The DOI matches its Crossref record; 292 of the 292 references it cites were found in a registry or an index.
The Controlled Display of Biomolecules on Nanoparticles: A Challenge Suited to Bioorthogonal Chemistry
Abstract
Interest in developing diverse nanoparticle (NP)-biological composite materials continues to grow almost unabated. This is motivated primarily by the desire to simultaneously exploit the properties of both NP and biological components in new hybrid devices or materials that can be applied in areas ranging from energy harvesting and nanoscale electronics to biomedical diagnostics. The utility and effectiveness of these composites will be predicated on the ability to assemble these structures with control over NP/biomolecule ratio, biomolecular orientation, biomolecular activity, and the separation distance within the NP-bioconjugate architecture. This degree of control will be especially critical in creating theranostic NP-bioconjugates that, as a single vector, are capable of multiple functions in vivo, including targeting, image contrast, biosensing, and drug delivery. In this review, a perspective is given on current and developing chemistries that can provide improved control in the preparation of NP-bioconjugates. The nanoscale properties intrinsic to several prominent NP materials are briefly described to highlight the motivation behind their use. NP materials of interest include quantum dots, carbon nanotubes, viral capsids, liposomes, and NPs composed of gold, lanthanides, silica, polymers, or magnetic materials. This review includes a critical discussion on the design considerations for NP-bioconjugates and the unique challenges associated with chemistry at the biological-nanoscale interface-the liabilities of traditional bioconjugation chemistries being particularly prominent therein. Select bioorthogonal chemistries that can address these challenges are reviewed in detail, and include chemoselective ligations (e.g., hydrazone and Staudinger ligation), cycloaddition reactions in click chemistry (e.g., azide-alkyne cyclyoaddition, tetrazine ligation), metal-affinity coordination (e.g., polyhistidine), enzyme driven modifications (e.g., HaloTag, biotin ligase), and other site-specific chemistries. The benefits and liabilities of particular chemistries are discussed by highlighting relevant NP-bioconjugation examples from the literature. Potential chemistries that have not yet been applied to NPs are also discussed, and an outlook on future developments in this field is given.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Items 201–292 of 292
A Reactive Peptidic Linker for Self-Assembling Hybrid Quantum Dot−DNA Bioconjugates
Medintz, I. L., Berti, L., Pons, T., Grimes, A. F., English, D. S., Alessandrini, A., Facci, P., & Mattoussi, H. (2007) · Nano Letters · doi:10.1021/nl070782v · Cited by 196
Self-citationNear-Infrared Fluorescent Materials for Sensing of Biological Targets
Amiot, C., Xu, S., Liang, S., Pan, L., & Zhao, J. (2008) · Sensors · doi:10.3390/s8053082 · Cited by 196
Bundy, B. C., & Swartz, J. R. (2010) · Bioconjugate Chemistry · doi:10.1021/bc9002844 · Cited by 194
A Review on Biomedical Applications of Single-Walled Carbon Nanotubes
Liang, F., & Chen, B. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710789957742 · Cited by 193
Polymer coating of quantum dots – A powerful tool toward diagnostics and sensorics
Hezinger, A. F. E., Teßmar, J., & Göpferich, A. (2008) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2007.05.013 · Cited by 190
Time-resolved detection of lanthanide luminescence for ultrasensitive bioanalytical assays
Gudgin Dickson, E. F., Pollak, A., & Diamandis, E. P. (1995) · Journal of Photochemistry and Photobiology B: Biology · doi:10.1016/1011-1344(94)07086-4 · Cited by 182
Unnatural Amino Acid Incorporation into Virus-Like Particles
Strable, E., Prasuhn, D. E., Udit, A. K., Brown, S., Link, A. J., Ngo, J. T., Lander, G., Quispe, J., Potter, C. S., Carragher, B., et al. (2008) · Bioconjugate Chemistry · doi:10.1021/bc700390r · Cited by 181
Self-citationGupta, S. S., Raja, K. S., Kaltgrad, E., Strable, E., & Finn, M. G. (2005) · Chemical Communications · doi:10.1039/b502444g · Cited by 179
Chemical probes shed light on protein function
O’Hare, H. M., Johnsson, K., & Gautier, A. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.07.005 · Cited by 177
Characterization of the Functional Binding Properties of Antibody Conjugated Quantum Dots
Pathak, S., Davidson, M. C., & Silva, G. A. (2007) · Nano Letters · doi:10.1021/nl062706i · Cited by 177
A Genetically Encoded Boronate‐Containing Amino Acid
Brustad, E., Bushey, M. L., Lee, J. W., Groff, D., Liu, W., & Schultz, P. G. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200803240 · Cited by 174
Azide-Derivatized Gold Nanorods: Functional Materials for “Click” Chemistry
Gole, A., & Murphy, C. J. (2008) · Langmuir · doi:10.1021/la7026303 · Cited by 173
High Relaxivity Gadolinium Hydroxypyridonate−Viral Capsid Conjugates: Nanosized MRI Contrast Agents1
Datta, A., Hooker, J. M., Botta, M., Francis, M. B., Aime, S., & Raymond, K. N. (2008) · Journal of the American Chemical Society · doi:10.1021/ja0765363 · Cited by 172
Molecular Mapping of Tumor Heterogeneity on Clinical Tissue Specimens with Multiplexed Quantum Dots
Liu, J., Lau, S. K., Varma, V. A., Moffitt, R. A., Caldwell, M., Liu, T., Young, A. N., Petros, J. A., Osunkoya, A. O., Krogstad, T., et al. (2010) · ACS Nano · doi:10.1021/nn100213v · Cited by 168
Xia, Z., Xing, Y., So, M.-K., Koh, A. L., Sinclair, R., & Rao, J. (2008) · Analytical Chemistry · doi:10.1021/ac801562f · Cited by 168
Intracellular Delivery of Quantum Dot−Protein Cargos Mediated by Cell Penetrating Peptides
Medintz, I. L., Pons, T., Delehanty, J. B., Susumu, K., Brunel, F. M., Dawson, P. E., & Mattoussi, H. (2008) · Bioconjugate Chemistry · doi:10.1021/bc800089r · Cited by 167
Self-citationSolution Synthesis of Alkyl- and Alkyl/Alkoxy-Capped Silicon Nanoparticles via Oxidation of Mg2Si
Pettigrew, K. A., Liu, Q., Power, P. P., & Kauzlarich, S. M. (2003) · Chemistry of Materials · doi:10.1021/cm034403k · Cited by 166
Bernardin, A., Cazet, A., Guyon, L., Delannoy, P., Vinet, F., Bonnaffé, D., & Texier, I. (2010) · Bioconjugate Chemistry · doi:10.1021/bc900564w · Cited by 165
Facile Chemoselective Synthesis of Dehydroalanine-Containing Peptides
Okeley, N. M., Zhu, Y., & van der Donk, W. A. (2000) · Organic Letters · doi:10.1021/ol006485d · Cited by 165
Feng, W., Sun, L.-D., Zhang, Y.-W., & Yan, C.-H. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.02.007 · Cited by 165
In Vivo Synthesis of Diverse Metal Nanoparticles by Recombinant Escherichia coli
Park, T. J., Lee, S. Y., Heo, N. S., & Seo, T. S. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201001524 · Cited by 164
HaloTag Protein‐Mediated Site‐Specific Conjugation of Bioluminescent Proteins to Quantum Dots
Zhang, Y., So, M., Loening, A. M., Yao, H., Gambhir, S. S., & Rao, J. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200601197 · Cited by 164
Stamped microbattery electrodes based on self-assembled M13 viruses
Nam, K. T., Wartena, R., Yoo, P. J., Liau, F. W., Lee, Y. J., Chiang, Y.-M., Hammond, P. T., & Belcher, A. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711620105 · Cited by 160
Brunel, F. M., Lewis, J. D., Destito, G., Steinmetz, N. F., Manchester, M., Stuhlmann, H., & Dawson, P. E. (2010) · Nano Letters · doi:10.1021/nl1002526 · Cited by 155
Self-citationOlefin Metathesis for Site‐Selective Protein Modification
Lin, Y. A., Chalker, J. M., & Davis, B. G. (2009) · ChemBioChem · doi:10.1002/cbic.200900002 · Cited by 155
Lallana, E., Fernández-Megía, E., & Riguera, R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8100243 · Cited by 153
Jiang, W., Singhal, A., Zheng, J., Wang, C., & Chan, W. C. W. (2006) · Chemistry of Materials · doi:10.1021/cm061311x · Cited by 152
Recent developments in the site‐specific immobilization of proteins onto solid supports
Camarero, J. A. (2007) · Biopolymers · doi:10.1002/bip.20803 · Cited by 152
Hooker, J. M., Datta, A., Botta, M., Raymond, K. N., & Francis, M. B. (2007) · Nano Letters · doi:10.1021/nl070512c · Cited by 144
Faulds, K., McKenzie, F., Smith, W. E., & Graham, D. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604265 · Cited by 142
Xie, H., Zhen, R., Wang, B., Feng, Y., Chen, P., & Hao, J. (2010) · The Journal of Physical Chemistry C · doi:10.1021/jp910753f · Cited by 141
Selective chemical labeling of proteins in living cells
Miller, L. W., & Cornish, V. W. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.12.007 · Cited by 140
Nanoparticles Comprising a Mixed Monolayer for Specific Bindings with Biomolecules
Zheng, M. S., & Huang, X. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047029d · Cited by 139
Virus hybrids as nanomaterials for biotechnology
Soto, C. M., & Ratna, B. R. (2010) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2010.07.004 · Cited by 136
Liu, Y., Feizi, T., Campanero‐Rhodes, M. A., Childs, R. A., Zhang, Y., Mulloy, B., Evans, P. G., Osborn, H. M. I., Otto, D. M. E., Crocker, P. R., et al. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.06.009 · Cited by 131
Sandhu, A., Handa, H., & Abe, M. (2010) · Nanotechnology · doi:10.1088/0957-4484/21/44/442001 · Cited by 131
Optimization of a Biomimetic Transamination Reaction
Scheck, R. A., Dedeo, M. T., Iavarone, A. T., & Francis, M. B. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802495w · Cited by 129
Buckyballs Meet Viral Nanoparticles: Candidates for Biomedicine
Steinmetz, N. F., Hong, V., Spoerke, E. D., Lu, P., Breitenkamp, K., Finn, M. G., & Manchester, M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja902293w · Cited by 128
Faulds, K., Jarvis, R. M., Smith, W. E., Graham, D., & Goodacre, R. (2008) · The Analyst · doi:10.1039/b800506k · Cited by 128
Olefin metathesis for chemical biology
Binder, J. B., & Raines, R. T. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.09.022 · Cited by 127
Cheung, E. N. M., Alvares, R. D. A., Oakden, W., Chaudhary, R., Hill, M. L., Pichaandi, J., Mo, G. C. H., Yip, C. M., Macdonald, P. M., Stanisz, G. J., et al. (2010) · Chemistry of Materials · doi:10.1021/cm101036a · Cited by 126
Immuno‐Polymeric Nanoparticles by Diels–Alder Chemistry
Shi, M., Wosnick, J. H., Ho, K., Keating, A., & Shoichet, M. S. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200701032 · Cited by 126
Quantitative Enhanced Raman Scattering of Labeled DNA from Gold and Silver Nanoparticles
Stokes, R. J., MacAskill, A., Lundahl, P. J., Smith, W. E., Faulds, K., & Graham, D. (2007) · Small · doi:10.1002/smll.200600662 · Cited by 126
Nanohybrids Composed of Quantum Dots and Cytochrome P450 as Photocatalysts
Ipe, B. I., & Niemeyer, C. M. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200503084 · Cited by 123
A Biosynthetic Route to Dehydroalanine‐Containing Proteins
Wang, J., Schiller, S., & Schultz, P. G. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702305 · Cited by 118
Functionalized Carbon Nanotubes for Probing and Modulating Molecular Functions
Ménard‐Moyon, C., Kostarelos, K., Prato, M., & Bianco, A. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.01.009 · Cited by 118
A Reagentless Biosensing Assembly Based on Quantum Dot–Donor Förster Resonance Energy Transfer
Medintz, I. L., Clapp, A. R., Melinger, J. S., Deschamps, J. R., & Mattoussi, H. M. (2005) · Advanced Materials · doi:10.1002/adma.200500722 · Cited by 117
Self-citationGehring, A. M., Lambalot, R. H., Vogel, K. W., Drueckhammer, D. G., & Walsh, C. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90233-7 · Cited by 115
Oxidative coupling of peptides to a virus capsid containing unnatural amino acids
Carrico, Z. M., Romanini, D. W., Mehl, R. A., & Francis, M. B. (2008) · Chemical Communications · doi:10.1039/b717826c · Cited by 114
Roullier, V., Clarke, S. J., You, C., Pinaud, F. F., Gouzer, G., Schaible, D., Marchi, V., Piehler, J., & Dahan, M. (2009) · Nano Letters · doi:10.1021/nl9001298 · Cited by 114
Surface Modification of Magnetic Nanoparticle via Cu(I)-Catalyzed Alkyne-azide [2 + 3] Cycloaddition
Lin, P., Ueng, S., Yu, S., Jan, M.-D., Adak, A. K., Yu, C., & Lin, C. (2007) · Organic Letters · doi:10.1021/ol070588f · Cited by 112
Potato Virus X as a Novel Platform for Potential Biomedical Applications
Steinmetz, N. F., Mertens, M. E., Taurog, R. E., Johnson, J. E., Commandeur, U., Fischer, R., & Manchester, M. (2009) · Nano Letters · doi:10.1021/nl9035753 · Cited by 111
Algar, W. R., & Krull, U. J. (2006) · Langmuir · doi:10.1021/la062217y · Cited by 110
Self-citationBanerjee, S. S., & Chen, D. (2008) · Nanotechnology · doi:10.1088/0957-4484/19/50/505104 · Cited by 106
Bioluminescent nanosensors for protease detection based upon gold nanoparticle–luciferase conjugates
Kim, Y., Daniel, W. L., Xia, Z., Xie, H., Mirkin, C. A., & Rao, J. (2009) · Chemical Communications · doi:10.1039/b915612g · Cited by 106
Plasma Clearance of Bacteriophage Qβ Particles as a Function of Surface Charge
Prasuhn, D. E., Singh, P. N. P., Strable, E., Brown, S. D., Manchester, M., & Finn, M. G. (2008) · Journal of the American Chemical Society · doi:10.1021/ja075937f · Cited by 104
Self-citationRegioselective Labeling of Antibodies through N-Terminal Transamination
Scheck, R. A., & Francis, M. B. (2007) · ACS Chemical Biology · doi:10.1021/cb6003959 · Cited by 102
Kodama, K., Fukuzawa, S., Nakayama, H., Kigawa, T., Sakamoto, K., Yabuki, T., Matsuda, N., Shirouzu, M., Takio, K., Tachibana, K., et al. (2005) · ChemBioChem · doi:10.1002/cbic.200500290 · Cited by 102
Site‐Specific Functionalization of Proteins by Organopalladium Reactions
Kodama, K., Fukuzawa, S., Nakayama, H., et al. (2006) · ChemBioChem · doi:10.1002/cbic.200600432 · Cited by 101
Attachment of Peptide Building Blocks to Proteins Through Tyrosine Bioconjugation
Romanini, D. W., & Francis, M. B. (2007) · Bioconjugate Chemistry · doi:10.1021/bc700231v · Cited by 99
Suzuki coupling for protein modification
Ojida, A., Tsutsumi, H., Kasagi, N., & Hamachi, I. (2005) · Tetrahedron Letters · doi:10.1016/j.tetlet.2005.03.094 · Cited by 96
Prasuhn, D. E., Blanco‐Canosa, J. B., Vora, G. J., Delehanty, J. B., Susumu, K., Mei, B. C., Dawson, P. E., & Medintz, I. L. (2010) · ACS Nano · doi:10.1021/nn901393v · Cited by 95
Self-citationProtein−Liposome Conjugates Using Cysteine-Lipids And Native Chemical Ligation
Reulen, S. W. A., Brusselaars, W. W. T., Langereis, S., Mulder, W. J. M., Breurken, M., & Merkx, M. (2007) · Bioconjugate Chemistry · doi:10.1021/bc0602782 · Cited by 89
Polito, L., Monti, D., Caneva, E., Delnevo, E., Russo, G., & Prosperi, D. (2008) · Chemical Communications · doi:10.1039/b716113a · Cited by 87
Surface-Immobilized Self-Assembled Protein-Based Quantum Dot Nanoassemblies
Sapsford, K. E., Medintz, I. L., Golden, J. P., Deschamps, J. R., Uyeda, H. T., & Mattoussi, H. M. (2004) · Langmuir · doi:10.1021/la049263n · Cited by 82
Self-citationSpecific and covalent labeling of a membrane protein with organic fluorochromes and quantum dots
Bonasio, R., Carman, C. V., Kim, E., Sage, P. T., Love, K. R., Mempel, T. R., Springer, T. A., & von Andrian, U. H. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705201104 · Cited by 81
Protein splicing and its applications
Perler, F. B., & Adam, E. (2000) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00113-0 · Cited by 79
Rapid Covalent Ligation of Fluorescent Peptides to Water Solubilized Quantum Dots
Blanco‐Canosa, J. B., Medintz, I. L., Farrell, D. F., Mattoussi, H. M., & Dawson, P. E. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910988d · Cited by 79
Self-citationKim, S. H., Jeyakumar, M., & Katzenellenbogen, J. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja074443f · Cited by 78
Chen, I., Choi, Y., & Ting, A. Y. (2007) · Journal of the American Chemical Society · doi:10.1021/ja071013g · Cited by 74
Lockett, M. R., Phillips, M. F., Jarecki, J. L., Peelen, D., & Smith, L. M. (2007) · Langmuir · doi:10.1021/la702493u · Cited by 73
Surface‐Modified Upconverting Microparticles and Nanoparticles for Use in Click Chemistries
Mader, H. S., Link, M., Achatz, D. E., Uhlmann, K., Li, X., & Wolfbeis, O. S. (2010) · Chemistry - A European Journal · doi:10.1002/chem.201000117 · Cited by 72
Carbon nanotubes in drug delivery: focus on infectious diseases
Rosen, Y., & Elman, N. M. (2009) · Expert Opinion on Drug Delivery · doi:10.1517/17425240902865579 · Cited by 71
HaloTag protein-mediated specific labeling of living cells with quantum dots
So, M., Yao, H., & Rao, J. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.07.004 · Cited by 71
Nanoscale Integration of Sensitizing Chromophores and Porphyrins with Bacteriophage MS2
Stephanopoulos, N., Carrico, Z. M., & Francis, M. B. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200902727 · Cited by 70
The modification of quantum dot probes used for the targeted imaging of his-tagged fusion proteins
Bae, P. K., Kim, K. N., Lee, S. J., Chang, H. J., Lee, C. K., & Park, J. K. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.10.049 · Cited by 65
Mechanistic and Kinetic Considerations of Protein Splicing
Evans, T. C., & Xu, M. (2002) · Chemical Reviews · doi:10.1021/cr9601369 · Cited by 63
Chemoselective Ligation in the Functionalization of Polysaccharide-Based Particles
Beaudette, T. T., Cohen, J. A., Bachelder, E. M., Broaders, K. E., Cohen, J. L., Engleman, E. G., & Fréchet, J. M. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja903984s · Cited by 62
Biosensing Using Nanomaterials
(2009) · Wiley eBooks · doi:10.1002/9780470447734 · Cited by 62
Franzen, S., & Lommel, S. A. (2009) · Nanomedicine · doi:10.2217/nnm.09.23 · Cited by 61
Genome-free Viral Capsids as Carriers for Positron Emission Tomography Radiolabels
Hooker, J. M., O’Neil, J. P., Romanini, D. W., Taylor, S. E., & Francis, M. B. (2008) · Molecular Imaging and Biology · doi:10.1007/s11307-008-0136-5 · Cited by 55
Stachler, M. D., Chen, I., Ting, A. Y., & Bartlett, J. S. (2008) · Molecular Therapy · doi:10.1038/mt.2008.129 · Cited by 53
Collagen Targeting Using Protein-Functionalized Micelles: The Strength of Multiple Weak Interactions
Reulen, S. W. A., Dankers, P. Y. W., Bomans, P. H. H., Meijer, E. W., & Merkx, M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja807723p · Cited by 46
Protein Design Provides Lead(II) Ion Biosensors for Imaging Molecular Fluxes around Red Blood Cells
Shete, V. S., & Benson, D. E. (2008) · Biochemistry · doi:10.1021/bi801777h · Cited by 45
Transfer of Stereochemical Information in a Minimal Self-Replicating System
Allen, V. C., Philp, D., & Spencer, N. (2001) · Organic Letters · doi:10.1021/ol015540v · Cited by 41
Enzyme catalyzed site-specific protein labeling and cell imaging with quantum dots
Sünbül, M., Yen, M., Zou, Y., & Yin, J. (2008) · Chemical Communications · doi:10.1039/b812162a · Cited by 37
Prasuhn, D. E., Kuzelka, J., Strable, E., Udit, A. K., Cho, S., Lander, G. C., Quispe, J. D., Diers, J. R., Bocian, D. F., Potter, C. S., et al. (2008) · Chemistry & Biology · doi:10.1016/j.chembiol.2008.03.018 · Cited by 26
Self-citationReulen, S. W. A., van Baal, I., Raats, J., & Merkx, M. (2009) · BMC Biotechnology · doi:10.1186/1472-6750-9-66 · Cited by 26
CrAsH−Quantum Dot Nanohybrids for Smart Targeting of Proteins
Génin, E., Carion, O., Mahler, B., Dubertret, B., Arhel, N. J., Charneau, P., Doris, E., & Mioskowski, C. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802987q · Cited by 25
Zou, Y., & Yin, J. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.08.085 · Cited by 24
Quantum Dots for the Development of Optical Biosensors Based on Fluorescence
Algar, W. R., & Krull, U. J. (2009) · doi:10.1002/9780470447734.ch7 · Cited by 10
Self-citationAlignment of Gold Clusters on DNA via a DNA-Recognizing Zinc Finger-Metallothionein Fusion Protein
Ariyasu, S., Onoda, A., Sakamoto, R. L., & Yamamura, T. (2009) · Bioconjugate Chemistry · doi:10.1021/bc9002713 · Cited by 9
Cited by
Localized surface plasmon resonance: Nanostructures, bioassays and biosensing—A review
Petryayeva, E., & Krull, U. J. (2011) · Analytica Chimica Acta · doi:10.1016/j.aca.2011.08.020 · Cited by 1,379
Nicolas, J., Mura, S., Brambilla, D., Mackiewicz, N., & Couvreur, P. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35265f · Cited by 1,270
Oximes and Hydrazones in Bioconjugation: Mechanism and Catalysis
Kölmel, D. K., & Kool, E. T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00090 · Cited by 699
Quantum dots in biomedical applications
Wagner, A. M., Knipe, J. M., Orive, G., & Peppas, N. A. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2019.05.022 · Cited by 632
Surface Functionalization of Exosomes Using Click Chemistry
Smyth, T., Petrova, K., Payton, N. M., Persaud, I., Redzic, J. S., Graner, M. W., Smith-Jones, P., & Anchordoquy, T. J. (2014) · Bioconjugate Chemistry · doi:10.1021/bc500291r · Cited by 532
Metadata
- Authors
- Algar, W. R., Prasuhn, D. E., Stewart, M. H., Jennings, T. L., Blanco-Canosa, J. B., Dawson, P. E., & Medintz, I. L.
- Venue
- Bioconjugate Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2011-05-18
- Volume
- 22
- Issue
- 5
- Pages
- 825-858
- ISSN
- 1043-1802 (ISSN-L)
- 1520-4812
- OpenAlex
- W2049753441
- Cited by
- 502
- References
- 292
- FWCI
- 27.83
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
