The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Ostwald’s rule of stages governs structural transitions and morphology of dipeptide supramolecular polymers
Open accessOverview
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
The kinetics of precipitation from supersaturated solid solutions
Lifshitz, I. M., & Slyozov, V. V. (1961) · Journal of Physics and Chemistry of Solids · doi:10.1016/0022-3697(61)90054-3 · Cited by 8,433
Functional Supramolecular Polymers
Aida, T., Meijer, E. W., & Stupp, S. I. (2012) · Science · doi:10.1126/science.1205962 · Cited by 3,696
Discher, D. E., & Eisenberg, A. (2002) · Science · doi:10.1126/science.1074972 · Cited by 3,551
Fabrication of novel biomaterials through molecular self-assembly
Zhang, S. (2003) · Nature Biotechnology · doi:10.1038/nbt874 · Cited by 3,347
Lehn, J. (1990) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199013041 · Cited by 3,027
Brunsveld, L., Folmer, B. J. B., Meijer, E. W., & Sijbesma, R. P. (2001) · Chemical Reviews · doi:10.1021/cr990125q · Cited by 3,006
Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes
Reches, M., & Gazit, E. (2003) · Science · doi:10.1126/science.1082387 · Cited by 2,530
Self-citationStudien über die Bildung und Umwandlung fester Körper: 1. Abhandlung: Übersättigung und Überkaltung
Ostwald, W. (1897) · Zeitschrift für Physikalische Chemie · doi:10.1515/zpch-1897-2233 · Cited by 2,103
Optically healable supramolecular polymers
Burnworth, M., Tang, L., Kumpfer, J. R., Duncan, A. J., Beyer, F. L., Fiore, G. L., Rowan, S. J., & Weder, C. (2011) · Nature · doi:10.1038/nature09963 · Cited by 1,778
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
Cohen, S. I. A., Linse, S., Luheshi, L. M., Hellstrand, E., White, D. A., Rajah, L., Otzen, D. E., Vendruscolo, M., Dobson, C. M., & Knowles, T. P. J. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218402110 · Cited by 1,440
Self-citationAn Analytical Solution to the Kinetics of Breakable Filament Assembly
Knowles, T. P. J., Waudby, C. A., Devlin, G. L., Cohen, S. I. A., Aguzzi, A., Vendruscolo, M., Terentjev, E. M., Welland, M. E., & Dobson, C. M. (2009) · Science · doi:10.1126/science.1178250 · Cited by 1,139
Self-citationSelf-assembly and application of diphenylalanine-based nanostructures
Yan, X., Zhu, P., & Li, J. (2010) · Chemical Society Reviews · doi:10.1039/b915765b · Cited by 1,044
Pre-nucleation clusters as solute precursors in crystallisation
Gebauer, D., Kellermeier, M., Gale, J. D., Bergström, L., & Cölfen, H. (2014) · Chem. Soc. Rev. · doi:10.1039/c3cs60451a · Cited by 1,015
Preparation of Hollow Anatase TiO2 Nanospheres via Ostwald Ripening
Yang, H. G., & Zeng, H. C. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp0377782 · Cited by 979
Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein
Cremades, N., Cohen, S. I. A., Deas, E., Abramov, A. Y., Chen, A. Y., Orte, A., Sandal, M., Clarke, R. W., Dunne, P., Aprile, F. A., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.037 · Cited by 911
Self-citationRole of Intermolecular Forces in Defining Material Properties of Protein Nanofibrils
Knowles, T. P., Fitzpatrick, A. W., Meehan, S., Mott, H. R., Vendruscolo, M., Dobson, C. M., & Welland, M. E. (2007) · Science · doi:10.1126/science.1150057 · Cited by 782
Self-citationKinetics of Solidification of Supercooled Liquid Mercury Droplets
Turnbull, D. (1952) · The Journal of Chemical Physics · doi:10.1063/1.1700435 · Cited by 750
Self-Assembling Peptide Nanotubes
Hartgerink, J. D., Granja, J. R., Milligan, R. A., & Ghadiri, M. R. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953070s · Cited by 626
Hamley, I. W. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200700861 · Cited by 618
Supramolecular polymer chemistry—scope and perspectives
Lehn, J. (2002) · Polymer International · doi:10.1002/pi.852 · Cited by 520
Meisl, G., Yang, X., Hellstrand, E., Frohm, B., Kirkegaard, J. B., Cohen, S. I. A., Dobson, C. M., Linse, S., & Knowles, T. P. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401564111 · Cited by 505
Self-citationKinetics of sickle hemoglobin polymerization
Ferrone, F. A., Hofrichter, J., & Eaton, W. A. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90175-5 · Cited by 502
Strong Piezoelectricity in Bioinspired Peptide Nanotubes
Kholkin, A., Amdursky, N., Bdikin, I., Gazit, E., & Rosenman, G. (2010) · ACS Nano · doi:10.1021/nn901327v · Cited by 455
Self-citationFmoc-Diphenylalanine Self-Assembly Mechanism Induces Apparent p Ka Shifts
Tang, C., Smith, A. M., Collins, R. F., Ulijn, R. V., & Saiani, A. (2009) · Langmuir · doi:10.1021/la900653q · Cited by 444
Adler-Abramovich, L., Reches, M., Sedman, V. L., Allen, S., Tendler, S. J. B., & Gazit, E. (2006) · Langmuir · doi:10.1021/la052409d · Cited by 391
Self-citationGreenwood, R., & Kendall, K. (1999) · Journal of the European Ceramic Society · doi:10.1016/s0955-2219(98)00208-8 · Cited by 360
Growth Kinetics of Nanocrystalline ZnO Particles from Colloidal Suspensions
Wong, E. M., Bonevich, J. E., & Searson, P. C. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp982397n · Cited by 351
Ostwald Ripening: A Synthetic Approach for Hollow Nanomaterials
Chun Zeng, H. (2007) · Current Nanoscience · doi:10.2174/157341307780619279 · Cited by 341
Characterization of supramolecular polymers
Liu, Y., Wang, Z., & Zhang, X. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35084j · Cited by 340
Multiphase transformation and Ostwald’s rule of stages during crystallization of a metal phosphate
Chung, S.-Y., Kim, Y.-M., Kim, J.-G., & Kim, Y.-J. (2009) · Nature Physics · doi:10.1038/nphys1148 · Cited by 313
Ostwald ripening of precipitates
Kahlweit, M. (1975) · Advances in Colloid and Interface Science · doi:10.1016/0001-8686(75)85001-9 · Cited by 313
Kinetics of sickle hemoglobin polymerization
Ferrone, F. A., Hofrichter, J., & Eaton, W. A. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90174-3 · Cited by 288
Ikezoe, Y., Washino, G., Uemura, T., Kitagawa, S., & Matsui, H. (2012) · Nature Materials · doi:10.1038/nmat3461 · Cited by 227
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
Blue Luminescence Based on Quantum Confinement at Peptide Nanotubes
Amdursky, N., Molotskii, M., Aronov, D., Adler-Abramovich, L., Gazit, E., & Rosenman, G. (2009) · Nano Letters · doi:10.1021/nl9008265 · Cited by 209
Self-citationOn the ostwald ripening theory
Vengrenovitch, R. D. (1982) · Acta Metallurgica · doi:10.1016/0001-6160(82)90004-9 · Cited by 175
Expanding the Solvent Chemical Space for Self-Assembly of Dipeptide Nanostructures
Mason, T. O., Chirgadze, D. Y., Levin, A., Adler-Abramovich, L., Gazit, E., Knowles, T. P. J., & Buell, A. K. (2014) · ACS Nano · doi:10.1021/nn404237f · Cited by 172
Self-citationYan, 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
Observation of spatial propagation of amyloid assembly from single nuclei
Knowles, T. P. J., White, D. A., Abate, A. R., Agresti, J. J., Cohen, S. I. A., Sperling, R. A., De Genst, E. J., Dobson, C. M., & Weitz, D. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105555108 · Cited by 158
Self-citationJördens, S., Isa, L., Usov, I., et al. (2013) · Nature Communications · doi:10.1038/ncomms2911 · Cited by 147
Self‐Assembled Organic Nanostructures with Metallic‐Like Stiffness
Adler‐Abramovich, L., Kol, N., Yanai, I., Barlam, D. M., Shneck, R. Z., Gazit, E., & Rousso, I. Y. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201002037 · Cited by 144
Self-citationA Generic Mechanism of Emergence of Amyloid Protofilaments from Disordered Oligomeric Aggregates
Auer, S., Meersman, F., Dobson, C. M., & Vendruscolo, M. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000222 · Cited by 118
Self-citationYucelen, G. I., Choudhury, R. P., Vyalikh, A., et al. (2011) · Journal of the American Chemical Society · doi:10.1021/ja111055q · Cited by 75
Evidence of ferroelectricity and phase transition in pressed diphenylalanine peptide nanotubes
Bdikin, I. K., Bystrov, V. S., Kopyl, S., Lopes, R. P. G., Delgadillo, I., Gracio, J. J. D. A., Мишина, Е. Д., Sigov, A. S., & Kholkin, A. L. (2012) · Applied Physics Letters · doi:10.1063/1.3676417 · Cited by 67
Following the aggregation of amyloid-forming peptides by computer simulations
Melquiond, A. S. J., Boucher, G., Mousseau, N., & Derreumaux, P. (2005) · The Journal of Chemical Physics · doi:10.1063/1.1886725 · Cited by 64
What Determines the Structure and Stability of KFFE Monomers, Dimers, and Protofibrils?
Bellesia, G., & Shea, J. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.10.040 · Cited by 62
Hamley, I. W., Castelletto, V., Mykhaylyk, O. O., Yang, Z. L., May, R., Lyakhova, K. S., Sevink, G. J. A., & Zvelindovsky, A. V. (2004) · Langmuir · doi:10.1021/la0484927 · Cited by 57
Charalambidis, G., Kasotakis, E., Lazarides, T., Mitraki, A., & Coutsolelos, A. G. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201100362 · Cited by 55
Mapping out the multistage fibrillation of glucagon
Ghodke, S. D., Nielsen, S. B., Christiansen, G., Hjuler, H. A., Flink, J. M., & Otzen, D. E. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08465.x · Cited by 36
Spatial Propagation of Protein Polymerization
Cohen, S. I. A., Rajah, L., Yoon, C. H., Buell, A. K., White, D. A., Sperling, R. A., Vendruscolo, M., Terentjev, E. M., Dobson, C. M., Weitz, D. A., et al. (2014) · Physical Review Letters · doi:10.1103/physrevlett.112.098101 · Cited by 20
Self-citation
Cited by
Biomimetic peptide self-assembly for functional materials
Levin, A., Hakala, T. A., Schnaider, L., Bernardes, G. J. L., Gazit, E., & Knowles, T. P. J. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-0215-y · Cited by 853
Self-citationSelf-assembling peptide semiconductors
Tao, K., Makam, P., Aizen, R., & Gazit, E. (2017) · Science · doi:10.1126/science.aam9756 · Cited by 490
Self-citationViologen-Based Conjugated Covalent Organic Networks via Zincke Reaction
Das, G., Skorjanc, T., Sharma, S. K., Gándara, F., Lusi, M., Shankar Rao, D. S., Vimala, S., Krishna Prasad, S., Raya, J., Han, D. S., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02836 · Cited by 316
Delfi, M., Sartorius, R., Ashrafizadeh, M., Sharifi, E., Zhang, Y., De Berardinis, P., Zarrabi, A., Varma, R. S., Tay, F. R., Smith, B. R., et al. (2021) · Nano Today · doi:10.1016/j.nantod.2021.101119 · Cited by 253
Composite biomaterial scaffolds for cardiac tissue engineering
Shapira, A., Feiner, R., & Dvir, T. (2016) · International Materials Reviews · doi:10.1179/1743280415y.0000000012 · Cited by 114
Metadata
- Authors
- Levin, A., Mason, T. O., Adler-Abramovich, L., Buell, A. K., Meisl, G., Galvagnion, C., Bram, Y., Stratford, S. A., Dobson, C. M., Knowles, T. P. J., & Gazit, E.
- Venue
- Nature Communications
- Published
- 2014-11-13
- Volume
- 5
- Issue
- 1
- Pages
- 5219-5219
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2013455144
- Cited by
- 275
- References
- 50
- FWCI
- 6.18
- Type
- journal article
- Language
- en
- Open access
- bronze
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.