxin’s enzymatic subunit, J Biol Chem, 292, 872, 10.1074/jbc.M116.758102
Jackson, 2010, Recognizing and avoiding siRNA off-target effects for target identification and therapeutic application, Nat Rev Drug Discov, 9, 57, 10.1038/nrd3010
Kok, 2015, Reverse genetic screening reveals poor correlation between morpholino-induced and mutant phenotypes in zebrafish, Dev Cell, 32, 97, 10.1016/j.devcel.2014.11.018
Renicke, 2013, A LOV2 domain-based optogenetic tool to control protein degradation and cellular function, Chem Biol, 20, 619, 10.1016/j.chembiol.2013.03.005
Holland, 2012, Inducible, reversible system for the rapid and complete degradation of proteins in mammalian cells, Proc Natl Acad Sci U S A, 109, E3350, 10.1073/pnas.1216880109
Harder, 2008, TEV protease-mediated cleavage in Drosophila as a tool to analyze protein functions in living organisms, Biotechniques, 44, 765, 10.2144/000112884
Errington, 2012, Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase, Structure, 20, 1141, 10.1016/j.str.2012.04.009
Tang, 2016, Detection and manipulation of live antigen-expressing cells using conditionally stable nanobodies, Elife, 5, 10.7554/eLife.15312
Vance, 2013, Stepwise engineering of heterodimeric single domain camelid VHH antibodies that passively protect mice from ricin toxin, J Biol Chem, 288, 36538, 10.1074/jbc.M113.519207