The DOI matches its Crossref record; 533 of the 533 references it cites were found in a registry or an index.
Multicomponent peptide assemblies
Open accessAbstract
This review presents recent efforts in the development of multicomponent supramolecular peptide assemblies with a focus on multicomponent assemblies derived from β-sheet peptides, low molecular weight peptides, peptide amphiphiles, coiled coil peptides, collagen, and related systems.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Items 201–400 of 533
Peptides for nucleic acid delivery
Lehto, T., Ezzat, K., Wood, M. J. A., & EL Andaloussi, S. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2016.06.008 · Cited by 220
A Review of Injectable Polymeric Hydrogel Systems for Application in Bone Tissue Engineering
Kondiah, P., Choonara, Y., Kondiah, P., Marimuthu, T., Kumar, P., Du Toit, L., & Pillay, V. (2016) · Molecules · doi:10.3390/molecules21111580 · Cited by 219
Tunable Supramolecular Hydrogels for Selection of Lineage-Guiding Metabolites in Stem Cell Cultures
Alakpa, E. V., Jayawarna, V., Lampel, A., Burgess, K. V., West, C. C., Bakker, S. C. J., Roy, S., Javid, N., Fleming, S., Lamprou, D. A., et al. (2016) · Chem · doi:10.1016/j.chempr.2016.07.001 · Cited by 215
Cell-penetrating Peptides as Versatile Vehicles for Oligonucleotide Delivery
Margus, H., Padari, K., & Pooga, M. (2012) · Molecular Therapy · doi:10.1038/mt.2011.284 · Cited by 214
Role of Water in Directing Diphenylalanine Assembly into Nanotubes and Nanowires
Kim, J., Han, T. H., Kim, Y., Park, J. S., Choi, J., Churchill, D. G., Kim, S. O., & Ihee, H. (2010) · Advanced Materials · doi:10.1002/adma.200901973 · Cited by 213
Enhanced Mechanical Rigidity of Hydrogels Formed from Enantiomeric Peptide Assemblies
Nagy, K. J., Giano, M. C., Jin, A., Pochan, D. J., & Schneider, J. P. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206742m · Cited by 211
Self-Assembly and Biomaterials
Stupp, S. I. (2010) · Nano Letters · doi:10.1021/nl103567y · Cited by 210
Liu, K., Yuan, C., Zou, Q., Xie, Z., & Yan, X. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201704678 · Cited by 209
Aligned neurite outgrowth and directed cell migration in self-assembled monodomain gels
Berns, E. J., Sur, S., Pan, L., Goldberger, J. E., Suresh, S., Zhang, S., Kessler, J. A., & Stupp, S. I. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2013.09.077 · Cited by 208
Bowerman, C. J., Liyanage, W., Federation, A. J., & Nilsson, B. L. (2011) · Biomacromolecules · doi:10.1021/bm200510k · Cited by 207
Self-citationA Periodic Table of Coiled-Coil Protein Structures
Moutevelis, E., & Woolfson, D. N. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.028 · Cited by 204
Kim, S., Kim, J. H., Lee, J. S., & Park, C. B. (2015) · Small · doi:10.1002/smll.201500169 · Cited by 204
Reches, M., & Gazit, E. (2006) · Physical Biology · doi:10.1088/1478-3975/3/1/s02 · Cited by 202
Preparation of Nanostructures by Orthogonal Self‐Assembly of Hydrogelators and Surfactants
Brizard, A., Stuart, M., van Bommel, K., Friggeri, A., de Jong, M., & van Esch, J. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200704609 · Cited by 200
Functional peptides for siRNA delivery
Tai, W., & Gao, X. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2016.08.004 · Cited by 197
Synthetic collagen mimics: self-assembly of homotrimers, heterotrimers and higher order structures
Fallas, J. A., O'Leary, L. E. R., & Hartgerink, J. D. (2010) · Chemical Society Reviews · doi:10.1039/b919455j · Cited by 195
Panda, J. J., & Chauhan, V. S. (2014) · Polym. Chem. · doi:10.1039/c4py00173g · Cited by 195
Self-assembly of bioactive peptides, peptide conjugates, and peptide mimetic materials
Edwards-Gayle, C. J. C., & Hamley, I. W. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob01092c · Cited by 195
Ryan, D. M., Anderson, S. B., & Nilsson, B. L. (2010) · Soft Matter · doi:10.1039/c0sm00018c · Cited by 194
Self-citationAbedini, A., & Raleigh, D. P. (2009) · Protein Engineering Design and Selection · doi:10.1093/protein/gzp036 · Cited by 192
Structure–mechanical property correlations of hydrogel forming β-sheet peptides
De Leon Rodriguez, L. M., Hemar, Y., Cornish, J., & Brimble, M. A. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00941c · Cited by 192
Drug Carriers for the Delivery of Therapeutic Peptides
Du, A. W., & Stenzel, M. H. (2014) · Biomacromolecules · doi:10.1021/bm500169p · Cited by 190
Fradinger, E. A., Monien, B. H., Urbanc, B., Lomakin, A., Tan, M., Li, H., Spring, S. M., Condron, M. M., Cruz, L., Xie, C.-W., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807163105 · Cited by 186
Dipeptide and Tripeptide Conjugates as Low‐Molecular‐Weight Hydrogelators
Adams, D. J. (2011) · Macromolecular Bioscience · doi:10.1002/mabi.201000316 · Cited by 185
Trace Solvent as a Predominant Factor To Tune Dipeptide Self-Assembly
Wang, J., Liu, K., Yan, L., Wang, A., Bai, S., & Yan, X. (2016) · ACS Nano · doi:10.1021/acsnano.5b06567 · Cited by 185
Self-assembled peptide nanofibers raising durable antibody responses against a malaria epitope
Rudra, J. S., Mishra, S., Chong, A. S., Mitchell, R. A., Nardin, E. H., Nussenzweig, V., & Collier, J. H. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.05.041 · Cited by 176
Shay, J. W. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.12.001 · Cited by 174
Self-Assembly of α-Helical Coiled Coil Nanofibers
Dong, H., Paramonov, S. E., & Hartgerink, J. D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8037323 · Cited by 174
Multifunctional Porous Microspheres Based on Peptide–Porphyrin Hierarchical Co‐Assembly
Zou, Q., Zhang, L., Yan, X., Wang, A., Ma, G., Li, J., Möhwald, H., & Mann, S. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308792 · Cited by 173
Self-Assembled Injectable Peptide Hydrogels Capable of Triggering Antitumor Immune Response
Xing, R., Li, S., Zhang, N., Shen, G., Möhwald, H., & Yan, X. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00787 · Cited by 173
Liu, K., Xing, R., Li, Y., Zou, Q., Möhwald, H., & Yan, X. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201606795 · Cited by 172
Panda, J. J., Mishra, A., Basu, A., & Chauhan, V. S. (2008) · Biomacromolecules · doi:10.1021/bm800404z · Cited by 168
Short to ultrashort peptide hydrogels for biomedical uses
Seow, W. Y., & Hauser, C. A. E. (2014) · Materials Today · doi:10.1016/j.mattod.2014.04.028 · Cited by 166
Yuan, H., Luo, K., Lai, Y., Pu, Y., He, B., Wang, G., Wu, Y., & Gu, Z. (2010) · Molecular Pharmaceutics · doi:10.1021/mp1000923 · Cited by 166
Self-Assembled Heterotrimeric Collagen Triple Helices Directed through Electrostatic Interactions
Gauba, V., & Hartgerink, J. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0683640 · Cited by 166
Protein aggregation: From background to inhibition strategies
Alam, P., Siddiqi, K., Chturvedi, S. K., & Khan, R. H. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.05.048 · Cited by 166
Bioenergetics and Life’s Origins
Deamer, D., & Weber, A. L. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004929 · Cited by 165
Nanda, J., Biswas, A., & Banerjee, A. (2013) · Soft Matter · doi:10.1039/c3sm27050e · Cited by 165
Biomedical Applications of Self-Assembling Peptides
Rad-Malekshahi, M., Lempsink, L., Amidi, M., Hennink, W. E., & Mastrobattista, E. (2016) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5b00487 · Cited by 165
Yan, X., Cui, Y., He, Q., Wang, K., Li, J., Mu, W., Wang, B., & Ou‐yang, Z. (2008) · Chemistry – A European Journal · doi:10.1002/chem.200800012 · Cited by 163
Amyloidogenesis of Tau protein
Nizynski, B., Dzwolak, W., & Nieznanski, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 162
Jeong, J. H., Kim, S. W., & Park, T. G. (2003) · Bioconjugate Chemistry · doi:10.1021/bc025632k · Cited by 161
The Phe-Phe Motif for Peptide Self-Assembly in Nanomedicine
Marchesan, S., Vargiu, A., & Styan, K. (2015) · Molecules · doi:10.3390/molecules201119658 · Cited by 161
Zhang, N., Zhao, F., Zou, Q., Li, Y., Ma, G., & Yan, X. (2016) · Small · doi:10.1002/smll.201602339 · Cited by 161
Hodges, J. A., & Raines, R. T. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054674r · Cited by 160
Biomimetic Nanocarrier for Direct Cytosolic Drug Delivery
Zhang, Z., Cao, W., Jin, H., Lovell, J. F., Yang, M., Ding, L., Chen, J., Corbin, I., Luo, Q., & Zheng, G. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200903112 · Cited by 158
Synaptic memory mechanisms: Alzheimer's disease amyloid β-peptide-induced dysfunction
Rowan, M. J., Klyubin, I. V., Wang, Q., Hu, N., & Anwyl, R. (2007) · Biochemical Society Transactions · doi:10.1042/bst0351219 · Cited by 155
Fluorous Biphase Systems—The New Phase‐Separation and Immobilization Technique
Cornils, B. (1997) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199720571 · Cited by 154
Self‐Assembled Proteins and Peptides as Scaffolds for Tissue Regeneration
Loo, Y., Goktas, M., Tekinay, A. B., Guler, M. O., Hauser, C. A. E., & Mitraki, A. (2015) · Advanced Healthcare Materials · doi:10.1002/adhm.201500402 · Cited by 153
Structurally Defined Nanoscale Sheets from Self-Assembly of Collagen-Mimetic Peptides
Jiang, T., Xu, C., Liu, Y., Liu, Z., Wall, J. S., Zuo, X., Lian, T. T., Salaita, K. S., Ni, C., Pochan, D. J., et al. (2014) · Journal of the American Chemical Society · doi:10.1021/ja412867z · Cited by 153
Coiled-Coil Design: Updated and Upgraded
Woolfson, D. N. (2017) · Subcellular Biochemistry · doi:10.1007/978-3-319-49674-0_2 · Cited by 149
Chirality effects at each amino acid position on tripeptide self-assembly into hydrogel biomaterials
Marchesan, S., Easton, C. D., Styan, K. E., Waddington, L. J., Kushkaki, F., Goodall, L., McLean, K. M., Forsythe, J. S., & Hartley, P. G. (2014) · Nanoscale · doi:10.1039/c3nr06752a · Cited by 149
Protein misfolding and aggregation: Mechanism, factors and detection
Chaturvedi, S. K., Siddiqi, M. K., Alam, P., & Khan, R. H. (2016) · Process Biochemistry · doi:10.1016/j.procbio.2016.05.015 · Cited by 149
Nagy-Smith, K. J., Beltramo, P. J., Moore, E. W., Tycko, R., Furst, E. M., & Schneider, J. P. (2017) · ACS Central Science · doi:10.1021/acscentsci.7b00115 · Cited by 149
Hyaluronic acid‐based nanocomposite hydrogels for ocular drug delivery applications
Widjaja, L. K., Bora, M., Chan, P. N. P. H., Lipik, V. T., Wong, T. T. L., & Venkatraman, S. S. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34976 · Cited by 148
Stabilization of the Collagen Triple Helix byO-Methylation of Hydroxyproline Residues
Kotch, F. W., Guzei, I. A., & Raines, R. T. (2008) · Journal of the American Chemical Society · doi:10.1021/ja800225k · Cited by 147
pH-Responsive Bioactive Glycopolypeptides with Enhanced Helicity and Solubility in Aqueous Solution
Krannig, K.-S., & Schlaad, H. (2012) · Journal of the American Chemical Society · doi:10.1021/ja308772d · Cited by 144
Ranieri, J. P., Bellamkonda, R., Bekos, E. J., Vargo, T. G., Gardella, J. A. J., & Aebischer, P. (1995) · Journal of Biomedical Materials Research · doi:10.1002/jbm.820290614 · Cited by 144
Switching the Immunogenicity of Peptide Assemblies Using Surface Properties
Wen, Y., Waltman, A., Han, H., & Collier, J. H. (2016) · ACS Nano · doi:10.1021/acsnano.6b03409 · Cited by 143
Kim, Y., Lee, Y., Choe, J., Lee, H., Kim, Y., & Jeoung, D. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708319200 · Cited by 142
Wang, H., & Yang, Z. (2012) · Nanoscale · doi:10.1039/c2nr31149f · Cited by 142
β1 integrins and osteoclast function: Involvement in collagen recognition and bone resorption
Helfrich, M. H., Nesbitt, S. A., Lakkakorpi, P. T., Barnes, M. J., Bodary, S. C., Shankar, G., Mason, W. T., Mendrick, D. L., Väänänen, H. K., & Horton, M. A. (1996) · Bone · doi:10.1016/s8756-3282(96)00223-2 · Cited by 139
Sieminski, A. L., Semino, C. E., Gong, H., & Kamm, R. D. (2008) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.31785 · Cited by 139
Prati, F., Bottegoni, G., Bolognesi, M. L., & Cavalli, A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00393 · Cited by 139
Overview of Extracellular Matrix
Mecham, R. P. (1998) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb1001s00 · Cited by 138
Self-Assembling Peptide Nanofibrous Hydrogel as a Versatile Drug Delivery Platform
Yu, Z., Xu, Q., Dong, C., Lee, S. S., Gao, L., Li, Y., D'Ortenzio, M., & Wu, J. (2015) · Current Pharmaceutical Design · doi:10.2174/1381612821666150901104821 · Cited by 137
pH‐Switchable Ampholytic Supramolecular Copolymers
Frisch, H., Unsleber, J. P., Lüdeker, D., Peterlechner, M., Brunklaus, G., Waller, M. P., & Besenius, P. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201303810 · Cited by 136
Harnessing self-assembled peptide nanoparticles in epitope vaccine design
Negahdaripour, M., Golkar, N., Hajighahramani, N., Kianpour, S., Nezafat, N., & Ghasemi, Y. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.05.002 · Cited by 136
Poly(glutamic Acid) for Biomedical Applications
Richard, A., & Margaritis, A. (2001) · Critical Reviews in Biotechnology · doi:10.1080/07388550108984171 · Cited by 135
Peptide-based hydrogel nanoparticles as effective drug delivery agents
Ischakov, R., Adler‐Abramovich, L., Buzhansky, L., Shekhter, T., & Gazit, E. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.03.012 · Cited by 135
Peptidic Biomaterials: From Self-Assembling to Regenerative Medicine
Pugliese, R., & Gelain, F. (2017) · Trends in Biotechnology · doi:10.1016/j.tibtech.2016.09.004 · Cited by 133
Chang, S., Shefelbine, S. J., & Buehler, M. J. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.11.3999 · Cited by 131
Tyrosine-mediated two-dimensional peptide assembly and its role as a bio-inspired catalytic scaffold
Jang, H., Lee, J., Park, Y.-S., Kim, Y., Park, J., Yang, T., Jin, K., Lee, J., Park, S., You, J. M., et al. (2014) · Nature Communications · doi:10.1038/ncomms4665 · Cited by 131
Huang, C., Jin, H., Qian, Y., Qi, S., Luo, H., Luo, Q., & Zhang, Z. (2013) · ACS Nano · doi:10.1021/nn400683s · Cited by 131
Amyloid structure and assembly: Insights from scanning transmission electron microscopy
Goldsbury, C. S., Baxa, U., Simon, M. N., Steven, A. C., Engel, A. H., Wall, J. S., Aebi, U., & Müller, S. A. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.09.018 · Cited by 128
Hirakura, T., Yasugi, K., Nemoto, T., Sato, M., Shimoboji, T., Aso, Y., Morimoto, N., & Akiyoshi, K. (2009) · Journal of Controlled Release · doi:10.1016/j.jconrel.2009.11.023 · Cited by 128
Colquhoun, C., Draper, E. R., Eden, E. G. B., Cattoz, B., Morris, K. L., Chen, L., McDonald, T. O., Terry, A. E., Griffiths, P. C., Serpell, L. C., et al. (2014) · Nanoscale · doi:10.1039/c4nr04039b · Cited by 125
Koga, T., Matsuoka, M., & Higashi, N. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0558387 · Cited by 125
Biomimetic Self-Assembling Peptides as Scaffolds for Soft Tissue Engineering
Maude, S., Ingham, E., & Aggeli, A. (2013) · Nanomedicine · doi:10.2217/nnm.13.65 · Cited by 124
Connexin43 in retinal injury and disease
Danesh-Meyer, H. V., Zhang, J., Acosta, M. L., Rupenthal, I. D., & Green, C. R. (2015) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2015.09.004 · Cited by 124
Targeting the Prion-like Aggregation of Mutant p53 to Combat Cancer
Silva, J. L., Cino, E. A., Soares, I. N., Ferreira, V. F., & de Oliveira, G. A. P. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00473 · Cited by 121
Wang, X., Horii, A., & Zhang, S. (2008) · Soft Matter · doi:10.1039/b807155a · Cited by 120
Das, T., Häring, M., Haldar, D., & Díaz, D. D. (2017) · Biomaterials Science · doi:10.1039/c7bm00882a · Cited by 120
Jung, J. P., Moyano, J. V., & Collier, J. H. (2011) · Integrative Biology · doi:10.1039/c0ib00112k · Cited by 119
Ardoña, H. A. M., Draper, E. R., Citossi, F., Wallace, M., Serpell, L. C., Adams, D. J., & Tovar, J. D. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04006 · Cited by 119
Self-Assembly of Fiber-Forming Collagen Mimetic Peptides Controlled by Triple-Helical Nucleation
Sarkar, B., O’Leary, L. E. R., & Hartgerink, J. D. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504377s · Cited by 117
Charged Diphenylalanine Nanotubes and Controlled Hierarchical Self-Assembly
Wang, M., Du, L., Wu, X., Xiong, S., & Chu, P. K.-H. (2011) · ACS Nano · doi:10.1021/nn2016524 · Cited by 117
Controlling the Physical Dimensions of Peptide Nanotubes by Supramolecular Polymer Coassembly
Adler‐Abramovich, L., Marco, P., Arnon, Z. A., Creasey, R. C. G., Michaels, T. C. T., Levin, A., Scurr, D. J., Roberts, C. J., Knowles, T. P. J., Tendler, S. J. B., et al. (2016) · ACS Nano · doi:10.1021/acsnano.6b01587 · Cited by 115
Ruan, L., Zhang, H., Luo, H., Liu, J., Tang, F., Shi, Y., & Zhao, X. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900026106 · Cited by 114
Supramolecular structure of helical ribbons self-assembled from a β-sheet peptide
Hwang, W., Marini, D. M., Kamm, R. D., & Zhang, S. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1524618 · Cited by 113
Lemkul, J. A., & Bevan, D. R. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300091a · Cited by 113
Cell-penetrating peptides (CPPs) as a vector for the delivery of siRNAs into cells
Nakase, I., Tanaka, G., & Futaki, S. (2012) · Molecular BioSystems · doi:10.1039/c2mb25467k · Cited by 113
Enzyme‐instructed self‐assembly of peptide derivatives to form nanofibers and hydrogels
Gao, Y., Yang, Z., Kuang, Y., Ma, M., Li, J., Zhao, F., & Xu, B. (2010) · Biopolymers · doi:10.1002/bip.21321 · Cited by 112
Direct Observation of Nucleation and Growth in Amyloid Self-Assembly
Liang, Y., Lynn, D. G., & Berland, K. M. (2010) · Journal of the American Chemical Society · doi:10.1021/ja910964c · Cited by 112
Liu, X., Wang, X., Horii, A., Wang, X., Qiao, L., Zhang, S., & Cui, F. (2012) · Nanoscale · doi:10.1039/c2nr00001f · Cited by 111
A Genetically Engineered Protein Responsive to Multiple Stimuli
Dutta, N. K., Truong, M. Y., Mayavan, S., et al. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201007920 · Cited by 111
Biomaterials for Tissue Engineering Applications: A Review of the Past and Future Trends
Burdick, J. A., & Mauck, R. L. (2010) · Springer eBooks · doi:10.1007/978-3-7091-0385-2 · Cited by 110
Magnetic Deformation of Self-Assembled Sexithiophene Spherical Nanocapsules
Shklyarevskiy, I. O., Jonkheijm, P., Christianen, P. C. M., Schenning, A. P. H. J., Meijer, E. W., Henze, O., Kilbinger, A. F. M., Feast, W. J., Guerzo, A. D., Desvergne, J., et al. (2005) · Journal of the American Chemical Society · doi:10.1021/ja0431096 · Cited by 107
Guo, C., Arnon, Z. A., Qi, R., Zhang, Q., Adler‐Abramovich, L., Gazit, E., & Wei, G. (2016) · ACS Nano · doi:10.1021/acsnano.6b02739 · Cited by 106
Cell‐Penetrating‐Peptide‐Coated Nanoribbons for Intracellular Nanocarriers
Lim, Y., Lee, E. J., & Lee, M. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604576 · Cited by 105
Hyaluronic Acid Coated Albumin Nanoparticles for Targeted Peptide Delivery to the Retina
Huang, D., Chen, Y.-S., & Rupenthal, I. D. (2016) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.6b01029 · Cited by 104
Comparison of Cationic and Amphipathic Cell Penetrating Peptides for siRNA Delivery and Efficacy
Mo, R. H., Zaro, J. L., & Shen, W. (2011) · Molecular Pharmaceutics · doi:10.1021/mp200481g · Cited by 103
Surprisingly High Stability of Collagen ABC Heterotrimer: Evaluation of Side Chain Charge Pairs
Gauba, V., & Hartgerink, J. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja075854z · Cited by 103
Dutta, S., Foley, A. R., Warner, C. J. A., Zhang, X., Rolandi, M., Abrams, B. S., & Raskatov, J. A. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201706279 · Cited by 103
A Self‐Adjuvanting Supramolecular Vaccine Carrying a Folded Protein Antigen
Hudalla, G. A., Modica, J. A., Tian, Y. F., Rudra, J. S., Chong, A. S., Sun, T., Mrksich, M., & Collier, J. H. (2013) · Advanced Healthcare Materials · doi:10.1002/adhm.201200435 · Cited by 102
Marchesan, S., Styan, K. E., Easton, C. D., Waddington, L. J., & Vargiu, A. V. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb00858a · Cited by 101
Inhibition of Amyloid-β Aggregation in Alzheimer's Disease
Wang, Q., Yu, X., Li, L., & Zheng, J. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113199990068 · Cited by 101
Halperin‐Sternfeld, M., Ghosh, M., Sevostianov, R., Grigoriants, I., & Adler‐Abramovich, L. (2017) · Chemical Communications · doi:10.1039/c7cc04187j · Cited by 101
Toft, D. J., Moyer, T. J., Standley, S. M., Ruff, Y., Ugolkov, A. V., Stupp, S. I., & Cryns, V. L. (2012) · ACS Nano · doi:10.1021/nn302503s · Cited by 100
Cai, C., Li, Y., Lin, J., Wang, L., Lin, S., Wang, X., & Jiang, T. (2013) · Angewandte Chemie International Edition · doi:10.1002/anie.201210024 · Cited by 100
Structural Aspects of Porphyrins for Functional Materials Applications
Cook, L. P., Brewer, G. A., & Wong-Ng, W. (2017) · Crystals · doi:10.3390/cryst7070223 · Cited by 100
Single amino acid based self-assembled structure
Perween, S., Chandanshive, B., Kotamarthi, H. C., & Khushalani, D. (2013) · Soft Matter · doi:10.1039/c3sm51054a · Cited by 99
Yu, Z., Erbaş, A., Tantakitti, F., Palmer, L. C., Jackman, J. A., de la Cruz, M. O., Cho, N., & Stupp, S. I. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02058 · Cited by 99
Fallas, J. A., Gauba, V., & Hartgerink, J. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014753 · Cited by 96
Engineering β-sheet peptide assemblies for biomedical applications
Yu, Z., Cai, Z., Chen, Q., Liu, M., Ye, L., Ren, J., Liao, W., & Liu, S. (2015) · Biomaterials Science · doi:10.1039/c5bm00472a · Cited by 96
Rationally Designed Peptidomimetic Modulators of Aβ Toxicity in Alzheimer's Disease
Rajasekhar, K., Suresh, S., Manjithaya, R. R., & Govindaraju, T. (2015) · Scientific Reports · doi:10.1038/srep08139 · Cited by 95
New generation of efficient peptide-based vectors, NickFects, for the delivery of nucleic acids
Arukuusk, P., Pärnaste, L., Oskolkov, N., Copolovici, D. M., Margus, H., Padari, K., Möll, K., Maslovskaja, J., Tegova, R., Kivi, G., et al. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.01.011 · Cited by 93
Protein astrogliopathies in human neurodegenerative diseases and aging
Kovács, G. G., Lee, V. M., & Trojanowski, J. Q. (2017) · Brain Pathology · doi:10.1111/bpa.12536 · Cited by 93
Filamentous Artificial Virus from a Self‐Assembled Discrete Nanoribbon
Lim, Y., Lee, E. J., Yoon, Y., Lee, M. S., & Lee, M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200800266 · Cited by 92
Cooperative Self-Assembly of Peptide Gelators and Proteins
Javid, N., Roy, S., Zelzer, M., Yang, Z., Šefčík, J., & Ulijn, R. V. (2013) · Biomacromolecules · doi:10.1021/bm401319c · Cited by 92
Directed Stem Cell Differentiation: The Role of Physical Forces
Clause, K. C., Liu, L., & Tobita, K. (2010) · Cell Communication & Adhesion · doi:10.3109/15419061.2010.492535 · Cited by 92
Retaining Antibodies in Tumors with a Self-Assembling Injectable System
Wen, Y., Kolonich, H. R., Kruszewski, K. M., Giannoukakis, N., Gawalt, E. S., & Meng, W. S. (2013) · Molecular Pharmaceutics · doi:10.1021/mp300504z · Cited by 92
Ghosh, M., Halperin‐Sternfeld, M., Grigoriants, I., Lee, J., Nam, K. T., & Adler‐Abramovich, L. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00876 · Cited by 92
Synthetic Collagen Heterotrimers: Structural Mimics of Wild-Type and Mutant Collagen Type I
Gauba, V., & Hartgerink, J. D. (2008) · Journal of the American Chemical Society · doi:10.1021/ja801670v · Cited by 91
Mechanical Control of Stem Cell Differentiation
Rosenfeld, D., Sagi, M., Levenberg, S., & Zemel, A. (2011) · Regenerative Medicine · doi:10.2217/rme.11.99 · Cited by 90
Design of Asymmetric Peptide Bilayer Membranes
Li, S., Mehta, A. K., Sidorov, A., Orlando, T. M., Jiang, Z., Anthony, N. R., & Lynn, D. G. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b00977 · Cited by 90
Mechanical Properties of Self-Assembled Fmoc-Diphenylalanine Molecular Gels
Dudukovic, N. A., & Zukoski, C. F. (2014) · Langmuir · doi:10.1021/la500589f · Cited by 90
Di Domenico, F., Tramutola, A., Foppoli, C., Head, E., Perluigi, M., & Butterfield, D. A. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.009 · Cited by 89
Current preclinical small interfering RNA (siRNA)-based conjugate systems for RNA therapeutics
Hyeon, L. S., Kang, Y. Y., Jang, H.-E., & Mok, H. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.10.009 · Cited by 89
Multivalent RGD synthetic peptides as potent α V β 3 integrin ligands
Garanger, É., Boturyn, D., Coll, J., Favrot, M., & Dumy, P. (2006) · Organic & Biomolecular Chemistry · doi:10.1039/b517706e · Cited by 89
Supramolecular Nanofibers of Peptide Amphiphiles for Medicine
Webber, M. J., Berns, E. J., & Stupp, S. I. (2013) · Israel Journal of Chemistry · doi:10.1002/ijch.201300046 · Cited by 89
Charalambidis, G., Georgilis, E., Panda, M. K., Anson, C. E., Powell, A. K., Doyle, S., Moss, D., Jochum, T., Horton, P. N., Coles, S. J., et al. (2016) · Nature Communications · doi:10.1038/ncomms12657 · Cited by 89
Fairman, R., Chao, H.-G., Lavoie, T., Villafranca, J. J., Matsueda, G. R., & Novotný, J. (1996) · Biochemistry · doi:10.1021/bi952784c · Cited by 88
Spencer, R. K., Li, H., & Nowick, J. S. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5017409 · Cited by 88
Cooperative, ion-sensitive co-assembly of tripeptide hydrogels
Abul‐Haija, Y. M., Scott, G. G., Sahoo, J. K., Tuttle, T., & Ulijn, R. V. (2017) · Chemical Communications · doi:10.1039/c7cc04796g · Cited by 87
Sanders, A. M., Magnanelli, T. J., Bragg, A. E., & Tovar, J. D. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b12001 · Cited by 86
Electrospinning of Diphenylalanine Nanotubes
Singh, G., Bittner, A. M., Loscher, S., Malinowski, N., & Kern, K. (2008) · Advanced Materials · doi:10.1002/adma.200702802 · Cited by 85
Qin, L., Nie, Xiaoguang, et al. (2011) · 中国药理学报:英文版 · Cited by 85
Cell-penetrating peptide-conjugated lipid nanoparticles for siRNA delivery
Asai, T., Tsuzuku, T., Takahashi, S., Okamoto, A., Dewa, T., Nango, M., Hyodo, K., Ishihara, H., Kikuchi, H., & Oku, N. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.107 · Cited by 84
β-Sheet interfering molecules acting against β-amyloid aggregation and fibrillogenesis
Francioso, A., Punzi, P., Boffi, A., Lori, C., Martire, S., Giordano, C., D’Erme, M., & Mosca, L. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.02.041 · Cited by 84
Mimicking Biosilicification: Programmed Coassembly of Peptide–Polymer Nanotapes and Silica
Kessel, S., Thomas, A., & Börner, H. G. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200703752 · Cited by 84
Amphiphilic Peptide Self-Assembly: Expansion to Hybrid Materials
Mikhalevich, V., Craciun, I., Kyropoulou, M., Palivan, C. G., & Meier, W. P. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00764 · Cited by 84
Cai, C., Lin, J., Chen, T., Wang, X., & Lin, S. (2009) · Chemical Communications · doi:10.1039/b823367e · Cited by 83
Shive, M. S., Salloum, M. L., & Anderson, J. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110463197 · Cited by 83
Tissue-Factor Targeted Peptide Amphiphile Nanofibers as an Injectable Therapy To Control Hemorrhage
Morgan, C. E., Dombrowski, A. W., Pérez, C. M. R., Bahnson, E. M., Tsihlis, N. D., Jiang, W., Jiang, Q., Vercammen, J. M., Prakash, V. S., Pritts, T. A., et al. (2015) · ACS Nano · doi:10.1021/acsnano.5b06025 · Cited by 83
Design of Polyelectrolyte Multilayers to Promote Immunological Tolerance
Tostanoski, L. H., Chiu, Y.-C., Andorko, J. I., Guo, M., Zeng, X., Zhang, P., Royal, W., & Jewell, C. M. (2016) · ACS Nano · doi:10.1021/acsnano.6b04001 · Cited by 80
Wang, C. S., & Stewart, R. J. (2011) · Journal of Experimental Biology · doi:10.1242/jeb.065011 · Cited by 78
Resilin-Based Materials for Biomedical Applications
Li, L., & Kiick, K. L. (2013) · ACS Macro Letters · doi:10.1021/mz4002194 · Cited by 76
Chen, C., Liu, K., Li, J., & Yan, X. (2015) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2015.09.001 · Cited by 76
Liyanage, W., Vats, K., Rajbhandary, A., Benoit, D. S. W., & Nilsson, B. L. (2015) · Chemical Communications · doi:10.1039/c5cc03162a · Cited by 75
Self-citationLim, Y., Park, S., Lee, E. J., Jeong, H., Ryu, J., Lee, M. S., & Lee, M. (2007) · Biomacromolecules · doi:10.1021/bm0700901 · Cited by 75
Self-assembling peptide-based delivery of therapeutics for myocardial infarction
French, K. M., Somasuntharam, I., & Davis, M. E. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.04.023 · Cited by 74
The application of self-assembled nanostructures in peptide-based subunit vaccine development
Zhao, G., Chandrudu, S., Skwarczyński, M., & Tóth, I. (2017) · European Polymer Journal · doi:10.1016/j.eurpolymj.2017.02.014 · Cited by 74
A retro-inverso cell-penetrating peptide for siRNA delivery
Vaissière, A., Aldrian, G., Konate, K., Lindberg, M. F., Jourdan, C., Telmar, A., Seisel, Q., Fernandez, F., Viguier, V., Genevois, C., et al. (2017) · Journal of Nanobiotechnology · doi:10.1186/s12951-017-0269-2 · Cited by 74
Low molecular weight gelator–dextran composites
Chen, L., Revel, S., Morris, K. L., Spiller, D. G., Serpell, L. C., & Adams, D. J. (2010) · Chemical Communications · doi:10.1039/c0cc01842b · Cited by 73
Swanekamp, R. J., Welch, J. J., & Nilsson, B. L. (2014) · Chemical Communications · doi:10.1039/c4cc04644g · Cited by 73
Self-citationFrom Pathways to Targets: Understanding the Mechanisms behind Polyglutamine Disease
Weber, J. J., Sowa, A. S., Binder, T., & Hübener‐Schmid, J. (2014) · BioMed Research International · doi:10.1155/2014/701758 · Cited by 73
Directed Intermixing in Multicomponent Self-Assembling Biomaterials
Gasiorowski, J. Z., & Collier, J. H. (2011) · Biomacromolecules · doi:10.1021/bm200763y · Cited by 72
Modulation of Fluorescence through Coassembly of Molecules in Organic Nanostructures
Behanna, H. A., Rajangam, K. L., & Stupp, S. I. (2006) · Journal of the American Chemical Society · doi:10.1021/ja062415b · Cited by 72
Jiang, T., Meyer, T. A., Modlin, C., Zuo, X., Conticello, V. P., & Ke, Y. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b08087 · Cited by 72
Tanaka, K., Kanazawa, T., Ogawa, T., Takashima, Y., Fukuda, T., & Okada, H. (2010) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2010.07.038 · Cited by 71
Self-assembling peptides form nanodiscs that stabilize membrane proteins
Midtgaard, S. R., Pedersen, M. C., Kirkensgaard, J. J. K., Sørensen, K. K., Mortensen, K., Jensen, K. J., & Arleth, L. (2013) · Soft Matter · doi:10.1039/c3sm51727f · Cited by 71
Molecular Design of β-Hairpin Peptides for Material Construction
Rughani, R. V., & Schneider, J. P. (2008) · MRS Bulletin · doi:10.1557/mrs2008.106 · Cited by 70
Techniques for monitoring protein misfolding and aggregation in vitro and in living cells
Gregoire, S., Irwin, J. A., & Kwon, I. (2012) · Korean Journal of Chemical Engineering · doi:10.1007/s11814-012-0060-x · Cited by 69
Metal-Mediated Tandem Coassembly of Collagen Peptides into Banded Microstructures
Pires, M. M., Przybyla, D. E., Pérez, C. M. R., & Chmielewski, J. A. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2042645 · Cited by 69
Wen, Y., Roudebush, S. L., Buckholtz, G. A., Goehring, T., Giannoukakis, N., Gawalt, E., & Meng, W. S. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.03.009 · Cited by 68
Belluti, F., Rampa, A., Gobbi, S., & Bisi, A. (2013) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2013.772983 · Cited by 68
Coassembly in Binary Mixtures of Peptide Amphiphiles Containing Oppositely Charged Residues
Hamley, I. W., Dehsorkhi, A., & Castelletto, V. (2013) · Langmuir · doi:10.1021/la400163q · Cited by 68
Photo-induced Reversible Structural Transition of Cationic Diphenylalanine Peptide Self-Assembly
Ma, H., Fei, J., Li, Q., & Li, J. (2014) · Small · doi:10.1002/smll.201402140 · Cited by 68
The relationship between amyloid structure and cytotoxicity
Marshall, K. E., Marchante, R., Xue, W., & Serpell, L. C. (2014) · Prion · doi:10.4161/pri.28860 · Cited by 67
Ardoña, H. A. M., & Tovar, J. D. (2014) · Chemical Science · doi:10.1039/c4sc03122a · Cited by 67
Modification of β-Sheet Forming Peptide Hydrophobic Face: Effect on Self-Assembly and Gelation
Elsawy, M. A., Smith, A. M., Hodson, N. W., Squires, A. M., Miller, A. F., & Saiani, A. (2016) · Langmuir · doi:10.1021/acs.langmuir.5b03841 · Cited by 67
Self-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly properties
Aronsson, C., Dånmark, S., Zhou, F., Öberg, P. Å., Enander, K., Su, H., & Aili, D. (2015) · Scientific Reports · doi:10.1038/srep14063 · Cited by 66
Wang, J., Yuan, C., Han, Y., Wang, Y., Liu, X., Zhang, S., & Yan, X. (2017) · Small · doi:10.1002/smll.201702175 · Cited by 66
Choi, D., Lee, H., Kim, H.-B., Yang, M., Heo, J., Won, Y., Jang, S. S., Park, J. K., Son, Y., Oh, T. I., et al. (2017) · Chemistry of Materials · doi:10.1021/acs.chemmater.6b04096 · Cited by 65
Collagen-Like Peptide Bioconjugates
Luo, T., & Kiick, K. L. (2017) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.6b00673 · Cited by 65
Side-chain interaction between the α-helices of poly-γ-benzyl-l- and d-glutamates
Mitsui, Y., Iitaka, Y., & Tsuboi, M. (1967) · Journal of Molecular Biology · doi:10.1016/0022-2836(67)90085-x · Cited by 64
Structure-Based Design of Dendritic Peptide Bolaamphiphiles for siRNA Delivery
Zeng, H., Johnson, M. E., Oldenhuis, N. J., Tiambeng, T. N., & Guan, Z. (2015) · ACS Central Science · doi:10.1021/acscentsci.5b00233 · Cited by 64
Sathaye, S., Zhang, H., Sönmez, C., Schneider, J. P., MacDermaid, C. M., Bargen, C. D. V., Saven, J. G., & Pochan, D. J. (2014) · Biomacromolecules · doi:10.1021/bm500874t · Cited by 64
Modular self-assembling biomaterials for directing cellular responses
Collier, J. H. (2008) · Soft Matter · doi:10.1039/b805563g · Cited by 63
Borges, J., Sousa, M. P., Çınar, G., Caridade, S. G., Guler, M. O., & Mano, J. F. (2017) · Advanced Functional Materials · doi:10.1002/adfm.201605122 · Cited by 63
Decorating Self-Assembled Peptide Cages with Proteins
Ross, J. F., Bridges, A. M., Fletcher, J. M., Shoemark, D. K., Alibhai, D., Bray, H. E. V., Beesley, J. L., Dawson, W., Hodgson, L. R., Mantell, J., et al. (2017) · ACS Nano · doi:10.1021/acsnano.7b02368 · Cited by 63
Coassembly of Oppositely Charged Short Peptides into Well-Defined Supramolecular Hydrogels
Xu, X., Chen, C., Lu, B., et al. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp9102417 · Cited by 62
Biocatalytically Triggered Co‐Assembly of Two‐Component Core/Shell Nanofibers
Abul‐Haija, Y. M., Roy, S., Frederix, P. W. J. M., Javid, N., Jayawarna, V., & Ulijn, R. V. (2013) · Small · doi:10.1002/smll.201301668 · Cited by 62
Complex coacervates of oppositely charged co-polypeptides inspired by the sandcastle worm glue
Zhang, L., Lipik, V. T., & Miserez, A. (2016) · Journal of Materials Chemistry B · doi:10.1039/c5tb02298c · Cited by 62
Advances in Hyaluronic Acid-Based Drug Delivery Systems
Jiao, Y., Pang, X., & Zhai, G. (2016) · Current Drug Targets · doi:10.2174/1389450116666150531155200 · Cited by 61
Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets
Khondker, A., Alsop, R. J., & Rheinstadter, M. C. (2017) · Membranes · doi:10.3390/membranes7030049 · Cited by 61
Building the Microtubule Cytoskeleton Piece by Piece
Alfaro-Aco, R., & Petry, S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.638452 · Cited by 60
Applications of self-assembling peptide scaffolds in regenerative medicine: the way to the clinic
Ravichandran, R., Griffith, M., & Phopase, J. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb01095g · Cited by 60
Peptide Self-Assemblies for Drug Delivery
Leite, D. M., Barbu, E., Pilkington, G. J., & Lalatsa, A. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150605120456 · Cited by 60
Roodyn, D. B. (1978) · Springer eBooks · doi:10.1007/978-1-4615-7942-7 · Cited by 60
Short Homodimeric and Heterodimeric Coiled Coils
Dong, H., & Hartgerink, J. D. (2006) · Biomacromolecules · doi:10.1021/bm050833n · Cited by 59
Thixotropic Hydrogelators Based on a Cyclo(dipeptide) Derivative
Hoshizawa, H., Minemura, Y., Yoshikawa, K., Suzuki, M., & Hanabusa, K. (2013) · Langmuir · doi:10.1021/la402333h · Cited by 59
Selective Assembly of a High Stability AAB Collagen Heterotrimer
O’Leary, L. E. R., Fallas, J. A., & Hartgerink, J. D. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909720g · Cited by 58
Enhanced Oligonucleotide Binding to Self-Assembled Nanofibers
Guler, M. O., Pokorski, J. K., Appella, D. H., & Stupp, S. I. (2005) · Bioconjugate Chemistry · doi:10.1021/bc050053b · Cited by 58
Marques, M., Alves, V. D., & Coelhoso, I. M. (2016) · Membranes · doi:10.3390/membranes7010001 · Cited by 58
Cyclic Peptides as Inhibitors of Amyloid Fibrillation
Luo, J., & Abrahams, J. P. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201304253 · Cited by 57
Tanaka, K., Kanazawa, T., Horiuchi, S., Ando, T., Sugawara, K., Takashima, Y., Seta, Y., & Okada, H. (2013) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2013.07.069 · Cited by 57
Tai, Z., Wang, X., Tian, J., Gao, Y., Zhang, L., Yao, C., Wu, X., Zhang, W., Zhu, Q., & Gao, S. (2015) · Biomacromolecules · doi:10.1021/bm501777a · Cited by 57
How Metal Ions Affect Amyloid Formation: Cu2+‐ and Zn2+‐Sensitive Peptides
Pagel, K., Seri, T., von Berlepsch, H., Griebel, J., Kirmse, R., Böttcher, C., & Koksch, B. (2008) · ChemBioChem · doi:10.1002/cbic.200700656 · Cited by 57
Cited by
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
Supramolecular Photothermal Effects: A Promising Mechanism for Efficient Thermal Conversion
Zhao, L., Liu, Y., Xing, R., & Yan, X. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201909825 · Cited by 339
Primitive selection of the fittest emerging through functional synergy in nucleopeptide networks
Bandela, A. K., Wagner, N., Sadihov, H., Morales-Reina, S., Chotera-Ouda, A., Basu, K., Cohen-Luria, R., de la Escosura, A., & Ashkenasy, G. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2015285118 · Cited by 49
Metadata
- Authors
- Raymond, D. M., & Nilsson, B. L.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2018
- Volume
- 47
- Issue
- 10
- Pages
- 3659-3720
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2802297868
- Cited by
- 346
- References
- 533
- FWCI
- 2.10
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.