Chemical and Biophysical Signatures of the Protein Corona in Nanomedicine

Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles

Cedervall, T., Lynch, I., Lindman, S., Berggård, T., Thulin, E., Nilsson, H., Dawson, K. A., & Linse, S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608582104 · Cited by 3,281

Patisiran, an RNAi Therapeutic, for Hereditary Transthyretin Amyloidosis

Adams, D., Gonzalez-Duarte, A., O’Riordan, W. D., Yang, C.-C., Ueda, M., Kristen, A. V., Tournev, I., Schmidt, H. H., Coelho, T., Berk, J. L., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1716153 · Cited by 3,047

Nanoparticle size and surface properties determine the protein corona with possible implications for biological impacts

Lundqvist, M., Stigler, J., Elia, G., Lynch, I., Cedervall, T., & Dawson, K. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805135105 · Cited by 2,823

Rapid formation of plasma protein corona critically affects nanoparticle pathophysiology

Tenzer, S., Docter, D., Kuharev, J., Musyanovych, A., Fetz, V., Hecht, R., Schlenk, F., Fischer, D., Kiouptsi, K., Reinhardt, C., et al. (2013) · Nature Nanotechnology · doi:10.1038/nnano.2013.181 · Cited by 2,283

Nanoparticle Size and Surface Chemistry Determine Serum Protein Adsorption and Macrophage Uptake

Walkey, C. D., Olsen, J. B., Guo, H., Emili, A., & Chan, W. C. W. (2012) · Journal of the American Chemical Society · doi:10.1021/ja2084338 · Cited by 1,926

Transferrin-functionalized nanoparticles lose their targeting capabilities when a biomolecule corona adsorbs on the surface

Salvati, A., Pitek, A. S., Monopoli, M. P., Prapainop, K., Bombelli, F. B., Hristov, D. R., Kelly, P. M., Åberg, C., Mahon, E., & Dawson, K. A. (2013) · Nature Nanotechnology · doi:10.1038/nnano.2012.237 · Cited by 1,912

Systemic RNA delivery to dendritic cells exploits antiviral defence for cancer immunotherapy

Kranz, L. M., Diken, M., Haas, H., Kreiter, S., Loquai, C., Reuter, K. C., Meng, M., Fritz, D., Vascotto, F., Hefesha, H., et al. (2016) · Nature · doi:10.1038/nature18300 · Cited by 1,819

Understanding and controlling the interaction of nanomaterials with proteins in a physiological environment

Walkey, C. D., & Chan, W. C. W. (2012) · Chem. Soc. Rev. · doi:10.1039/c1cs15233e · Cited by 1,758

The entry of nanoparticles into solid tumours

Sindhwani, S., Syed, A. M., Ngai, J., Kingston, B. R., Maiorino, L., Rothschild, J., MacMillan, P., Zhang, Y., Rajesh, N. U., Hoang, T., et al. (2020) · Nature Materials · doi:10.1038/s41563-019-0566-2 · Cited by 1,732

Drug delivery systems for RNA therapeutics

Paunovska, K., Loughrey, D., & Dahlman, J. E. (2022) · Nature Reviews Genetics · doi:10.1038/s41576-021-00439-4 · Cited by 1,349

Protein adsorption is required for stealth effect of poly(ethylene glycol)- and poly(phosphoester)-coated nanocarriers

Schöttler, S., Becker, G., Winzen, S., Steinbach, T., Mohr, K., Landfester, K., Mailänder, V., & Wurm, F. R. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2015.330 · Cited by 1,272

Targeted delivery of RNAi therapeutics with endogenous and exogenous ligand-based mechanisms

Akinc, A., Querbes, W., De, S., Qin, J., Frank-Kamenetsky, M., Jayaprakash, K. N., Jayaraman, M., Rajeev, K. G., Cantley, W. L., Dorkin, J. R., et al. (2010) · Molecular Therapy · doi:10.1038/mt.2010.85 · Cited by 1,261

Protein-binding assays in biological liquids using microscale thermophoresis

Wienken, C. J., Baaske, P., Rothbauer, U., Braun, D., & Duhr, S. (2010) · Nature Communications · doi:10.1038/ncomms1093 · Cited by 1,138

On the mechanism of tissue-specific mRNA delivery by selective organ targeting nanoparticles

Dilliard, S. A., Cheng, Q., & Siegwart, D. J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109256118 · Cited by 1,018

The effect of the shape of mesoporous silica nanoparticles on cellular uptake and cell function

Huang, X., Teng, X., Chen, D., Tang, F., & He, J. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2009.09.060 · Cited by 1,002

Structure-based programming of lymph-node targeting in molecular vaccines

Liu, H., Moynihan, K. D., Zheng, Y., Szeto, G. L., Li, A. V., Huang, B., Van Egeren, D. S., Park, C., & Irvine, D. J. (2014) · Nature · doi:10.1038/nature12978 · Cited by 943

Binding of blood proteins to carbon nanotubes reduces cytotoxicity

Ge, C., Du, J., Zhao, L., Wang, L., Liu, Y., Li, D., Yang, Y., Zhou, R., Zhao, Y., Chai, Z., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105270108 · Cited by 940

The Shape Effect of Mesoporous Silica Nanoparticles on Biodistribution, Clearance, and Biocompatibility in Vivo

Huang, X., Li, L., Liu, T., Hao, N., Liu, H., Chen, D., & Tang, F. (2011) · ACS Nano · doi:10.1021/nn200365a · Cited by 921

Protein Corona-Mediated Mitigation of Cytotoxicity of Graphene Oxide

Hu, W., Peng, C., Lv, M., Li, X., Zhang, Y., Chen, N., Fan, C., & Huang, Q. (2011) · ACS Nano · doi:10.1021/nn200021j · Cited by 895

Detailed Identification of Plasma Proteins Adsorbed on Copolymer Nanoparticles

Cedervall, T., Lynch, I., Foy, M., Berggård, T., Donnelly, S. C., Cagney, G., Linse, S., & Dawson, K. A. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200700465 · Cited by 777

The Evolution of the Protein Corona around Nanoparticles: A Test Study

Lundqvist, M., Stigler, J., Cedervall, T., Berggård, T., Flanagan, M. B., Lynch, I., Elia, G., & Dawson, K. (2011) · ACS Nano · doi:10.1021/nn202458g · Cited by 752

Mechanistic understanding of in vivo protein corona formation on polymeric nanoparticles and impact on pharmacokinetics

Bertrand, N., Grenier, P., Mahmoudi, M., Lima, E. M., Appel, E. A., Dormont, F., Lim, J.-M., Karnik, R., Langer, R., & Farokhzad, O. C. (2017) · Nature Communications · doi:10.1038/s41467-017-00600-w · Cited by 708

A Decade of the Protein Corona

Ke, P. C., Lin, S., Parak, W. J., Davis, T. P., & Caruso, F. (2017) · ACS Nano · doi:10.1021/acsnano.7b08008 · Cited by 672

Therapeutic Protein–Polymer Conjugates: Advancing Beyond PEGylation

Pelegri-O’Day, E. M., Lin, E.-W., & Maynard, H. D. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504390x · Cited by 622

The Crown and the Scepter: Roles of the Protein Corona in Nanomedicine

Cai, R., & Chen, C. (2019) · Advanced Materials · doi:10.1002/adma.201805740 · Cited by 589

Effect of polyethyleneglycol (PEG) chain length on the bio–nano-interactions between PEGylated lipid nanoparticles and biological fluids: from nanostructure to uptake in cancer cells

Pozzi, D., Colapicchioni, V., Caracciolo, G., Piovesana, S., Capriotti, A. L., Palchetti, S., De Grossi, S., Riccioli, A., Amenitsch, H., & Laganà, A. (2014) · Nanoscale · doi:10.1039/c3nr05559k · Cited by 581

Palladium-mediated intracellular chemistry

Yusop, R. M., Unciti-Broceta, A., Johansson, E. M. V., Sánchez-Martín, R. M., & Bradley, M. (2011) · Nature Chemistry · doi:10.1038/nchem.981 · Cited by 531

Development and application of bond cleavage reactions in bioorthogonal chemistry

Li, J., & Chen, P. R. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2024 · Cited by 529

Recent advances in stealth coating of nanoparticle drug delivery systems

Amoozgar, Z., & Yeo, Y. (2012) · WIREs Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1157 · Cited by 528

Zwitterionic‐Coated “Stealth” Nanoparticles for Biomedical Applications: Recent Advances in Countering Biomolecular Corona Formation and Uptake by the Mononuclear Phagocyte System

García, K. P., Zarschler, K., Barbaro, L., Barreto, J. A., O'Malley, W., Spiccia, L., Stephan, H., & Graham, B. (2014) · Small · doi:10.1002/smll.201303540 · Cited by 519

Transcytosis and brain uptake of transferrin-containing nanoparticles by tuning avidity to transferrin receptor

Wiley, D. T., Webster, P., Gale, A., & Davis, M. E. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307152110 · Cited by 519

Palladium-triggered deprotection chemistry for protein activation in living cells

Li, J., Yu, J., Zhao, J., Wang, J., Zheng, S., Lin, S., Chen, L., Yang, M., Jia, S., Zhang, X., et al. (2014) · Nature Chemistry · doi:10.1038/nchem.1887 · Cited by 463

Titanium dioxide nanomaterials cause endothelial cell leakiness by disrupting the homophilic interaction of VE–cadherin

Setyawati, M. I., Tay, C. Y., Chia, S. L., Goh, S. L., Fang, W., Neo, M. J., Chong, H. C., Tan, S. M., Loo, S. C. J., Ng, K. W., et al. (2013) · Nature Communications · doi:10.1038/ncomms2655 · Cited by 458

Cloaking nanoparticles with protein corona shield for targeted drug delivery.

Oh, J. Y., Kim, H. S., Palanikumar, L., Go, E. M., Jana, B., Park, S. A., Kim, H. Y., Kim, K., Seo, J. K., Kwak, S. K., et al. (2018) · Nature communications · doi:10.1038/s41467-018-06979-4 · Cited by 409

Chemistry of Aqueous Silica Nanoparticle Surfaces and the Mechanism of Selective Peptide Adsorption

Patwardhan, S. V., Emami, F. S., Berry, R. J., Jones, S. E., Naik, R. R., Deschaume, O., Heinz, H., & Perry, C. C. (2012) · Journal of the American Chemical Society · doi:10.1021/ja211307u · Cited by 398

Systematic Investigation of the Thermodynamics of HSA Adsorption to N-iso-Propylacrylamide/N-tert-Butylacrylamide Copolymer Nanoparticles. Effects of Particle Size and Hydrophobicity

Lindman, S., Lynch, I., Thulin, E., Nilsson, H., Dawson, K. A., & Linse, S. (2007) · Nano Letters · doi:10.1021/nl062743+ · Cited by 377

In vivo formation of protein corona on gold nanoparticles. The effect of their size and shape

García-Álvarez, R., Hadjidemetriou, M., Sánchez-Iglesias, A., Liz-Marzán, L. M., & Kostarelos, K. (2018) · Nanoscale · doi:10.1039/c7nr08322j · Cited by 373

Polyethylene Glycol Backfilling Mitigates the Negative Impact of the Protein Corona on Nanoparticle Cell Targeting

Dai, Q., Walkey, C., & Chan, W. C. W. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201309464 · Cited by 371

Influence of particle size on the in vivo potency of lipid nanoparticle formulations of siRNA

Chen, S., Tam, Y. Y. C., Lin, P. J. C., Sung, M. M. H., Tam, Y. K., & Cullis, P. R. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.05.059 · Cited by 366

Nanoparticles with decreasing surface hydrophobicities: influence on plasma protein adsorption

Gessner, A., Waicz, R., Lieske, A., Paulke, B.-R., Mäder, K., & Müller, R. H. (2000) · International Journal of Pharmaceutics · doi:10.1016/s0378-5173(99)00432-9 · Cited by 358

Blood-brain barrier transcytosis of insulin in developing rabbits

Duffy, K. R., & Pardridge, W. M. (1987) · Brain Research · doi:10.1016/0006-8993(87)90236-8 · Cited by 358

Influence of surface charge density on protein adsorption on polymeric nanoparticles: analysis by two-dimensional electrophoresis

Gessner, A., Lieske, A., Paulke, B. R., & Müller, R. H. (2002) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/s0939-6411(02)00081-4 · Cited by 356

Regulation of Macrophage Recognition through the Interplay of Nanoparticle Surface Functionality and Protein Corona

Saha, K., Rahimi, M., Yazdani, M., Kim, S. T., Moyano, D. F., Hou, S., Das, R., Mout, R., Rezaee, F., Mahmoudi, M., et al. (2016) · ACS Nano · doi:10.1021/acsnano.6b00053 · Cited by 355

Surface-enhanced Raman scattering for protein detection

Han, X. X., Zhao, B., & Ozaki, Y. (2009) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-009-2702-3 · Cited by 349

Synergistic lipid compositions for albumin receptor mediated delivery of mRNA to the liver

Miao, L., Lin, J., Huang, Y., Li, L., Delcassian, D., Ge, Y., Shi, Y., & Anderson, D. G. (2020) · Nature Communications · doi:10.1038/s41467-020-16248-y · Cited by 343

Brain-targeted drug delivery by manipulating protein corona functions

Zhang, Z., Guan, J., Jiang, Z., Yang, Y., Liu, J., Hua, W., Mao, Y., Li, C., Lu, W., Qian, J., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11593-z · Cited by 334

Impact of protein pre-coating on the protein corona composition and nanoparticle cellular uptake

Mirshafiee, V., Kim, R., Park, S., Mahmoudi, M., & Kraft, M. L. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2015.10.019 · Cited by 316

Nanoparticles' interactions with vasculature in diseases

Tee, J. K., Yip, L. X., Tan, E. S., Santitewagun, S., Prasath, A., Ke, P. C., Ho, H. K., & Leong, D. T. (2019) · Chemical Society Reviews · doi:10.1039/c9cs00309f · Cited by 314

The Nano–Bio Interactions of Nanomedicines: Understanding the Biochemical Driving Forces and Redox Reactions

Wang, Y., Cai, R., & Chen, C. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.9b00126 · Cited by 303

Effect of gold nanoparticle morphology on adsorbed protein structure and function

Gagner, J. E., Lopez, M. D., Dordick, J. S., & Siegel, R. W. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.05.091 · Cited by 297

Transcytosis at the blood–brain barrier

Ayloo, S., & Gu, C. (2019) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.12.014 · Cited by 296

Controlling the Stealth Effect of Nanocarriers through Understanding the Protein Corona

Schöttler, S., Landfester, K., & Mailänder, V. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201602233 · Cited by 291

Use of Synchrotron Radiation-Analytical Techniques To Reveal Chemical Origin of Silver-Nanoparticle Cytotoxicity

Wang, L., Zhang, T., Li, P., Huang, W., Tang, J., Wang, P., Liu, J., Yuan, Q., Bai, R., Li, B., et al. (2015) · ACS Nano · doi:10.1021/acsnano.5b02483 · Cited by 290

Pre-adsorption of antibodies enables targeting of nanocarriers despite a biomolecular corona

Tonigold, M., Simon, J., Estupiñán, D., Kokkinopoulou, M., Reinholz, J., Kintzel, U., Kaltbeitzel, A., Renz, P., Domogalla, M. P., Steinbrink, K., et al. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0171-6 · Cited by 289

Revealing the Binding Structure of the Protein Corona on Gold Nanorods Using Synchrotron Radiation-Based Techniques: Understanding the Reduced Damage in Cell Membranes

Wang, L., Li, J., Pan, J., Jiang, X., Ji, Y., Li, Y., Qu, Y., Zhao, Y., Wu, X., & Chen, C. (2013) · Journal of the American Chemical Society · doi:10.1021/ja406924v · Cited by 287

Interactions between Metal Oxides and Biomolecules: from Fundamental Understanding to Applications

Limo, M. J., Sola-Rabada, A., Boix, E., Thota, V., Westcott, Z. C., Puddu, V., & Perry, C. C. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00660 · Cited by 287

Gold Nanoparticles Induced Endothelial Leakiness Depends on Particle Size and Endothelial Cell Origin

Setyawati, M. I., Tay, C. Y., Bay, B. H., & Leong, D. T. (2017) · ACS Nano · doi:10.1021/acsnano.7b01744 · Cited by 282

Molybdenum derived from nanomaterials incorporates into molybdenum enzymes and affects their activities in vivo

Cao, M., Cai, R., Zhao, L., Guo, M., Wang, L., Wang, Y., Zhang, L., Wang, X., Yao, H., Xie, C., et al. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-00856-w · Cited by 271

GolP-CHARMM: First-Principles Based Force Fields for the Interaction of Proteins with Au(111) and Au(100)

Wright, L. B., Rodger, P. M., Corni, S., & Walsh, T. R. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct301018m · Cited by 269

Detecting Cryptic Epitopes Created by Nanoparticles

Lynch, I., Dawson, K. A., & Linse, S. (2006) · Science's STKE · doi:10.1126/stke.3272006pe14 · Cited by 268

Carbon‐Based Nanomaterials for Cancer Therapy via Targeting Tumor Microenvironment

Saleem, J., Wang, L., & Chen, C. (2018) · Advanced Healthcare Materials · doi:10.1002/adhm.201800525 · Cited by 262

Tailoring the component of protein corona via simple chemistry

Lu, X., Xu, P., Ding, H.-M., Yu, Y.-S., Huo, D., & Ma, Y.-Q. (2019) · Nature Communications · doi:10.1038/s41467-019-12470-5 · Cited by 246

The ancillary effects of nanoparticles and their implications for nanomedicine

Stater, E. P., Sonay, A. Y., Hart, C., & Grimm, J. (2021) · Nature Nanotechnology · doi:10.1038/s41565-021-01017-9 · Cited by 245

Identification of Receptor Binding to the Biomolecular Corona of Nanoparticles

Lara, S., Alnasser, F., Polo, E., Garry, D., Lo Giudice, M. C., Hristov, D. R., Rocks, L., Salvati, A., Yan, Y., & Dawson, K. A. (2017) · ACS Nano · doi:10.1021/acsnano.6b07933 · Cited by 243

On the issue of transparency and reproducibility in nanomedicine

Leong, H. S., Butler, K. S., Brinker, C. J., Azzawi, M., Conlan, S., Dufés, C., Owen, A., Rannard, S., Scott, C., Chen, C., et al. (2019) · Nature Nanotechnology · doi:10.1038/s41565-019-0496-9 · Cited by 242

Functional groups on polystyrene model nanoparticles: Influence on protein adsorption

Gessner, A., Lieske, A., Paulke, B., & Müller, R. H. (2003) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.10371 · Cited by 239

Peptide Adsorption on Silica Nanoparticles: Evidence of Hydrophobic Interactions

Puddu, V., & Perry, C. C. (2012) · ACS Nano · doi:10.1021/nn301866q · Cited by 226

Mapping and identification of soft corona proteins at nanoparticles and their impact on cellular association

Mohammad-Beigi, H., Hayashi, Y., Zeuthen, C. M., Eskandari, H., Scavenius, C., Juul-Madsen, K., Vorup-Jensen, T., Enghild, J. J., & Sutherland, D. S. (2020) · Nature Communications · doi:10.1038/s41467-020-18237-7 · Cited by 218

Biomimetic Magnetosomes as Versatile Artificial Antigen-Presenting Cells to Potentiate T-Cell-Based Anticancer Therapy

Zhang, Q., Wei, W., Wang, P., Zuo, L., Li, F., Xu, J., Xi, X., Gao, X., Ma, G., & Xie, H.-Y. (2017) · ACS Nano · doi:10.1021/acsnano.7b04955 · Cited by 210

Evolution of Nanoparticle Protein Corona across the Blood–Brain Barrier

Cox, A., Andreozzi, P., Dal Magro, R., Fiordaliso, F., Corbelli, A., Talamini, L., Chinello, C., Raimondo, F., Magni, F., Tringali, M., et al. (2018) · ACS Nano · doi:10.1021/acsnano.8b03500 · Cited by 208

The Influence of Nanoparticle Shape on Protein Corona Formation

Madathiparambil Visalakshan, R., González García, L. E., Benzigar, M. R., Ghazaryan, A., Simon, J., Mierczynska‐Vasilev, A., Michl, T. D., Vinu, A., Mailänder, V., Morsbach, S., et al. (2020) · Small · doi:10.1002/smll.202000285 · Cited by 201

Albumin corona on nanoparticles – a strategic approach in drug delivery

Mariam, J., Sivakami, S., & Dongre, P. M. (2016) · Drug Delivery · doi:10.3109/10717544.2015.1048488 · Cited by 196

Zwitterionic polymer ligands: an ideal surface coating to totally suppress protein-nanoparticle corona formation?

Debayle, M., Balloul, E., Dembele, F., Xu, X., Hanafi, M., Ribot, F., Monzel, C., Coppey, M., Fragola, A., Dahan, M., et al. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119357 · Cited by 196

Hyaluronic Acid Coated Chitosan Nanoparticles Reduced the Immunogenicity of the Formed Protein Corona

Almalik, A., Benabdelkamel, H., Masood, A., Alanazi, I. O., Alradwan, I., Majrashi, M. A., Alfadda, A. A., Alghamdi, W. M., Alrabiah, H., Tirelli, N., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10836-7 · Cited by 195

Long-term pulmonary exposure to multi-walled carbon nanotubes promotes breast cancer metastatic cascades

Lu, X., Zhu, Y., Bai, R., Wu, Z., Qian, W., Yang, L., Cai, R., Yan, H., Li, T., Pandey, V., et al. (2019) · Nature Nanotechnology · doi:10.1038/s41565-019-0472-4 · Cited by 192

Walking the line: The fate of nanomaterials at biological barriers

Meng, H., Leong, W., Leong, K. W., Chen, C., & Zhao, Y. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.04.056 · Cited by 186

The protein corona hampers the transcytosis of transferrin-modified nanoparticles through blood-brain barrier and attenuates their targeting ability to brain tumor.

Xiao, W., Wang, Y., Zhang, H., Liu, Y., Xie, R., He, X., Zhou, Y., Liang, L., & Gao, H. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.120888 · Cited by 174

Dynamic protein coronas revealed as a modulator of silver nanoparticle sulphidation in vitro

Miclăuş, T., Beer, C., Chevallier, J., Scavenius, C., Bochenkov, V. E., Enghild, J. J., & Sutherland, D. S. (2016) · Nature Communications · doi:10.1038/ncomms11770 · Cited by 174

Zwitterion-Stabilized Silica Nanoparticles: Toward Nonstick Nano

Estephan, Z. G., Jaber, J. A., & Schlenoff, J. B. (2010) · Langmuir · doi:10.1021/la103095d · Cited by 172

Significance of surface charge and shell material of superparamagnetic iron oxide nanoparticle (SPION) based core/shell nanoparticles on the composition of the protein corona

Sakulkhu, U., Mahmoudi, M., Maurizi, L., Coullerez, G., Hofmann-Amtenbrink, M., Vries, M., Motazacker, M., Rezaee, F., & Hofmann, H. (2015) · Biomaterials Science · doi:10.1039/c4bm00264d · Cited by 163

Chiral Surface of Nanoparticles Determines the Orientation of Adsorbed Transferrin and Its Interaction with Receptors

Wang, X., Wang, M., Lei, R., Zhu, S. F., Zhao, Y., & Chen, C. (2017) · ACS Nano · doi:10.1021/acsnano.7b00200 · Cited by 162

Understanding Nanomaterial–Liver Interactions to Facilitate the Development of Safer Nanoapplications

Li, J., Chen, C., & Xia, T. (2022) · Advanced Materials · doi:10.1002/adma.202106456 · Cited by 162

Biodistribution of gold nanoparticles in mouse lung following intratracheal instillation

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Corona of Thorns: The Surface Chemistry-Mediated Protein Corona Perturbs the Recognition and Immune Response of Macrophages

Cai, R., Ren, J., Ji, Y., Wang, Y., Liu, Y., Chen, Z., Sabet, Z. F., Wu, X., Lynch, I., & Chen, C. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b15910 · Cited by 160

Quantitative Protein Corona Composition and Dynamics on Carbon Nanotubes in Biological Environments

Pinals, R. L., Yang, D., Rosenberg, D. J., Chaudhary, T., Crothers, A. R., Iavarone, A. T., Hammel, M., & Landry, M. P. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202008175 · Cited by 160

Protein Nanoparticle Charge and Hydrophobicity Govern Protein Corona and Macrophage Uptake

Pustulka, S. M., Ling, K., Pish, S. L., & Champion, J. A. (2020) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.0c12341 · Cited by 160

Caveolae-Mediated Endocytosis Is Critical for Albumin Cellular Uptake and Response to Albumin-Bound Chemotherapy

Chatterjee, M., Ben‐Josef, E., Robb, R. N., Vedaie, M., Seum, S., Thirumoorthy, K., Palanichamy, K., Harbrecht, M. T., Chakravarti, A., & Williams, T. M. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-0604 · Cited by 159

Techniques for the experimental investigation of the protein corona

Carrillo-Carrion, C., Carril, M., & Parak, W. J. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.02.009 · Cited by 158

Effect of Surface Chemistry and Associated Protein Corona on the Long-Term Biodegradation of Iron Oxide Nanoparticles In Vivo

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An Analysis of the Binding Function and Structural Organization of the Protein Corona

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Resolving Single-Nanoconstruct Dynamics during Targeting and Nontargeting Live-Cell Membrane Interactions

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The Protein Corona Conundrum: Exploring the Advantages and Drawbacks of its Presence around Amphiphilic Nanoparticles

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Protein Corona Gold Nanoparticles Fingerprinting Reveals a Profile of Blood Coagulation Proteins in the Serum of HER2-Overexpressing Breast Cancer Patients

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Protein-Cloaked Nanoparticles for Enhanced Cellular Association and Controlled Pathophysiology via Immunosurveillance Escape

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