Nanoparticle protein corona: from structure and function to therapeutic targeting
Open accessAbstract
. Since the function of a protein is closely connected to its folded structure, slight differences in the surrounding environment as well as the surface characteristics of the NP materials may cause proteins to lose or gain a function. As a result, this can alter the downstream functionality of the NPs. This review introduces the main biological factors affecting the conformation of proteins associated with the PC. Then, four types of NPs with extensive utility in biomedical applications are described in greater detail, focusing on the conformation and orientation of adsorbed proteins. This is followed by a discussion on the instances in which the conformation of adsorbed proteins can be leveraged for therapeutic purposes, such as controlling protein conformation in assembled matrices in tissue, as well as controlling the PC conformation for modulating immune responses. The review concludes with a perspective on the remaining challenges and unexplored areas at the interface of PC and NP research.
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Upon systemic injection, nanoparticles often adsorb serum proteins to form a protein corona that alters pharmacokinetics, targeting specificity, and immunogenicity.
“Upon systemic injection, NPs often adsorb serum proteins to form a “protein corona” that alters pharmacokinetics, targeting specificity, and immunogenicity [183, 184].”
From Targeted Nanoparticles for Drug Delivery Across the Blood–Brain Barrier in Early and Late Stages of Alzheimer's Disease: A Review (2026) · cites this paper as [184]
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Self-Assembled Monolayers of Thiolates on Metals as a Form of Nanotechnology
Love, J. C., Estroff, L. A., Kriebel, J. K., Nuzzo, R. G., & Whitesides, G. M. (2005) · Chemical Reviews · doi:10.1021/cr0300789 · Cited by 8,279 · see citing works
Re-epithelialization and immune cell behaviour in an ex vivo human skin model
Rakita, A., Nikolić, N., Mildner, M., Matiasek, J., & Elbe‐Bürger, A. (2020) · Scientific Reports · doi:10.1038/s41598-019-56847-4 · Cited by 8,228 · see citing works
U1 snRNP regulates cancer cell migration and invasion in vitro
Oh, J.-M., Venters, C. C., Di, C., Pinto, A. M., Wan, L., Younis, I., Cai, Z., Arai, C., So, B. R., Duan, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13993-7 · Cited by 7,157 · see citing works
Understanding biophysicochemical interactions at the nano–bio interface
Nel, A. E., Mädler, L., Velegol, D., Xia, T., Hoek, E. M. V., Somasundaran, P., Klaessig, F., Castranova, V., & Thompson, M. (2009) · Nature Materials · doi:10.1038/nmat2442 · Cited by 7,083 · see citing works
Principles of nanoparticle design for overcoming biological barriers to drug delivery
Blanco, E., Shen, H., & Ferrari, M. (2015) · Nature Biotechnology · doi:10.1038/nbt.3330 · Cited by 7,002 · see citing works
Doxil® — The first FDA-approved nano-drug: Lessons learned
Barenholz, Y. (. (2012) · Journal of Controlled Release · doi:10.1016/j.jconrel.2012.03.020 · Cited by 4,792 · see citing works
The extracellular matrix at a glance
Frantz, C., Stewart, K. M., & Weaver, V. M. (2010) · Journal of Cell Science · doi:10.1242/jcs.023820 · Cited by 4,334 · see citing works
The golden age: gold nanoparticles for biomedicine
Dreaden, E. C., Alkilany, A. M., Huang, X., Murphy, C. J., & El‐Sayed, M. A. (2011) · Chemical Society Reviews · doi:10.1039/c1cs15237h · Cited by 3,572 · see citing works
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 3,037 · see citing works
Extracellular matrix structure
Theocharis, A. D., Skandalis, S. S., Gialeli, C., & Karamanos, N. K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.001 · Cited by 2,598 · see citing works
Gref, R., Lück, M., Quellec, P., Marchand, M., Dellacherie, E., Harnisch, S., Blunk, T., & Müller, R. H. (2000) · Colloids and Surfaces B Biointerfaces · doi:10.1016/s0927-7765(99)00156-3 · Cited by 1,725 · see citing works
Understanding protein adsorption phenomena at solid surfaces
Rabe, M., Verdes, D., & Seeger, S. (2011) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2010.12.007 · Cited by 1,672 · see citing works
Inflammation and wound healing: the role of the macrophage
Koh, T. J., & DiPietro, L. A. (2011) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411001943 · Cited by 1,667 · see citing works
Synthesis, characterization, applications, and challenges of iron oxide nanoparticles
Ali, A., Zafar, H., Zia, M., ul Haq, I., Phull, A. R., Ali, J. S., & Hussain, A. (2016) · Nanotechnology, Science and Applications · doi:10.2147/nsa.s99986 · Cited by 1,591 · see citing works
Acidity Generated by the Tumor Microenvironment Drives Local Invasion
Estrella, V. C., Chen, T., Lloyd, M. C., Wojtkowiak, J. W., Cornnell, H. H., Ibrahim‐Hashim, A., Bailey, K. M., Balagurunathan, Y., Rothberg, J. M., Sloane, B. F., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-2796 · Cited by 1,404 · see citing works
Gold Nanomaterials at Work in Biomedicine
Yang, X., Yang, M., Pang, B., Vara, M., & Younan Xia, A. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00193 · Cited by 1,169 · see citing works
Keselowsky, B. G., Collard, D. M., & García, A. J. (2003) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.10537 · Cited by 949 · see citing works
Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation
Deng, Z. J., Liang, M., Monteiro, M. J., Tóth, I., & Minchin, R. F. (2010) · Nature Nanotechnology · doi:10.1038/nnano.2010.250 · Cited by 893 · see citing works
Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer’s diseases
Huang, Y., & Mahley, R. W. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.025 · Cited by 829 · see citing works
Functional structure and composition of the extracellular matrix
Bosman, F. T., & Stamenkovic, I. (2003) · The Journal of Pathology · doi:10.1002/path.1437 · Cited by 823 · see citing works
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. A. (2011) · ACS Nano · doi:10.1021/nn202458g · Cited by 800 · see citing works
Mechanisms of Ligand Recognition in Myoglobin
Springer, B. A., Sligar, S. G., Olson, J. S., & Phillips, G. N. J. (1994) · Chemical Reviews · doi:10.1021/cr00027a007 · Cited by 755 · see citing works
Protein corona: a new approach for nanomedicine design
Nguyen, V. H., & Lee, B. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s129300 · Cited by 640 · see citing works
The Crown and the Scepter: Roles of the Protein Corona in Nanomedicine
Cai, R., & Chen, C. (2018) · Advanced Materials · doi:10.1002/adma.201805740 · Cited by 599 · see citing works
Complement proteins bind to nanoparticle protein corona and undergo dynamic exchange in vivo
Chen, F., Wang, G., Griffin, J. I., Brenneman, B., Banda, N. K., Holers, V. M., Backos, D. S., Wu, L., Moghimi, S. M., & Simberg, D. (2017) · Nature Nanotechnology · doi:10.1038/nnano.2016.269 · Cited by 599 · see citing works
Shang, L., Wang, Y., Jiang, J., & Dong, S. (2007) · Langmuir · doi:10.1021/la062064e · Cited by 557 · see citing works
Dawidczyk, C. M., Kim, C., Park, J. H., Russell, L. M., Lee, K. H., Pomper, M. G., & Searson, P. C. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.05.036 · Cited by 526 · see citing works
Murayama, K., & Tomida, M. (2004) · Biochemistry · doi:10.1021/bi0489154 · Cited by 482 · see citing works
Integrin Dynamics and Matrix Assembly
Pankov, R., Cukierman, E., Katz, B.-Z., Matsumoto, K., Lin, D. C., Lin, S., Hahn, C., & Yamada, K. M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.5.1075 · Cited by 482 · see citing works
Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic
Ferraboschi, P., Ciceri, S., & Grisenti, P. (2021) · Antibiotics · doi:10.3390/antibiotics10121534 · Cited by 455 · see citing works
Force-Induced Unfolding of Fibronectin in the Extracellular Matrix of Living Cells
Smith, M. L., Gourdon, D., Little, W. C., Kubow, K. E., Eguiluz, R. C. A., Luna, S., & Viola Vogel, B. (2007) · PLoS Biology · doi:10.1371/journal.pbio.0050268 · Cited by 441 · see citing works
Molecular Interaction of Proteins and Peptides with Nanoparticles
Shemetov, A. A., Nabiev, I. R., & Sukhanova, A. V. (2012) · ACS Nano · doi:10.1021/nn300415x · Cited by 432 · see citing works
Why Drugs Fail - A Study on Side Effects in New Chemical Entities
Schuster, D., Laggner, C., & Langer, T. (2005) · Current Pharmaceutical Design · doi:10.2174/138161205774414510 · Cited by 417 · see citing works
High Wall Shear Stress and Spatial Gradients in Vascular Pathology: A Review
Dolan, J. M., Kolega, J. J., & Meng, H. (2012) · Annals of Biomedical Engineering · doi:10.1007/s10439-012-0695-0 · Cited by 416 · see citing works
Choi, Y. H., & Han, H. (2017) · Journal of Pharmaceutical Investigation · doi:10.1007/s40005-017-0370-4 · Cited by 408 · see citing works
Gold Nanoparticles Can Induce the Formation of Protein-based Aggregates at Physiological pH
Zhang, D., Neumann, O., Wang, H., Yuwono, V. M., Barhoumi, A., Perham, M., Hartgerink, J. D., Wittung-Stafshede, P. E., & Halas, N. J. (2009) · Nano Letters · doi:10.1021/nl803054h · Cited by 391 · see citing works
Piella, J., Bastús, N. G., & Puntes, V. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00575 · Cited by 383 · see citing works
Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
Baneyx, G., Baugh, L., & Viola Vogel, B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072650799 · Cited by 376 · see citing works
Drugs, Devices, and the FDA: Part 1
Van Norman, G. A. (2016) · JACC: Basic to Translational Science · doi:10.1016/j.jacbts.2016.03.002 · Cited by 366 · see citing works
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 · see citing works
Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix
Kubow, K. E., Vukmirovic, R., Zhe, L., Klotzsch, E., Smith, M. L., Gourdon, D., Luna, S., & Viola Vogel, B. (2015) · Nature Communications · doi:10.1038/ncomms9026 · Cited by 342 · see citing works
Velling, T., Risteli, J., Wennerberg, K., Mosher, D., & Johansson, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206286200 · Cited by 339 · see citing works
Temperature: The “Ignored” Factor at the NanoBio Interface
Mahmoudi, M., Abdelmonem, A. M., Behzadi, S., Clement, J. H., Dutz, S., Ejtehadi, M. R., Hartmann, R., Kantner, K., Linne, U., Maffre, P., et al. (2013) · ACS Nano · doi:10.1021/nn305337c · Cited by 334 · see citing works
Rezwan, K., Meier, L. P., Rezwan, M., Vörös, J., Textor, M., & Gauckler, L. J. (2004) · Langmuir · doi:10.1021/la048459k · Cited by 314 · see citing works
Vu, V. P., Gifford, G. B., Chen, F., Benasutti, H., Wang, G., Groman, E. V., Scheinman, R. I., Saba, L. M., Moghimi, S. M., & Simberg, D. (2018) · Nature Nanotechnology · doi:10.1038/s41565-018-0344-3 · Cited by 310 · see citing works
Personalized protein coronas: a “key” factor at the nanobiointerface
Hajipour, M. J., Laurent, S., Aghaie, A., Rezaee, F., & Mahmoudi, M. (2014) · Biomaterials Science · doi:10.1039/c4bm00131a · Cited by 309 · see citing works
Corona Composition Can Affect the Mechanisms Cells Use to Internalize Nanoparticles
Francia, V., Yang, K., Deville, S., Reker‐Smit, C., Nelissen, I., & Salvati, A. L. (2019) · ACS Nano · doi:10.1021/acsnano.9b03824 · Cited by 306 · see citing works
Fibronectin in development and wound healing
Patten, J., & Wang, K. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.09.005 · Cited by 303 · see citing works
Self-citationEstimation of the increase in solubility of drugs as a function of bile salt concentration
Mithani, S. D., Bakatselou, V., TenHoor, C. N., & Dressman, J. B. (1996) · Pharmaceutical Research · doi:10.1023/a:1016062224568 · Cited by 303 · see citing works
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 298 · see citing works
Structure–Function Properties of Food Proteins
(1994) · Elsevier eBooks · doi:10.1016/c2009-0-02425-8 · Cited by 298 · see citing works
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 292 · see citing works
Understanding the Kinetics of Protein–Nanoparticle Corona Formation
Vilanova, O., Mittag, J. J., Kelly, P. M., Milani, S., Dawson, K. A., Rädler, J. O., & Franzese, G. (2016) · ACS Nano · doi:10.1021/acsnano.6b04858 · Cited by 292 · see citing works
A Comprehensive Map of FDA-Approved Pharmaceutical Products
Zhong, H., Chan, G., Yuanjia, H., Hu, H., & Ouyang, D. (2018) · Pharmaceutics · doi:10.3390/pharmaceutics10040263 · Cited by 288 · see citing works
Role of nanotechnology behind the success of mRNA vaccines for COVID-19
Khurana, A., Allawadhi, P., Khurana, I., Allwadhi, S., Weiskirchen, R., Banothu, A. K., Chhabra, D., Joshi, K., & Bharani, K. K. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101142 · Cited by 286 · see citing works
Current Insights into Collagen Type I
Naomi, R., Ridzuan, P. M., & Bahari, H. (2021) · Polymers · doi:10.3390/polym13162642 · Cited by 256 · see citing works
Kruse, C., Singh, M., Targosinski, S., Sinha, I., Sørensen, J. A., Eriksson, E. K., & Nuutila, K. (2017) · Wound Repair and Regeneration · doi:10.1111/wrr.12526 · Cited by 252 · see citing works
Understanding the Lipid and Protein Corona Formation on Different Sized Polymeric Nanoparticles
Lima, T., Bernfur, K., Vilanova, M., & Cedervall, T. (2020) · Scientific Reports · doi:10.1038/s41598-020-57943-6 · Cited by 251 · see citing works
Adsorption and Unfolding of a Single Protein Triggers Nanoparticle Aggregation
Domínguez-Medina, S., Kisley, L., Tauzin, L. J., Hoggard, A., Shuang, B., Indrasekara, A. S. D. S., Chen, S., Wang, L.-Y., Derry, P. J., Liopo, A. V., et al. (2016) · ACS Nano · doi:10.1021/acsnano.5b06439 · Cited by 236 · see citing works
The protein corona of circulating PEGylated liposomes
Palchetti, S., Colapicchioni, V., Digiacomo, L., Caracciolo, G., Pozzi, D., Capriotti, A. L., Barbera, G. L., & Laganà, A. (2015) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.11.012 · Cited by 234 · see citing works
The “Sweet” Side of the Protein Corona: Effects of Glycosylation on Nanoparticle–Cell Interactions
Wan, S., Kelly, P. M., Mahon, E., Stöckmann, H., Rudd, P. M., Caruso, F., Dawson, K. A., Yan, Y., & Monopoli, M. P. (2015) · ACS Nano · doi:10.1021/nn506060q · Cited by 223 · see citing works
Estey, T., Kang, J., Schwendeman, S. P., & Carpenter, J. F. (2006) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20625 · Cited by 221 · see citing works
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 221 · see citing works
Conformational states of fibronectin. Effects of pH, ionic strength, and collagen binding.
Williams, E. C., Janmey, P. A., Ferry, J. D., & Mosher, D. F. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33379-9 · Cited by 215 · see citing works
Sacks, L. V., Shamsuddin, H. H., Yasinskaya, Y., Bouri, K., Lanthier, M. L., & Sherman, R. E. (2014) · JAMA · doi:10.1001/jama.2013.282542 · Cited by 214 · see citing works
The effects of shear flow on protein structure and function
Bekard, I. B., Asimakis, P., Bertolini, J., & Dunstan, D. E. (2011) · Biopolymers · doi:10.1002/bip.21646 · Cited by 209 · see citing works
Nanoengineered silica: Properties, applications and toxicity
Mebert, A. M., Baglole, C. J., Desimone, M. F., & Maysinger, D. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.05.054 · Cited by 209 · see citing works
Mahmoudi, M., Shokrgozar, M. A., Sardari, S., Moghadam, M. K., Vali, H., Laurent, S., & Stroeve, P. (2011) · Nanoscale · doi:10.1039/c0nr00733a · Cited by 204 · see citing works
Ag Nanoparticles Cluster with pH‐Triggered Reassembly in Targeting Antimicrobial Applications
Xie, X., Sun, T., Xue, J., Miao, Z., Yan, X., Fang, W., Li, Q., Tang, R., Lü, Y., Tang, L., et al. (2020) · Advanced Functional Materials · doi:10.1002/adfm.202000511 · Cited by 197 · see citing works
Engineering the drug carrier biointerface to overcome biological barriers to drug delivery
Finbloom, J. A., Sousa, F., Stevens, M. M., & Desai, T. A. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.06.007 · Cited by 192 · see citing works
pH Impacts the Orientation of Antibody Adsorbed onto Gold Nanoparticles
Ruiz, G. N., Tripathi, K., Okyem, S., & Driskell, J. D. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00123 · Cited by 192 · see citing works
Baneyx, G., Baugh, L., & Viola Vogel, B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.251422998 · Cited by 188 · see citing works
Lü, R., Li, W., Katzir, A., Raichlin, Y., Yu, H., & Mizaikoff, B. (2014) · The Analyst · doi:10.1039/c4an01495b · Cited by 187 · see citing works
GABE, I. T., Gault, J. H., Ross, J., Mason, D. T., MILLS, C. J., Shillingford, J. P., & D, E. B. M. (1969) · Circulation · doi:10.1161/01.cir.40.5.603 · Cited by 186 · see citing works
Characterization of protein adsorption onto silica nanoparticles: influence of pH and ionic strength
Meissner, J., Prause, A., Bharti, B., & Findenegg, G. H. (2015) · Colloid & Polymer Science · doi:10.1007/s00396-015-3754-x · Cited by 184 · see citing works
Lee, M. H., Ducheyne, P., Lynch, L., Boettiger, D., & Composto, R. J. (2006) · Biomaterials · doi:10.1016/j.biomaterials.2005.11.003 · Cited by 183 · see citing works
Underwood, P. A., Steele, J. G., & Dalton, B. A. (1993) · Journal of Cell Science · doi:10.1242/jcs.104.3.793 · Cited by 176 · see citing works
Satzer, P., Švec, F., Sekot, G., & Jungbauer, A. (2015) · Engineering in Life Sciences · doi:10.1002/elsc.201500059 · Cited by 175 · see citing works
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 175 · see citing works
Dolan, J. M., Meng, H., Singh, S., Paluch, R. A., & Kolega, J. J. (2011) · Annals of Biomedical Engineering · doi:10.1007/s10439-011-0267-8 · Cited by 173 · see citing works
The Human In Vivo Biomolecule Corona onto PEGylated Liposomes: A Proof‐of‐Concept Clinical Study
Hadjidemetriou, M., McAdam, S., Garner, G., Thackeray, C., Knight, D., Smith, D. L., Al-Ahmady, Z. S., Mazza, M., Rogan, J., Clamp, A. R., et al. (2018) · Advanced Materials · doi:10.1002/adma.201803335 · Cited by 173 · see citing works
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 164 · see citing works
The biomolecular corona of nanoparticles in circulating biological media
Pozzi, D., Caracciolo, G., Digiacomo, L., Colapicchioni, V., Palchetti, S., Capriotti, A. L., Cavaliere, C., Chiozzi, R. Z., Puglisi, A., & Laganà, A. (2015) · Nanoscale · doi:10.1039/c5nr03701h · Cited by 163 · see citing works
Quantum dots and other nanoparticles: what can they offer to drug discovery?
Ozkan, M. (2004) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03291-x · Cited by 159 · see citing works
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 153 · see citing works
An Analysis of the Binding Function and Structural Organization of the Protein Corona
Zhang, Y., Wu, J. L. Y., Lazarovits, J., & Chan, W. C. W. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c01853 · Cited by 151 · see citing works
Givens, B. E., Xu, Z., Fiegel, J., & Grassian, V. H. (2017) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2017.01.011 · Cited by 149 · see citing works
Ma, Z., Bai, J., Wang, Y., & Jiang, X. (2014) · ACS Applied Materials & Interfaces · doi:10.1021/am404860q · Cited by 149 · see citing works
Kollmannsberger, P., Bidan, C. M., Dunlop, J., Fratzl, P., & Viola Vogel, B. (2018) · Science Advances · doi:10.1126/sciadv.aao4881 · Cited by 149 · see citing works
Deng, Z. J., Liang, M., Tóth, I., Monteiro, M. J., & Minchin, R. F. (2012) · Nanotoxicology · doi:10.3109/17435390.2012.655342 · Cited by 146 · see citing works
Mechano-therapeutics: Targeting Mechanical Signaling in Fibrosis and Tumor Stroma
Tschumperlin, D. J., & Lagares, D. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107575 · Cited by 142 · see citing works
Baugh, L., & Viola Vogel, B. (2004) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.30026 · Cited by 141 · see citing works
Dynamics and mechanisms of quantum dot nanoparticle cellular uptake
Xiao, Y., Forry, S. P., Gao, X., Holbrook, R. D., Telford, W. G., & Tona, A. (2010) · Journal of Nanobiotechnology · doi:10.1186/1477-3155-8-13 · Cited by 141 · see citing works
Stealth Effect of Biomolecular Corona on Nanoparticle Uptake by Immune Cells
Caracciolo, G., Palchetti, S., Colapicchioni, V., Digiacomo, L., Pozzi, D., Capriotti, A. L., La Barbera, G., & Laganà, A. (2015) · Langmuir · doi:10.1021/acs.langmuir.5b02158 · Cited by 131 · see citing works
Cai, R., Ren, J., Ji, Y., Wang, Y., Liu, Y., Chen, Z.-Q., Sabet, Z. F., Wu, X.-C., Lynch, I., & Chen, C.-Y. (2019) · ACS Applied Materials and Interfaces · doi:10.1021/acsami.9b15910 · Cited by 131 · see citing works
Microelectrode measurements of local mass transport rates in heterogeneous biofilms
Rasmussen, K., & Lewandowski, Z. (1998) · Biotechnology and Bioengineering · doi:10.1002/(sici)1097-0290(19980805)59:3 · Cited by 130 · see citing works
Immunological Responses Induced by Blood Protein Coronas on Two-Dimensional MoS2 Nanosheets
Baimanov, D., Wu, J., Chu, R., Cai, R., Wang, B., Cao, M., Tao, Y., Liu, J., Guo, M., Wang, J., et al. (2020) · ACS Nano · doi:10.1021/acsnano.9b09744 · Cited by 130 · see citing works
Brummitt, R. K., Nesta, D. P., Chang, L., Chase, S. F., Laue, T. M., & Roberts, C. J. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22448 · Cited by 125 · see citing works
Wang, W., Huang, Z., Li, Y., Wang, W., Shi, J., Fu, F., Huang, Y., Pan, X., & Wu, C. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.023 · Cited by 123 · see citing works
Singh, N., Marets, C., Boudon, J., Millot, N., Saviot, L., & Maurizi, L. (2021) · Nanoscale Advances · doi:10.1039/d0na00863j · Cited by 118 · see citing works
Bharti, B., Meissner, J., Klapp, S. H. L., & Findenegg, G. H. (2013) · Soft Matter · doi:10.1039/c3sm52401a · Cited by 117 · see citing works
Gold Nanoparticles and Their Applications in Biomedicine
Versiani, A. F., de Andrade, L. M., Martins, E. M. N., Scalzo, S., Geraldo, J. M., Chaves, C. R., Ferreira, D. C., Ladeira, M. S., Guatimosim, S., Ladeira, L. O., et al. (2016) · Future Virology · doi:10.2217/fvl-2015-0010 · Cited by 117 · see citing works
Xu, Z., Yang, Q.-Q., Lan, J., Zhang, J., Wu, P. T., Jin, J.-C., Jiang, F., & Liu, Y. (2015) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2015.08.062 · Cited by 116 · see citing works
Pinals, R. L., Chio, L., Ledesma, F., & Landry, M. P. (2020) · The Analyst · doi:10.1039/d0an00633e · Cited by 115 · see citing works
[7] Human factor XII (Hageman factor)
Griffin, J. H., & Cochrane, C. G. (1976) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(76)45009-7 · Cited by 115 · see citing works
Ustunol, I. B., González-Pech, N. I., & Grassian, V. H. (2019) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2019.06.086 · Cited by 114 · see citing works
Disease-specific protein corona sensor arrays may have disease detection capacity
Caracciolo, G., Safavi‐Sohi, R., Malekzadeh, R., Poustchi, H., Vasighi, M., Chiozzi, R. Z., Capriotti, A. L., Laganà, A., Hajipour, M. J., Domenico, M. D., et al. (2019) · Nanoscale Horizons · doi:10.1039/c9nh00097f · Cited by 113 · see citing works
Coating nanoparticles with tunable surfactants facilitates control over the protein corona
Müller, J., Bauer, K. N., Prozeller, D., Simon, J., Mailänder, V., Wurm, F. R., Winzen, S., & Landfester, K. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.11.015 · Cited by 113 · see citing works
Sato, Y., Kinami, Y., Hashiba, K., & Harashima, H. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.03.006 · Cited by 108 · see citing works
Probing the Limits of Aptamer Affinity with a Microfluidic SELEX Platform
Ahmad, K. M., Oh, S. S., Kim, S. W., McClellen, F. M., Xiao, Y., & Soh, H. T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027051 · Cited by 106 · see citing works
Breast cancer cells alter the dynamics of stromal fibronectin-collagen interactions
Wang, K., Wu, F., Seo, B. R., Fischbach, C., Chen, W., Hsu, L., & Gourdon, D. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.08.001 · Cited by 105 · see citing works
Self-citationMeyer, B. K., Petrulis, J. R., & Perdew, G. H. (2000) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2000)005 · Cited by 105 · see citing works
Palchetti, S., Pozzi, D., Capriotti, A. L., Barbera, G. L., Chiozzi, R. Z., Digiacomo, L., Peruzzi, G., Caracciolo, G., & Laganà, A. (2017) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2017.02.037 · Cited by 105 · see citing works
A health concern regarding the protein corona, aggregation and disaggregation
Falahati, M., Attar, F., Sharifi, M., Haertlé, T., Berret, J., Khan, R. H., & Saboury, A. A. (2019) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2019.02.012 · Cited by 105 · see citing works
Demanèche, S., Chapel, J., Monrozier, L. J., & Quiquampoix, H. (2009) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2008.12.036 · Cited by 103 · see citing works
Probing Adsorption Behaviors of BSA onto Chiral Surfaces of Nanoparticles
Wang, X., Wang, X., Wang, M., Zhang, D., Yang, Q., Liu, T., Lei, R., Zhu, S., Zhao, Y., & Chen, C. (2018) · Small · doi:10.1002/smll.201703982 · Cited by 102 · see citing works
Bio-inspired silica–collagen materials: applications and perspectives in the medical field
Heinemann, S., Coradin, T., & Desimone, M. F. (2013) · Biomaterials Science · doi:10.1039/c3bm00014a · Cited by 100 · see citing works
Guo, M., Zhao, L., Liu, J., Wang, X., Yao, H., Chang, X., Liu, Y., Liu, J., You, M., Ren, J., et al. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c01048 · Cited by 99 · see citing works
Nanomedicine Delivery: does Protein Corona Route to the Target or off Road?
Maiolo, D., del Pino, P., Metrangolo, P., Parak, W. J., & Bombelli, F. B. (2015) · Nanomedicine · doi:10.2217/nnm.15.163 · Cited by 98 · see citing works
Protein adsorption in fused‐silica and polyacrylamide‐coated capillaries
Graf, M., García, R. G., & Wätzig, H. (2005) · Electrophoresis · doi:10.1002/elps.200410360 · Cited by 97 · see citing works
Solution and surface effects on plasma fibronectin structure.
Tooney, N. M., Mosesson, M. W., Amrani, D., Hainfeld, J. F., & Wall, J. S. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.6.1686 · Cited by 95 · see citing works
Pharmaceutical and biomedical applications of quantum dots
Bajwa, N., Mehra, N. K., Jain, K., & Jain, N. K. (2015) · Artificial Cells Nanomedicine and Biotechnology · doi:10.3109/21691401.2015.1052468 · Cited by 92 · see citing works
Kinetics of conformational changes of fibronectin adsorbed onto model surfaces
Baujard-Lamotte, L., Noinville, S., Goubard, F., Marque, P., & Pauthe, E. (2007) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2007.11.015 · Cited by 92 · see citing works
Adsorption of proteins on gold nanoparticles: One or more layers?
Sotnikov, D. V., Berlina, A. N., Ivanov, V. S., Zherdev, A. V., & Dzantiev, B. B. (2018) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2018.10.025 · Cited by 89 · see citing works
Wang, H., Ma, R., Nienhaus, K., & Nienhaus, G. U. (2019) · Small · doi:10.1002/smll.201900974 · Cited by 84 · see citing works
Quiquampoix, H., & Ratcliffe, R. G. (1992) · Journal of Colloid and Interface Science · doi:10.1016/0021-9797(92)90173-j · Cited by 82 · see citing works
Wang, K., Eguiluz, R. C. A., Wu, F., Seo, B. R., Fischbach, C., & Gourdon, D. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.03.019 · Cited by 82 · see citing works
Self-citationXu, Z., & Grassian, V. H. (2017) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.7b07525 · Cited by 80 · see citing works
Electrostatic effects in collagen fibril formation
Morozova, S., & Muthukumar, M. (2018) · The Journal of Chemical Physics · doi:10.1063/1.5036526 · Cited by 79 · see citing works
Ho, Y. T., Azman, N. ‘., Loh, F. W. Y., Ong, G. K. T., Engudar, G., Kriz, S. A., & Kah, J. C. Y. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00743 · Cited by 77 · see citing works
Murayama, K., Wu, Y., Czarnik‐Matusewicz, B., & Ozaki, Y. (2001) · The Journal of Physical Chemistry B · doi:10.1021/jp004537a · Cited by 76 · see citing works
Enhanced Cancer-targeted Drug Delivery Using Precoated Nanoparticles
Yu, L., Xu, M., Xu, W., Xiao, W., Jiang, X., Wang, L., & Gao, H. (2020) · Nano Letters · doi:10.1021/acs.nanolett.0c03982 · Cited by 74 · see citing works
Plasma concentration gradient influences the protein corona decoration on nanoparticles
Ghavami, M., Saffar, S., Emami, B. A., Peirovi, A., Shokrgozar, M. A., Serpooshan, V., & Mahmoudi, M. (2012) · RSC Advances · doi:10.1039/c2ra22093h · Cited by 73 · see citing works
Lv, L., Li, K., Xie, Y., Cao, Y., & Zheng, X. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.04.056 · Cited by 73 · see citing works
Protein Corona in Response to Flow: Effect on Protein Concentration and Structure
Jayaram, D. T., Pustulka, S. M., Mannino, R. G., Lam, W. A., & Payne, C. K. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.02.036 · Cited by 72 · see citing works
Zaccariello, G., Back, M., Zanello, M., Canton, P., Cattaruzza, E., Riello, P., Alimonti, A., & Benedetti, A. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b13252 · Cited by 71 · see citing works
Yu, G., & Zhou, J. W. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp01478j · Cited by 71 · see citing works
Gorshkov, V., Bubis, J. A., Solovyeva, E. M., Gorshkov, M. V., & Kjeldsen, F. (2019) · Environmental Science Nano · doi:10.1039/c8en01054d · Cited by 70 · see citing works
Probing fibronectin conformation on a protein corona layer around nanoparticles
Raoufi, M., Hajipour, M. J., Shahri, S. M. K., Schoen, I., Linn, U., & Mahmoudi, M. (2017) · Nanoscale · doi:10.1039/c7nr06970g · Cited by 69 · see citing works
Kari, O. K., Ndika, J., Parkkila, P., Louna, A., Lajunen, T., Puustinen, A., Viitala, T., Alenius, H. T., & Urtti, A. O. (2019) · Nanoscale · doi:10.1039/c9nr08186k · Cited by 69 · see citing works
Qu, S., Sun, F., Qiao, Z., Li, J., & Shang, L. (2020) · Small · doi:10.1002/smll.201907633 · Cited by 69 · see citing works
New Hybrid Organic/Inorganic Polysilsesquioxane–Silica Particles as Sunscreens
Tolbert, S. H., McFadden, P. D., & Loy, D. A. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b10472 · Cited by 68 · see citing works
Unfolded Protein Corona Surrounding Nanotubes Influence the Innate and Adaptive Immune System
Park, J., Park, S. J., Park, J. Y., Kim, S., Kwon, S. C., Jung, Y., & Khang, D. (2021) · Advanced Science · doi:10.1002/advs.202004979 · Cited by 66 · see citing works
Effects of gold nanoparticle morphologies on interactions with proteins
Wang, G., Wang, W., Shangguan, E., Gao, S., & Liu, Y. (2020) · Materials Science and Engineering C · doi:10.1016/j.msec.2020.110830 · Cited by 64 · see citing works
In Situ Analysis of Weakly Bound Proteins Reveals Molecular Basis of Soft Corona Formation
Sánchez-Guzmán, D., Giraudon--Colas, G., Marichal, L., Boulard, Y., Wien, F., Degrouard, J., Baeza‐Squiban, A., Pin, S., Renault, J., & Devineau, S. (2020) · ACS Nano · doi:10.1021/acsnano.0c04165 · Cited by 63 · see citing works
Selective Accelerated Proliferation of Malignant Breast Cancer Cells on Planar Graphene Oxide Films
Kenry, K., Chaudhuri, P. K., Loh, K. P., & Lim, C. T. (2016) · ACS Nano · doi:10.1021/acsnano.5b07409 · Cited by 62 · see citing works
Li, K., Liu, S., Hu, T., Razanau, I. U., Wu, X., Ao, H., Huang, L., Xie, Y., & Zheng, X. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.9b01717 · Cited by 62 · see citing works
Kinetics and Mechanisms of Protein Adsorption and Conformational Change on Hematite Particles
Liu, F., Li, X., Sheng, A., Shang, J., Wang, Z., & Liu, J. (2019) · Environmental Science & Technology · doi:10.1021/acs.est.9b02651 · Cited by 61 · see citing works
Adsorption of Myoglobin and Corona Formation on Silica Nanoparticles
Lee, J. G., Lannigan, K., Shelton, W. A., Meissner, J., & Bharti, B. (2020) · Langmuir · doi:10.1021/acs.langmuir.0c01613 · Cited by 61 · see citing works
Biopolymer-coated gold nanoparticles inhibit human insulin amyloid fibrillation
Meesaragandla, B., Karanth, S., Janke, U., & Delcea, M. (2020) · Scientific Reports · doi:10.1038/s41598-020-64010-7 · Cited by 60 · see citing works
Abduraimova, A., Molkenova, A., Duisembekova, A., Mulikova, T., Kanayeva, D. A., & Atabaev, T. S. (2021) · Nanomaterials · doi:10.3390/nano11020477 · Cited by 60 · see citing works
Khanal, D., Kondyurin, A. V., Hau, H., Knowles, J. C., Levinson, O., Ramzan, I. M., Fu, D., Marcott, C. A., & Chrzanowski, W. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00665 · Cited by 59 · see citing works
Capillary blood flow imaging within human finger cuticle using optical microangiography
Baran, U., Shi, L., & Wang, R. K. (2013) · Journal of Biophotonics · doi:10.1002/jbio.201300154 · Cited by 59 · see citing works
Mukhopadhyay, A., Basu, S., Singha, S., & Patra, H. K. (2018) · Research · doi:10.1155/2018/9712832 · Cited by 58 · see citing works
Abnormalities of prothrombin: a review of the pathophysiology, diagnosis, and treatment
Meeks, S. L., & Abshire, T. C. (2008) · Haemophilia · doi:10.1111/j.1365-2516.2008.01832.x · Cited by 57 · see citing works
Understanding Protein Structure Deformation on the Surface of Gold Nanoparticles of Varying Size
Woods, K. E., Perera, Y. R., Davidson, M. B., Wilks, C. A., Yadav, D. K., & Fitzkee, N. C. (2016) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.6b08089 · Cited by 57 · see citing works
Inside the Protein Corona: From Binding Parameters to Unstained Hard and Soft Coronas Visualization
Galdino, F. E., Picco, A. S., Capeletti, L. B., Bettini, J., & Cardoso, M. B. (2021) · Nano Letters · doi:10.1021/acs.nanolett.1c02416 · Cited by 57 · see citing works
Emerging opportunities of silica-based materials within the food industry
Videira‐Quintela, D., Martín, O., & Montalvo, G. (2021) · Microchemical Journal · doi:10.1016/j.microc.2021.106318 · Cited by 54 · see citing works
Engineering extracellular matrix to improve drug delivery for cancer therapy
He, X., Yang, Y., Li, L., Zhang, P., Guo, H., Liu, N., Yang, X., & Xu, F. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.06.029 · Cited by 54 · see citing works
Mo, J., Xu, Y., Wang, X., Wei, W., & Zhao, J. (2019) · Nanoscale · doi:10.1039/c9nr08570j · Cited by 54 · see citing works
Simon, J., Müller, J., Ghazaryan, A., Morsbach, S., Mailänder, V., & Landfester, K. (2018) · Nanoscale · doi:10.1039/c8nr07424k · Cited by 53 · see citing works
Influence of nanoparticle mechanical property on protein corona formation
Tengjisi, Hui, Y., Fan, Y., Zou, D., Talbo, G. H., Yang, G., & Zhao, C. (2021) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2021.08.148 · Cited by 51 · see citing works
Trinh, D. N., Gardner, R. A., Franciosi, A. N., McCarthy, C., Keane, M. P., Soliman, M. G., O’Donnell, J. S., Meleady, P., Spencer, D. I. R., & Monopoli, M. P. (2022) · ACS Nano · doi:10.1021/acsnano.1c09564 · Cited by 51 · see citing works
Marichal, L., Degrouard, J., Gatin, A., Raffray, N., Aude, J.-C., Boulard, Y., Combet, S., Cousin, F., Hourdez, S., Mary, J., et al. (2020) · Langmuir · doi:10.1021/acs.langmuir.0c01334 · Cited by 50 · see citing works
Gee, E. P. S., Ingber, D. E., & Stultz, C. M. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002373 · Cited by 49 · see citing works
Yin, M.-M., Chen, W.-Q., Lu, Y.-Q., Han, J., Liu, Y., & Jiang, F. (2020) · Nanoscale · doi:10.1039/c9nr09170j · Cited by 49 · see citing works
Wang, S., Fang, Y., Zhang, Z., Jin, Q., & Ji, J. (2021) · Colloids and Interface Science Communications · doi:10.1016/j.colcom.2020.100354 · Cited by 48 · see citing works
Felgueiras, H. P., Sommerfeld, S. D., Murthy, N. S., Kohn, J., & Migonney, V. (2014) · Langmuir · doi:10.1021/la501862f · Cited by 46 · see citing works
Gros, G., Forster, R. E., & Lin, L. Q. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33310-0 · Cited by 43 · see citing works
Huang, S., Qiu, H., Xie, J., Huang, C., Su, W., Hu, B., & Xiao, Q. (2016) · RSC Advances · doi:10.1039/c6ra01386d · Cited by 43 · see citing works
Sukhanova, A. V., Poly, S., Bozrova, S. V., Lambert, É., Ewald, M., Karaulov, A. V., Molinari, M., & Nabiev, I. R. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00480 · Cited by 42 · see citing works
H-Bonding-mediated binding and charge reorganization of proteins on gold nanoparticles
Meesaragandla, B., Garcı́a, I., Biedenweg, D., Toro‐Mendoza, J., Ivan Coluzza, B., Liz‐Marzán, L. M., & Delcea, M. (2020) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp06371d · Cited by 42 · see citing works
Human plasma protein corona decreases the toxicity of pillar-layer metal organic framework
Jafari, S., Izadi, Z., Alaei, L., Jaymand, M., Samadian, H., Kashani, V. O., Derakhshankhah, H., Hayati, P., Noori, F., Mansouri, K., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71170-z · Cited by 42 · see citing works
Wen, M., Li, Y., Zhong, W., Li, Q., Cao, L., Tan, L., & Shang, L. (2021) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2021.12.044 · Cited by 42 · see citing works
Weiss, A. C. G., Kempe, K., Förster, S., & Caruso, F. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b00196 · Cited by 41 · see citing works
Plasma Fibronectin Concentration
Mosher, D. F. (2006) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000223342.15969.7a · Cited by 41 · see citing works
Caño, R. D., Mateus, L., Sánchez-Obrero, G., Sevilla, J. M., Madueño, R., Blázquez, M., & Pineda, T. (2017) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2017.07.011 · Cited by 40 · see citing works
The intracellular ionic strength of red cells and the influence of complex formation
Mouat, M. F., & Manchester, K. L. (1998) · Comparative Clinical Pathology · doi:10.1007/bf02628107 · Cited by 40 · see citing works
Vahidi, S., Stocks, B. B., Mobarhan, Y. L., & Konermann, L. (2012) · Analytical Chemistry · doi:10.1021/ac302393g · Cited by 40 · see citing works
Bychkova, A. V., Lopukhova, M. V., Wasserman, L. A., Degtyarev, Y. N., Kovarski, A. L., Chakraborti, S., & Mitkevich, V. A. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.11.110 · Cited by 40 · see citing works
Li, X., Guo, W., Xu, R., Song, Z., & Ni, T. (2022) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2022.120983 · Cited by 40 · see citing works
Devineau, S., Zargarian, L., Renault, J., & Pin, S. (2017) · Langmuir · doi:10.1021/acs.langmuir.6b04281 · Cited by 38 · see citing works
Zhu, Y. F., Jiang, P., Luo, B., Lan, F., He, J. H., & Wu, Y. (2019) · Nanoscale · doi:10.1039/c8nr08614a · Cited by 38 · see citing works
Vitali, M., Rigamonti, V., Natalello, A., Colzani, B., Avvakumova, S., Brocca, S., Santambrogio, C., Narkiewicz, J., Legname, G., Colombo, M., et al. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.03.026 · Cited by 38 · see citing works
Moustaoui, H., Saber, J., Djeddi, I., Liu, Q., Movia, D., Prina‐Mello, A., Spadavecchia, J., de la Chapelle, M. L., & Djaker, N. (2019) · Nanoscale · doi:10.1039/c8nr09891c · Cited by 38 · see citing works
Luminescence turn-on/off sensing of biological iron by carbon dots in transferrin
Bhattacharya, A. A., Chatterjee, S., Khorwal, V., & Mukherjee, T. K. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c5cp05890b · Cited by 37 · see citing works
Impact of plasma concentration of transferrin on targeting capacity of nanoparticles
Sepand, M. R., Ghavami, M., Zanganeh, S., Stacks, S., Ghasemi, F., Montazeri, H., Corbo, C., Derakhshankhah, H., Ostad, S. N., Ghahremani, M. H., et al. (2020) · Nanoscale · doi:10.1039/c9nr08784b · Cited by 37 · see citing works
Interaction of γ-Fe2O3 nanoparticles with fibrinogen
Zhang, H., Wu, P., Zhu, Z., & Wang, Y. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.06.087 · Cited by 36 · see citing works
Elberskirch, L., Binder, K., Riefler, N., Sofranko, A., Liebing, J., Minella, C. B., Mädler, L., Razum, M., van Thriel, C., Unfried, K., et al. (2022) · Particle and Fibre Toxicology · doi:10.1186/s12989-021-00442-x · Cited by 35 · see citing works
Cell-Conditioned Protein Coronas on Engineered Particles Influence Immune Responses
Dai, Q., Guo, J., Yan, Y., Ang, C., Bertleff‐Zieschang, N., & Caruso, F. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.6b01545 · Cited by 35 · see citing works
Ghosh, G., Panicker, L., Ningthoujam, R. S., Barick, K. C., & Tewari, R. (2012) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2012.10.034 · Cited by 34 · see citing works
Muzzio, N., Pasquale, M., Ríos, X., Azzaroni, O., Llop, J., & Moya, S. (2019) · Advanced Materials Interfaces · doi:10.1002/admi.201900008 · Cited by 34 · see citing works
Contrasting Effects of Nanoparticle Binding on Protein Denaturation
Chen, P., Seabrook, S. A., Epa, V. C., Kurabayashi, K., Barnard, A. S., Winkler, D. A., Kirby, J. K., & Ke, P. C. (2014) · The Journal of Physical Chemistry C · doi:10.1021/jp506135m · Cited by 34 · see citing works
Yang, N., & Qin, Q. (2015) · Chinese Medical Journal · doi:10.4103/0366-6999.164983 · Cited by 33 · see citing works
Role of surface charge on the interaction between carbon nanodots and human serum albumin
Li, M., Xiao, C.-Q., Xu, Z., Yin, M.-M., Yang, Q.-Q., Yin, Y.-L., & Liu, Y. (2018) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2018.06.082 · Cited by 33 · see citing works
Chinnathambi, S., Hanagata, N., Yamazaki, T., & Shirahata, N. (2020) · Nanomaterials · doi:10.3390/nano10112250 · Cited by 33 · see citing works
Li, M., Zhang, X., Li, S., Shao, X., Chen, H., Lv, L., & Huang, X. (2021) · RSC Advances · doi:10.1039/d1ra02116h · Cited by 32 · see citing works
Barbir, R., Jiménez, R. R., Martín‐Rapún, R., Strasser, V., Jurašin, D. D., Dabelić, S., de la Fuente, J. M., & Vrček, I. V. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c04063 · Cited by 31 · see citing works
Siani, P., & Valentin, C. D. (2022) · Nanoscale · doi:10.1039/d1nr07647g · Cited by 30 · see citing works
Matsui, N., Nozaki, K., Ishihara, K., Yamashita, K., & Nagai, A. (2014) · Materials Science and Engineering C · doi:10.1016/j.msec.2014.12.042 · Cited by 30 · see citing works
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Havelikar, U. A., Ghorpade, K. B., Kumar, A., Patel, A., Singh, M., Banjare, N., & Gupta, P. N. (2024) · Discover Nano · doi:10.1186/s11671-024-04118-1 · Cited by 205 · see citing works
Hosseini-Kharat, M., Bremmell, K. E., & Prestidge, C. A. (2025) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2025.101436 · Cited by 188 · see citing works
Mrksich, K., Padilla, M. S., & Mitchell, M. J. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115446 · Cited by 155 · see citing works
Self-citationZheng, Y., Luo, S., Xu, M., He, Q., Xie, J., Wu, J., & Huang, Y. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.06.015 · Cited by 132 · see citing works
Placenta-tropic VEGF mRNA lipid nanoparticles ameliorate murine pre-eclampsia
Swingle, K. L., Hamilton, A. G., Safford, H. C., Geisler, H. C., Thatte, A. S., Palanki, R., Murray, A. M., Han, E. L., Mukalel, A. J., Han, X., et al. (2025) · Nature · doi:10.1038/s41586-024-08291-2 · Cited by 129 · see citing works
Self-citationOmo‐Lamai, S., Zamora, M. E., Patel, M. N., Wu, J., Nong, J., Wang, Z., Peshkova, A. D., Majumder, A., Melamed, J. R., Chase, L. S., et al. (2024) · Advanced Materials · doi:10.1002/adma.202312026 · Cited by 120 · see citing works
Cutting-edge approaches for targeted drug delivery in breast cancer: beyond conventional therapies
Chaudhari, R. H., Patel, V., & Kumar, A. (2024) · Nanoscale Advances · doi:10.1039/d4na00086b · Cited by 104 · see citing works
López-Estévez, A. M., Lapuhs, P., Pineiro‐Alonso, L., & Alonso, M. J. (2023) · Advanced Materials · doi:10.1002/adma.202309355 · Cited by 90 · see citing works
Application of Nanoparticles in Cancer Treatment: A Concise Review
Sell, M., Lopes, A. R., Escudeiro, M., Esteves, B., Monteiro, A. R., Trindade, T., & Cruz‐Lopes, L. (2023) · Nanomaterials · doi:10.3390/nano13212887 · Cited by 85 · see citing works
Recent Developments in Nanoparticle‐Hydrogel Hybrid Materials for Controlled Release
Fan, Y., Han, Q., Li, H., Cai, X., Dyett, B., Qiao, R., Drummond, C. J., Thang, S. H., & Zhai, J. (2025) · Advanced Science · doi:10.1002/advs.202507209 · Cited by 76 · see citing works
Influence of ionizable lipid tail length on lipid nanoparticle delivery of mRNA of varying length
Mrksich, K., Padilla, M. S., Joseph, R. A., Han, E. L., Kim, D., Palanki, R., Xu, J., & Mitchell, M. J. (2024) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.37705 · Cited by 65 · see citing works
Self-citationTeixeira, M. I., Lopes, C. M., Amaral, M. H., & Costa, P. C. (2024) · Acta Biomaterialia · doi:10.1016/j.actbio.2024.09.027 · Cited by 58 · see citing works
Hamilton, A. G., Swingle, K. L., Thatte, A. S., Mukalel, A. J., Safford, H. C., Billingsley, M. M., El-Mayta, R. D., Han, X., Nachod, B. E., Joseph, R. A., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c01171 · Cited by 55 · see citing works
Self-citationCybulski, P., Bravo, M. L., Chen, J. J., Zundert, I. V., Krzyzowska, S., Taemaitree, F., Uji‐i, H., Hofkens, J., Rocha, S., & Fortuni, B. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1520078 · Cited by 52 · see citing works
Kochman, U., Sitka, H., Kuźniar, J., Czaja, M., Kozubek, P., Beszłej, J. A., & Leszek, J. (2026) · Molecular Neurobiology · doi:10.1007/s12035-025-05417-z · Cited by 60 · see citing works
Unlocking the Potential of Silver Nanoparticles: From Synthesis to Versatile Bio-Applications
Almatroudi, A. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16091232 · Cited by 51 · see citing works
Jacinto, C., Javed, Y., Lavorato, G. C., Tárraga, W. A., Conde, B. I. C., Henao, J. M. O., Picco, A. S., Garcia, J., Dias, C. S. B., Malik, S., et al. (2025) · Nanoscale Advances · doi:10.1039/d5na00195a · Cited by 54 · see citing works
In-silico strategies in nano-drug design: Bridging nanomaterials and pharmacological applications
Dalbanjan, N. P., Korgaonkar, K., Eelager, M. P., Gonal, B. N., Kadapure, A. J., Arakera, S. B., & Kumar, S. K. P. (2025) · Nano TransMed · doi:10.1016/j.ntm.2025.100091 · Cited by 47 · see citing works
Moghadam, M. E., Sadeghi, M., Mansouri‐Torshizi, H., & Saeidifar, M. (2023) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2023.106477 · Cited by 45 · see citing works
Design Considerations for Organ-Selective Nanoparticles
Baek, M., Hur, W., Kashiwagi, S., & Choi, H. S. (2025) · ACS Nano · doi:10.1021/acsnano.5c00484 · Cited by 45 · see citing works
Peptide codes for organ-selective mRNA delivery
Chang, T., Zheng, Y., Jiang, M., Jia, S., Bai, J., Zheng, Z., Li, S., Guo, J., Wang, Y., Wang, Y., et al. (2025) · Nature Materials · doi:10.1038/s41563-025-02331-6 · Cited by 51 · see citing works
Decoding Nanomaterial‐Biosystem Interactions through Machine Learning
Dhoble, S., Wu, T., & Kenry, K. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202318380 · Cited by 42 · see citing works
Samal, P., Satpathy, S., Panigrahi, L. L., Jha, S., & Arakha, M. (2025) · Nanoscale Horizons · doi:10.1039/d5nh00076a · Cited by 39 · see citing works
The Protein Corona Paradox: Challenges in Achieving True Biomimetics in Nanomedicines
Mayordomo, N. M., Zatarain-Beraza, A., Valerio, F., Álvarez-Méndez, V., Turegano, P., Herranz-García, L., de Aguileta, A. L., Cattani, N., Álvarez-Alonso, A., & Fanárraga, M. L. (2025) · Biomimetics · doi:10.3390/biomimetics10050276 · Cited by 38 · see citing works
Nanometrology: particle sizing and influence on the toxicological profile
Mota, W. S., Severino, P. B., Kadian, V., Rao, R., Zielińska, A., Silva, A. M., Mahant, S., & Souto, E. B. (2025) · Frontiers in Nanotechnology · doi:10.3389/fnano.2025.1479464 · Cited by 38 · see citing works
Younas, A., Wang, S., Asad, M., al Mamun, A., Majeed, S., Sharif, A., Zhou, Q., Liu, Y., Geng, P.-W., Shao, C.-X., et al. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102660 · Cited by 61 · see citing works
Mechanisms of extracellular vesicle uptake and implications for the design of cancer therapeutics
Jackson, S. R., Flemming, J. P., Karagoz, K., Wermuth, P. J., & Mahoney, M. G. (2024) · Journal of Extracellular Biology · doi:10.1002/jex2.70017 · Cited by 37 · see citing works
Dar, A. I., Randhawa, S., Verma, M., Saini, T. C., & Acharya, A. (2025) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2025.103535 · Cited by 35 · see citing works
Madhusudanan, M., Zhang, J., Pandit, S., Singh, P., Jeong, G., Khan, F., & Mijakovic̀, I. (2025) · Advanced NanoBiomed Research · doi:10.1002/anbr.202400194 · Cited by 35 · see citing works
Isaac, I., Patel, L., Tran, N., Singam, A., Yun, D., Guha, P., Park, S., & Bhattacharya, C. (2025) · Advanced Materials · doi:10.1002/adma.202507657 · Cited by 33 · see citing works
Wang, S., Wang, H., Drabek, A. A., Smith, W. S., Liang, F., & Huang, Z. R. (2023) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.3c00735 · Cited by 34 · see citing works
Emerging strategies for nanomedicine in autoimmunity
Thatte, A. S., Billingsley, M. M., Weissman, D., Melamed, J. R., & Mitchell, M. J. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115194 · Cited by 35 · see citing works
Self-citationCroitoru, G.-A., Pîrvulescu, D.-C., Niculescu, A.-G., Epistatu, D., Rădulescu, M., Grumezescu, A. M., & Nicolae, C.-L. (2024) · Journal of Functional Biomaterials · doi:10.3390/jfb15080225 · Cited by 32 · see citing works
Singh, S. R., Kittur, B., Bhavi, S. M., Thokchom, B., Padti, A. C., Bhat, S. S., Bajire, S. K., Shastry, R. P., Srinath, B. S., Sillanpää, M. E. T., et al. (2024) · Hybrid Advances · doi:10.1016/j.hybadv.2024.100359 · Cited by 32 · see citing works
Artificial protein coronas: directing nanoparticles to targets
Caracciolo, G. (2024) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2024.05.003 · Cited by 31 · see citing works
Rui, X., Fu, K. G., Wang, H., Pan, T., & Wang, W. (2025) · Foods · doi:10.3390/foods14030512 · Cited by 32 · see citing works
Recent Advances in Simulation Studies on the Protein Corona
Lee, H. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16111419 · Cited by 25 · see citing works
Green synthesis of yeast cell wall-derived carbon quantum dots with multiple biological activities
Mirseyed, P. S., Arjmand, S., Rahmandoust, M., Kheirabadi, S., & Anbarteh, R. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e29440 · Cited by 23 · see citing works
Wu, J., Gupta, G. S., Buerki‐Thurnherr, T., Nowack, B., & Wick, P. (2024) · NanoImpact · doi:10.1016/j.impact.2024.100533 · Cited by 23 · see citing works
Protein-functionalized nanoparticles: Emerging strategies in drug delivery
Wietrzyk, A., Hutny, A., Jonderko, L., Biliński, K., Makieła, M., Kalinin, J., Jachimska, B., & Kulbacka, J. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118337 · Cited by 23 · see citing works
Daramy, K., Punnabhum, P., Hussain, M., Minelli, C., Pei, Y., Rattray, N. J. W., Perrie, Y., & Rattray, Z. (2023) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2023.12.021 · Cited by 22 · see citing works
Mehta, P., & Shende, P. K. (2023) · Cell Biochemistry and Function · doi:10.1002/cbf.3880 · Cited by 21 · see citing works
der Sanden, N. V., Paun, R. A., Yitayew, M. Y., Boyadjian, O., & Tabrizian, M. (2024) · Nanoscale Advances · doi:10.1039/d4na00783b · Cited by 21 · see citing works
Younis, M. A., Sato, Y., Kimura, S., & Harashima, H. (2025) · RSC Pharmaceutics · doi:10.1039/d5pm00079c · Cited by 22 · see citing works
Effect of the Protein Corona Formation on Antibody Functionalized Liquid Lipid Nanocarriers
Navarro-Marchal, S. A., Martín-Contreras, M., Castro-Santiago, D., del Castillo-Santaella, T., Graván, P., Jódar‐Reyes, A. B., Marchal, J. A., & Peula-García, J. M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242316759 · Cited by 20 · see citing works
Surface ligand-regulated renal clearance of MRI/SPECT dual-modality nanoprobes for tumor imaging
Chen, C., Huang, B., Zhang, R., Sun, C., Chen, L., Ge, J., Zhou, D., Li, Y., Wu, S., Qian, Z., et al. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02516-2 · Cited by 20 · see citing works
Ahmadi, M., Ayyoubzadeh, S. M., Ardakani, S. A., Ghaedrahmat, Z., Masoumi, N., Farnia, M. M., & Ghorbani-Bidkorpeh, F. (2025) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2025.126094 · Cited by 20 · see citing works
Protein Aggregation on Metal Oxides Governs Catalytic Activity and Cellular Uptake
Nißler, R., Dennebouy, L., Gogos, A., Gerken, L. R. H., Dommke, M., Zimmermann, M., Pais, M. A., Neuer, A. L., Matter, M. T., Kissling, V. M., et al. (2024) · Small · doi:10.1002/smll.202311115 · Cited by 20 · see citing works
Impact of Protein Coronas on Lipid Nanoparticle Uptake and Endocytic Pathways in Cells
Wang, R., He, J., Xu, Y., & Peng, B. (2024) · Molecules · doi:10.3390/molecules29204818 · Cited by 19 · see citing works
Castillo, C., Jeon, S., Hoang, K. N. L., Alford, C., Svendahl, E., Deng, C., Wang, Y., Wang, Y., Wei, X., Hernandez, R., et al. (2025) · Nature Nanotechnology · doi:10.1038/s41565-025-01944-x · Cited by 18 · see citing works
The Challenges and Opportunities of Protein Coronas for Nanoscale Biomolecular Sensing
Cheeseman, S., Moazzam, P., Mahmoudi, N., Mahmoudi, M., Caruso, F., Tricoli, A., & Nisbet, D. R. (2025) · Small · doi:10.1002/smll.202503820 · Cited by 18 · see citing works
Moya, S. E., Ruiz-Hernández, R., & Angelomé, P. C. (2024) · Advanced NanoBiomed Research · doi:10.1002/anbr.202400005 · Cited by 18 · see citing works
Toxicity of nanostructures in drug delivery applications
Edo, G. I., Ali, A. B. M., Okolie, M. C., Orogu, J. O., Emumejaye, K., Oghroro, E. E. A., Jikah, A. N., Yousif, E. A., Igbuku, U. A., Owheruo, J. O., et al. (2026) · Pharmaceutical Science Advances · doi:10.1016/j.pscia.2026.100117 · Cited by 17 · see citing works
Multiscale physics-based in silico modelling of nanocarrier-assisted intravascular drug delivery
Buchete, N., Cicha, I., Dutta, S., & Neofytou, P. (2024) · Frontiers in Drug Delivery · doi:10.3389/fddev.2024.1362660 · Cited by 17 · see citing works
The nanoparticle-Protein Corona untold history (1907–2007)
Casals, E., Vitali, M., & Puntes, V. (2024) · Nano Today · doi:10.1016/j.nantod.2024.102435 · Cited by 17 · see citing works
Lim, J., Oh, D., Cheng, M., Chintapula, U. K., Liu, S., Reynolds, D., Zhang, X., Zhou, Y., Xu, X., & Ko, J. (2025) · Small · doi:10.1002/smll.202410975 · Cited by 16 · see citing works
Haro-Martínez, E., Muscolino, E., Moral, N., Durán, J., & Fornaguera, C. (2025) · Drug Delivery and Translational Research · doi:10.1007/s13346-025-01887-9 · Cited by 16 · see citing works
Protein Corona as a Result of Interaction of Protein Molecules with Inorganic Nanoparticles
Sarimov, R. M., Molkova, E. A., Simakin, A. V., Dorokhov, A. S., & Gudkov, S. V. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26199771 · Cited by 16 · see citing works
Nano and microparticle drug delivery systems for the treatment of Brucella infections
Razei, A., Javanbakht, M., Hajizade, A., Heiat, M., Zhao, S., Aghamollaei, H., Saadati, M., Khafaei, M., Asadi, M., Cegolon, L., et al. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115875 · Cited by 17 · see citing works
Ferroptosis driven by nanoparticles for tackling glioblastoma
Carlos, A., Mendes, M., Cruz, M. T., Pais, A. A. C. C., & Vitorino, C. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.217392 · Cited by 15 · see citing works
The mucosal protein corona in local nanoparticle drug delivery
Stern, A., Petersen, A. P., Zierden, H. C., & Duncan, G. A. (2025) · Cell Biomaterials · doi:10.1016/j.celbio.2025.100043 · Cited by 15 · see citing works
Guo, F., Lv, Q., Zhao, J., Wang, J., Chen, J., Yu, N., Hong, W., Lu, Y., & Yang, G. (2025) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2025.114969 · Cited by 15 · see citing works
Engineering in vivo behavior of DNA nanostructures toward organ-targeted drug delivery
Won, J., Cho, S., Kim, K., Kim, S., & Ahn, D. (2025) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2025.115682 · Cited by 15 · see citing works
Modern Strategies of Drug Therapy: Multi-Target Drug Delivery, Bioimaging, Diagnostics
Fedorova, O. V., Ovchinnikova, I. G., Rusinov, G. L., Avdeeva, V. V., Zhdanov, А. P., Zhizhin, K. Y., Kuznetsov, N. T., Zakharova, L. Y., Kuznetsova, D. A., Razuvayeva, Y. S., et al. (2025) · Russian Journal of General Chemistry · doi:10.1134/s1070363225606726 · Cited by 15 · see citing works
Hamilton, A. G., Thatte, A. S., Xu, J., Luo, Z., Safford, H. C., Swingle, K. L., Muscat-Rivera, J., Kegel, M., Han, X., Joseph, R. A., et al. (2026) · Advanced Materials · doi:10.1002/adma.202514370 · Cited by 16 · see citing works
Self-citationElsayed, N. (2024) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2024.124819 · Cited by 15 · see citing works
Kaumbekova, S., Sakaguchi, N., Shah, D., & Umezawa, M. (2024) · ACS Omega · doi:10.1021/acsomega.4c06409 · Cited by 15 · see citing works
Valizadeh, A., Mirzapoor, A., Hallaji, Z., Talab, M. J., & Ranjbar, B. (2025) · Materials Research Bulletin · doi:10.1016/j.materresbull.2025.113345 · Cited by 15 · see citing works
Basety, S., Gudepu, R., & Velidandi, A. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18020196 · Cited by 14 · see citing works
Unraveling the impact of nanopollution on plant metabolism and ecosystem dynamics
Vignesh, A., Amal, T. C., Ramamoorthy, S., Selvakumar, S., & Vasanth, K. (2024) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2024.108598 · Cited by 14 · see citing works
Xia, Q., Zhou, S., Zhou, J., Zhao, X., Saif, M. S., Wang, J. P., Hasan, M., Zhao, M., & Liu, Q. (2025) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.4c02118 · Cited by 15 · see citing works
Therapeutic Implications of Biomolecular Corona on Lipid Nanoparticle‐Based Gene Delivery Systems
Greco, A., & Corbo, C. (2025) · Small Science · doi:10.1002/smsc.202500206 · Cited by 13 · see citing works
Sterin, E. H., Weinstein, L. A., Tiwari, A., Kramarenko, G. C., Chowdhury, C. R., Li, K., & Day, E. S. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2507922122 · Cited by 13 · see citing works
Dai, W., Song, X., Zhao, H., He, W., Yin, J., & Nie, S. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.114302 · Cited by 13 · see citing works
Ming, T., Yang, Y., Zhu, J., Lin, J., Yang, W., Yu, G., Wang, P., Zhang, E., Chen, Q., & Liu, J. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s541948 · Cited by 13 · see citing works
Patel, T., Clipstone, C., Girija, U. V., Ahmad, Z., & Singh, N. (2025) · Nanomaterials · doi:10.3390/nano15231766 · Cited by 13 · see citing works
Lu, Y., Sun, Y., Zhang, D., He, Z., Sun, B., & Sun, J. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.114154 · Cited by 14 · see citing works
Chahar, D., Jha, I., Jayamani, A., & Venkatesu, P. (2024) · ACS Applied Bio Materials · doi:10.1021/acsabm.3c01052 · Cited by 12 · see citing works
Sikorski, J., Matczuk, M., Stępień, M., Ogórek, K., Ruzik, L., & Jarosz, M. (2024) · Nanotechnology · doi:10.1088/1361-6528/ad2c54 · Cited by 12 · see citing works
Ziani, I., Guerraf, A. E., Bentouhami, N. E., Brahmi, M., Bouakline, H., Bachiri, A. E., Fauconnier, M., Ansar, S., & Sher, F. (2024) · Biocatalysis and Agricultural Biotechnology · doi:10.1016/j.bcab.2024.103223 · Cited by 12 · see citing works
Shah, N., Soma, S. R., Quaye, M. B., Mahmoud, D., Ahmed, S., Malkoochi, A., & Obaid, G. (2024) · ACS Applied Bio Materials · doi:10.1021/acsabm.4c00316 · Cited by 12 · see citing works
Asil, S. M., & Narayan, M. (2024) · Nanoscale Advances · doi:10.1039/d4na00842a · Cited by 12 · see citing works
Detailed Profiling of Protein Corona Formed by Polydopamine Nanoparticles in Human Plasma
Battaglini, M., Carmignani, A., Ciobanu, D. Z., Marino, A., Catalano, F., Armirotti, A., & Ciofani, G. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.4c21207 · Cited by 12 · see citing works
Wang, X., Tian, Z., Wang, M., Cai, X., Yang, S., Zeng, J., Fang, Y., Bai, X., Wang, P., Sun, Y., et al. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06924-2 · Cited by 13 · see citing works
The Hybrid Nano-Biointerface between Proteins/Peptides and Two-Dimensional Nanomaterials
Forte, G., Mendola, D. L., & Satriano, C. (2023) · Molecules · doi:10.3390/molecules28207064 · Cited by 11 · see citing works
Zhang, M., Van, L. M., & Amiji, M. M. (2025) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2025.102686 · Cited by 11 · see citing works
Emerging nano-immunotherapeutic strategies achieve metastatic colorectal cancer precision therapy
Jiang, S., Zhang, Z., Mao, Y., Xia, X., Luo, J., Zhang, Y., & Yuan, Y. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03933-7 · Cited by 10 · see citing works
Adsorption of immunomodulatory proteins over silica nanoparticles and the in vitro effect
Giorgi, E. D., Genovés, S., Díaz, M. E., Municoy, S., Desimone, M. F., & Marzi, M. C. D. (2023) · Materials Advances · doi:10.1039/d3ma00776f · Cited by 10 · see citing works
Tabassum, H., Maity, A., Singh, K. K., Bagchi, D., Prasad, A., & Chakraborty, A. (2024) · Langmuir · doi:10.1021/acs.langmuir.4c00019 · Cited by 10 · see citing works
du Preez, H. N., Lin, J., Maguire, G. E. M., Aldous, C. M., & Kruger, H. G. (2024) · European Journal of Clinical Investigation · doi:10.1111/eci.14296 · Cited by 12 · see citing works
Biosensing solutions for protein measurement in blood-derived media: a review
Bartnik, K., Janik, M., Koba, M., Rygiel, T. P., Musolf, P., & Smietana, M. J. (2025) · Measurement · doi:10.1016/j.measurement.2025.117756 · Cited by 10 · see citing works
dos Reis, R. A., da Silva, L. L., Pieretti, J. C., Creusot, B., Lahouari, S., Francius, G., Silva, R. A. G., Clarot, I., Boudier, A., & Seabra, A. B. (2025) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-025-03178-6 · Cited by 10 · see citing works
Controlling nanoparticle-induced endothelial leakiness with the protein corona
Nandakumar, A., Tang, H., Andrikopoulos, N., Quinn, J. F., Ding, F., Ke, P. C., & Li, Y. (2024) · Nanoscale · doi:10.1039/d4nr01311e · Cited by 9 · see citing works
Okonkwo, T. P., Amienghemhen, O. D., Nkwor, A. N., & Ifijen, I. H. (2024) · Nano-Structures & Nano-Objects · doi:10.1016/j.nanoso.2024.101370 · Cited by 9 · see citing works
Enhancing magnetic hyperthermia: Investigating iron oxide nanoparticle coating and stability
Santos, J., Silva, J. A. M. D. C., Valente, M. A., Vieira, T., & Soares, P. I. P. (2025) · Next Nanotechnology · doi:10.1016/j.nxnano.2025.100141 · Cited by 9 · see citing works
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Jiménez-Boland, D., Robles-Fernández, A., Martín-Rodríguez, A., Cuadros, M. Á., Traverso, J. A., Sánchez-Moreno, P., & Bramini, M. (2025) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5c07306 · Cited by 9 · see citing works
Płuciennik, K., Szabelski, M., Miłowska, K., Ciepluch, K., Duchnowicz, P., Krokosz, A., Sicińska, P., & Bukowska, B. (2025) · Scientific Reports · doi:10.1038/s41598-025-15422-w · Cited by 9 · see citing works
Cavalieri, G., Marson, D., Giurgevich, N., Valeri, R., Felluga, F., Laurini, E., & Pricl, S. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16040533 · Cited by 9 · see citing works
Chen, J., Lin, H., Cao, L., Sui, J., Wang, X., & Wang, K. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.144474 · Cited by 9 · see citing works
Self-citationUnlocking Transplant Tolerance with Biomaterials
Pham, J. A., & Coronel, M. M. (2024) · Advanced Healthcare Materials · doi:10.1002/adhm.202400965 · Cited by 8 · see citing works
- Authors
- Bashiri, G., Padilla, M. S., Swingle, K. L., Shepherd, S. J., Mitchell, M. J., & Wang, K.
- Affiliations
- Temple University (US)
- University of Pennsylvania (US)
- Abramson Cancer Center (US)
- Corresponding author
- Wang, Karin
- Venue
- Lab on a Chip
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2023
- Volume
- 23
- Issue
- 6
- Pages
- 1432-1466
- ISSN
- 1473-0189 (ISSN-L)
- 1473-0197
- PMC
- PMC10013352
- OpenAlex
- W4317434639
- Cited by
- 296
- References
- 266
- Citations by year
- 2026: 108 · 2025: 103 · 2024: 71 · 2023: 14
- FWCI
- 5.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Lab on a Chip (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Science Foundation (CBET-2145491, 1845298)
- NIH Office of the Director (DP2 TR002776)
- National Institutes of Health (NCI R01 CA241661, NCI R37 CA244911, NIDDK R01 DK123049)
- Burroughs Wellcome Fund (Career Award at the Scientific Interface)
- National Institute of Dental and Craniofacial Research (T90DE030854)
- Temple University (Startup Funds, Teaching Assistantship)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Nanoparticle-Based Drug Delivery
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Keywords
- protein corona, protein adsorption, protein conformation, protein orientation, nanoparticle surface properties, therapeutic targeting, immunomodulation, biomedical nanoparticles
- MeSH terms
- Protein Corona, Biological Factors, Protein Conformation, Proteins, Nanoparticles
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