The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Peptide supramolecular materials for therapeutics
Open accessAbstract
Supramolecular assembly of peptide-based monomers into nanostructures offers many promising applications in advanced therapies. In this Tutorial Review, we introduce molecular designs to control the structure and potential biological function of supramolecular assemblies.
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
Functional Supramolecular Polymers
Aida, T., Meijer, E. W., & Stupp, S. I. (2012) · Science · doi:10.1126/science.1205962 · Cited by 3,696
Self-citationSelf-Assembly and Mineralization of Peptide-Amphiphile Nanofibers
Hartgerink, J. D., Beniash, E., & Stupp, S. I. (2001) · Science · doi:10.1126/science.1063187 · Cited by 3,601
Self-citationPERSPECTIVE ARTICLE: Growth factors and cytokines in wound healing
Barrientos, S., Stojadinovic, O., Golinko, M. S., Brem, H., & Tomic‐Canic, M. (2008) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2008.00410.x · Cited by 3,583
Integrins and other cell adhesion molecules
Albelda, S. M., & Buck, C. A. (1990) · The FASEB Journal · doi:10.1096/fasebj.4.11.2199285 · Cited by 1,966
Self-assembling organic nanotubes based on a cyclic peptide architecture
Ghadiri, M. R., Granja, J. R., Milligan, R. A., McRee, D. E., & Khazanovich, N. (1993) · Nature · doi:10.1038/366324a0 · Cited by 1,746
Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.
Zhang, S., Holmes, T., Lockshin, C., & Rich, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3334 · Cited by 1,304
Smith, A. M., Williams, R. J., Tang, C., Coppo, P., Collins, R. F., Turner, M. L., Saiani, A., & Ulijn, R. V. (2008) · Advanced Materials · doi:10.1002/adma.200701221 · Cited by 995
Demystifying Heparan Sulfate–Protein Interactions
Xu, D., & Esko, J. D. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035314 · Cited by 805
Jones, F. S., & Jones, P. L. (2000) · Developmental Dynamics · doi:10.1002/(sici)1097-0177(200006)218:2<235::aid-dvdy2>3.0.co;2-g · Cited by 690
Paramonov, S. E., Jun, H.-W., & Hartgerink, J. D. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060573x · Cited by 675
Haines-Butterick, L., Rajagopal, K., Branco, M., Salick, D., Rughani, R., Pilarz, M., Lamm, M. S., Pochan, D. J., & Schneider, J. P. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701980104 · Cited by 642
A self-assembly pathway to aligned monodomain gels
Zhang, S., Greenfield, M. A., Mata, A., Palmer, L. C., Bitton, R., Mantei, J. R., Aparicio, C., de la Cruz, M. O., & Stupp, S. I. (2010) · Nature Materials · doi:10.1038/nmat2778 · Cited by 627
Self-citationEnergy landscapes and functions of supramolecular systems
Tantakitti, F., Boekhoven, J., Wang, X., Kazantsev, R. V., Yu, T., Li, J., Zhuang, E., Zandi, R., Ortony, J. H., Newcomb, C. J., et al. (2016) · Nature Materials · doi:10.1038/nmat4538 · Cited by 464
Self-citationSupramolecular Hydrogels Respond to Ligand−Receptor Interaction
Zhang, Y., Gu, H., Yang, Z., & Xu, B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036817k · Cited by 461
Cheng, T.-Y., Chen, M.-H., Chang, W.-H., Huang, M.-Y., & Wang, T.-W. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2012.11.043 · Cited by 383
Dong, H., Paramonov, S. E., Aulisa, L., Bakota, E. L., & Hartgerink, J. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072536r · Cited by 344
Hamley, I. W. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201310006 · Cited by 323
Synthetic lipidation of peptides and amino acids: monolayer structure and properties.
Berndt, P., Fields, G. B., & Tirrell, M. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00142a019 · Cited by 304
Pathway Selection in Peptide Amphiphile Assembly
Korevaar, P. A., Newcomb, C. J., Meijer, E. W., & Stupp, S. I. (2014) · Journal of the American Chemical Society · doi:10.1021/ja503882s · Cited by 265
Self-citationDynamic peptide libraries for the discovery of supramolecular nanomaterials
Pappas, C. G., Shafi, R., Sasselli, I. R., Siccardi, H., Wang, T., Narang, V., Abzalimov, R., Wijerathne, N., & Ulijn, R. V. (2016) · Nature Nanotechnology · doi:10.1038/nnano.2016.169 · Cited by 240
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
Self-citationpH and Amphiphilic Structure Direct Supramolecular Behavior in Biofunctional Assemblies
Moyer, T. J., Finbloom, J. A., Chen, F., Toft, D. J., Cryns, V. L., & Stupp, S. I. (2014) · Journal of the American Chemical Society · doi:10.1021/ja5042429 · Cited by 204
Self-citationInjectable Multidomain Peptide Nanofiber Hydrogel as a Delivery Agent for Stem Cell Secretome
Bakota, E. L., Wang, Y., Danesh, F. R., & Hartgerink, J. D. (2011) · Biomacromolecules · doi:10.1021/bm200035r · Cited by 184
Gel Scaffolds of BMP‐2‐Binding Peptide Amphiphile Nanofibers for Spinal Arthrodesis
Lee, S. S., Hsu, E. L., Mendoza, M., Ghodasra, J., Nickoli, M. S., Ashtekar, A., Polavarapu, M., Babu, J., Riaz, R. M., Nicolas, J. D., et al. (2015) · Advanced Healthcare Materials · doi:10.1002/adhm.201400129 · Cited by 183
Self-citationSulfated glycopeptide nanostructures for multipotent protein activation
Lee, S. S., Fyrner, T., Chen, F., Álvarez, Z., Sleep, E., Chun, D. S., Weiner, J. A., Cook, R. W., Freshman, R. D., Schallmo, M. S., et al. (2017) · Nature Nanotechnology · doi:10.1038/nnano.2017.109 · Cited by 182
Self-citationInternal dynamics of a supramolecular nanofibre
Ortony, J. H., Newcomb, C. J., Matson, J. B., Palmer, L. C., Doan, P. E., Hoffman, B. M., & Stupp, S. I. (2014) · Nature Materials · doi:10.1038/nmat3979 · Cited by 170
Self-citationda Silva, R. M. P., van der Zwaag, D., Albertazzi, L., Lee, S. S., Meijer, E. W., & Stupp, S. I. (2016) · Nature Communications · doi:10.1038/ncomms11561 · Cited by 161
Self-citationHighly Angiogenic Peptide Nanofibers
Kumar, V. A., Taylor, N. L., Shi, S., Wang, B. K., Jalan, A. A., Kang, M. K., Wickremasinghe, N. C., & Hartgerink, J. D. (2015) · ACS Nano · doi:10.1021/nn506544b · Cited by 160
Switching of self-assembly in a peptide nanostructure with a specific enzyme
Webber, M. J., Newcomb, C. J., Bitton, R., & Stupp, S. I. (2011) · Soft Matter · doi:10.1039/c1sm05610g · Cited by 152
Self-citationHeparin Mimetic Peptide Nanofibers Promote Angiogenesis
Mammadov, R., Mammadov, B., Ataca, S. T., Aydın, B., Yağcı, R., Tekinay, A. B., & Guler, M. O. (2011) · Biomacromolecules · doi:10.1021/bm200957s · Cited by 145
Presentation and Recognition of Biotin on Nanofibers Formed by Branched Peptide Amphiphiles
Guler, M. O., Soukasene, S., Hulvat, J. F., & Stupp, S. I. (2004) · Nano Letters · doi:10.1021/nl048238z · Cited by 125
Self-citationHamley, I. W., Ansari, I. A., Castelletto, V., Nuhn, H., Rösler, A., & Klok, H. (2005) · Biomacromolecules · doi:10.1021/bm049286g · Cited by 121
Treatment of hind limb ischemia using angiogenic peptide nanofibers
Kumar, V., Liu, Q., Wickremasinghe, N. C., Shi, S., Cornwright, T. T., Deng, Y., Azares, A. R., Moore, A. N., Acevedo‐Jake, A. M., Agudo, N. R., et al. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.04.032 · Cited by 106
Growth Factor Binding on Heparin Mimetic Peptide Nanofibers
Mammadov, R., Mammadov, B., Guler, M. O., & Tekinay, A. B. (2012) · Biomacromolecules · doi:10.1021/bm3010897 · Cited by 101
Griffin, K. S., Davis, K. M., McKinley, T. O., Anglen, J. O., Chu, T. G., Boerckel, J. D., & Kacena, M. A. (2015) · Clinical Reviews in Bone and Mineral Metabolism · doi:10.1007/s12018-015-9194-9 · Cited by 99
Injectable biomimetic liquid crystalline scaffolds enhance muscle stem cell transplantation
Sleep, E., Cosgrove, B. D., McClendon, M., Preslar, A. T., Chen, C. H., Sangji, M. H., Pérez, C. M. R., Haynes, R. D., Meade, T. J., Blau, H. M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708142114 · Cited by 94
Self-citationBerns, E. J., Álvarez, Z., Goldberger, J. E., et al. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.04.010 · Cited by 85
Water Dynamics from the Surface to the Interior of a Supramolecular Nanostructure
Ortony, J. H., Qiao, B., Newcomb, C. J., Keller, T. J., Palmer, L. C., Deiss‐Yehiely, E., de la Cruz, M. O., Han, S., & Stupp, S. I. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02969 · Cited by 74
Self-citationGlycosaminoglycan mimetic peptide nanofibers promote mineralization by osteogenic cells
Kocabey, S., Ceylan, H., Tekinay, A. B., & Guler, M. O. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.07.007 · Cited by 55
Epitope topography controls bioactivity in supramolecular nanofibers
Sur, S., Tantakitti, F., Matson, J. B., & Stupp, S. I. (2015) · Biomaterials Science · doi:10.1039/c4bm00326h · Cited by 54
Self-citationCovalent Capture of Aligned Self-Assembling Nanofibers
Li, I.-C., & Hartgerink, J. D. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04655 · Cited by 54
Choe, S., Veliceasa, D., Bond, C. W., Harrington, D. A., Stupp, S. I., McVary, K. T., & Podlasek, C. A. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.01.014 · Cited by 52
Self-citationPreslar, A. T., Tantakitti, F., Park, K., Zhang, S., Stupp, S. I., & Meade, T. J. (2016) · ACS Nano · doi:10.1021/acsnano.6b00267 · Cited by 51
Self-citationMotalleb, R., Berns, E. J., Patel, P., Gold, J., Stupp, S. I., & Kuhn, H. G. (2018) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.2644 · Cited by 38
Self-citationTenascin-C Mimetic Peptide Nanofibers Direct Stem Cell Differentiation to Osteogenic Lineage
Sever, M., Mammadov, B., Guler, M. O., & Tekinay, A. B. (2014) · Biomacromolecules · doi:10.1021/bm501271x · Cited by 29
A glycosaminoglycan mimetic peptide nanofiber gel as an osteoinductive scaffold
Tansık, G., Kılıç, E., Beter, M., Demiralp, B., Şendur, G. K., Can, N., Özkan, H., Duman, E., Guler, M. O., & Tekinay, A. B. (2016) · Biomaterials Science · doi:10.1039/c6bm00179c · Cited by 29
Microtubules viewed as molecular ant colonies
Tabony, J. (2006) · Biology of the Cell · doi:10.1042/bc20050087 · Cited by 27
Gouveia, R. M., Hamley, I. W., & Connon, C. J. (2015) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-015-5581-5 · Cited by 19
Cited by
Targeted Drug Delivery via the Use of ECM-Mimetic Materials
Hwang, J., Sullivan, M. O., & Kiick, K. L. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00069 · Cited by 76
Chiral Recognition of Lipid Bilayer Membranes by Supramolecular Assemblies of Peptide Amphiphiles
Sato, K., Ji, W., Álvarez, Z., Palmer, L. C., & Stupp, S. I. (2019) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.9b00553 · Cited by 35
Self-citation
Metadata
- Authors
- Sato, K., Hendricks, M. P., Palmer, L. C., & Stupp, S. I.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2018
- Volume
- 47
- Issue
- 20
- Pages
- 7539-7551
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W2889913341
- Cited by
- 285
- References
- 48
- FWCI
- 1.71
- 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.
