Multicomponent peptide assemblies

Matrix elasticity directs stem cell lineage specification

Engler, A. J., Sen, S., Sweeney, H. L., & Discher, D. E. (2006) · Cell · doi:10.1016/j.cell.2006.06.044 · Cited by 13,915

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin

Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,423

Scaffolds in tissue engineering bone and cartilage

Hutmacher, D. W. (2000) · Biomaterials · doi:10.1016/s0142-9612(00)00121-6 · Cited by 4,994

New Perspectives in Cell Adhesion: RGD and Integrins

Ruoslahti, E., & Pierschbacher, M. D. (1987) · Science · doi:10.1126/science.2821619 · Cited by 4,865

A perivascular origin for mesenchymal stem cells in multiple human organs

Crisan, M., Yap, S., Casteilla, L., Chen, C.-W., Corselli, M., Park, T. S., Andriolo, G., Sun, B., Zheng, B., Zhang, L., et al. (2008) · Cell Stem Cell · doi:10.1016/j.stem.2008.07.003 · Cited by 3,991

Collagen Structure and Stability

Shoulders, M. D., & Raines, R. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.032207.120833 · Cited by 3,923

Fabrication of novel biomaterials through molecular self-assembly

Zhang, S. (2003) · Nature Biotechnology · doi:10.1038/nbt874 · Cited by 3,347

Methods in Molecular Biology

Ranade, V. V. (2009) · American Journal of Therapeutics · doi:10.1097/mjt.0b013e31817c941f · Cited by 2,775

Huntington's disease

Walker, F. O. (2007) · The Lancet · doi:10.1016/s0140-6736(07)60111-1 · Cited by 2,603

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

Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes

Reches, M., & Gazit, E. (2003) · Science · doi:10.1126/science.1082387 · Cited by 2,530

CD44: From adhesion molecules to signalling regulators

Ponta, H., Sherman, L., & Herrlich, P. A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1004 · Cited by 2,386

Imaging and Photodynamic Therapy: Mechanisms, Monitoring, and Optimization

Celli, J. P., Spring, B. Q., Rizvi, I., Evans, C. L., Samkoe, K. S., Verma, S., Pogue, B. W., & Hasan, T. (2010) · Chemical Reviews · doi:10.1021/cr900300p · Cited by 2,324

Structure of the cross-β spine of amyloid-like fibrils

Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

Biancalana, M., & Koide, S. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.04.001 · Cited by 2,195

Selective Differentiation of Neural Progenitor Cells by High-Epitope Density Nanofibers

Silva, G. A., Czeisler, C., Niece, K. L., Beniash, E., Harrington, D. A., Kessler, J. A., & Stupp, S. I. (2004) · Science · doi:10.1126/science.1093783 · Cited by 2,169

A practical guide to hydrogels for cell culture

Caliari, S. R., & Burdick, J. A. (2016) · Nature Methods · doi:10.1038/nmeth.3839 · Cited by 2,075

Cryo-EM structures of tau filaments from Alzheimer’s disease

Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061

Water Gelation by Small Organic Molecules

Estroff, L. A., & Hamilton, A. D. (2004) · Chemical Reviews · doi:10.1021/cr0302049 · Cited by 2,034

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 1,996

Biomedical applications of collagen

Lee, C. H., Singla, A., & Lee, Y. (2001) · International Journal of Pharmaceutics · doi:10.1016/s0378-5173(01)00691-3 · Cited by 1,945

High-water-content mouldable hydrogels by mixing clay and a dendritic molecular binder

Wang, Q., Mynar, J. L., Yoshida, M., Lee, E., Lee, M., Okuro, K., Kinbara, K., & Aida, T. (2010) · Nature · doi:10.1038/nature08693 · Cited by 1,580

Nanoscale Forces and Their Uses in Self‐Assembly

Bishop, K. J. M., Wilmer, C. E., Soh, S., & Grzybowski, B. A. (2009) · Small · doi:10.1002/smll.200900358 · Cited by 1,521

Injectable and biodegradable hydrogels: gelation, biodegradation and biomedical applications

Li, Y., Rodrigues, J., & Tomás, H. (2012) · Chem. Soc. Rev. · doi:10.1039/c1cs15203c · Cited by 1,445

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365

Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions

Hynes, R. O., & Naba, A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004903 · Cited by 1,349

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

High‐Tech Applications of Self‐Assembling Supramolecular Nanostructured Gel‐Phase Materials: From Regenerative Medicine to Electronic Devices

Hirst, A. R., Escuder, B., Miravet, J. F., & Smith, D. K. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200800022 · Cited by 1,273

Altered regulation of IL-6 production with normal aging. Possible linkage to the age-associated decline in dehydroepiandrosterone and its sulfated derivative

Daynes, R. A., Araneo, B. A., Ershler, W. B., Maloney, C., Li, G. Z., & Ryu, S. Y. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.12.5219 · Cited by 1,264

Structures, mechanical properties and applications of silk fibroin materials

Koh, L.-D., Cheng, Y., Teng, C.-P., Khin, Y.-W., Loh, X.-J., Tee, S.-Y., Low, M., Ye, E., Yu, H.-D., Zhang, Y.-W., et al. (2015) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2015.02.001 · Cited by 1,241

Molecular and cellular regulation of glucose transporter (GLUT) proteins in cancer

Macheda, M. L., Rogers, S., & Best, J. D. (2005) · Journal of Cellular Physiology · doi:10.1002/jcp.20166 · Cited by 1,229

Hydrogel scaffolds for tissue engineering: Progress and challenges

El-Sherbiny, I. M., & Yacoub, M. H. (2013) · Global Cardiology Science and Practice · doi:10.5339/gcsp.2013.38 · Cited by 1,062

Coiled coils: a highly versatile protein folding motif

Burkhard, P., Stetefeld, J., & Strelkov, S. V. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01898-5 · Cited by 1,054

Self-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

Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils

Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044

Fibril structure of amyloid-β(1–42) by cryo–electron microscopy

Gremer, L., Schölzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., Lopez-Iglesias, C., Hoyer, W., Heise, H., et al. (2017) · Science · doi:10.1126/science.aao2825 · Cited by 1,041

The Ultraviolet Circular Dichroism of Polypeptides1

Holzwarth, G., & Doty, P. (1965) · Journal of the American Chemical Society · doi:10.1021/ja01080a015 · Cited by 1,036

Peptide self-assembly: thermodynamics and kinetics

Wang, J., Liu, K., Xing, R., & Yan, X. (2016) · Chemical Society Reviews · doi:10.1039/c6cs00176a · Cited by 1,035

Nanostructured Hydrogels for Three‐Dimensional Cell Culture Through Self‐Assembly of Fluorenylmethoxycarbonyl–Dipeptides

Jayawarna, V., Ali, M., Jowitt, T. A., Miller, A. F., Saiani, A., Gough, J. E., & Ulijn, R. V. (2006) · Advanced Materials · doi:10.1002/adma.200501522 · Cited by 1,028

Hydrogel biomaterials: A smart future?

Kopeček, J. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.07.044 · Cited by 1,003

Fmoc‐Diphenylalanine Self Assembles to a Hydrogel via a Novel Architecture Based on π–π Interlocked β‐Sheets

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

Methods Molecular Biology

Bharathavikru, S., & Dudnakova, T. (2016) · Cited by 957

Biological Photothermal Nanodots Based on Self-Assembly of Peptide–Porphyrin Conjugates for Antitumor Therapy

Zou, Q., Abbas, M., Zhao, L., Li, S., Shen, G., & Yan, X. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b11382 · Cited by 929

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

Wei, G., Su, Z., Reynolds, N. P., Arosio, P., Hamley, I. W., Gazit, E., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00542j · Cited by 904

Recent Studies of Pickering Emulsions: Particles Make the Difference

Wu, J., & Ma, G. (2016) · Small · doi:10.1002/smll.201600877 · Cited by 877

Design of nanostructures based on aromatic peptide amphiphiles

Fleming, S., & Ulijn, R. V. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00247d · Cited by 840

Collagen

(2008) · Springer eBooks · doi:10.1007/978-0-387-73906-9 · Cited by 827

X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS

EANES, E. D., & GLENNER, G. G. (1968) · Journal of Histochemistry & Cytochemistry · doi:10.1177/16.11.673 · Cited by 823

Rigid, Self‐Assembled Hydrogel Composed of a Modified Aromatic Dipeptide

Mahler, A., Reches, M., Rechter, M., Cohen, S., & Gazit, E. (2006) · Advanced Materials · doi:10.1002/adma.200501765 · Cited by 813

Nano neuro knitting: Peptide nanofiber scaffold for brain repair and axon regeneration with functional return of vision

Ellis-Behnke, R. G., Liang, Y.-X., You, S.-W., Tay, D. K. C., Zhang, S., So, K.-F., & Schneider, G. E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600559103 · Cited by 796

Exploring the sequence space for (tri-)peptide self-assembly to design and discover new hydrogels

Frederix, P. W. J. M., Scott, G. G., Abul-Haija, Y. M., Kalafatovic, D., Pappas, C. G., Javid, N., Hunt, N. T., Ulijn, R. V., & Tuttle, T. (2015) · Nature Chemistry · doi:10.1038/nchem.2122 · Cited by 774

On the lag phase in amyloid fibril formation

Arosio, P., Knowles, T. P. J., & Linse, S. (2015) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp05563b · Cited by 766

Stimuli-responsive polymers: Biomedical applications and challenges for clinical translation

Hoffman, A. S. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.11.004 · Cited by 759

Challenges and breakthroughs in recent research on self-assembly

Ariga, K., Hill, J. P., Lee, M. V., Vinu, A., Charvet, R., & Acharya, S. (2008) · Science and Technology of Advanced Materials · doi:10.1088/1468-6996/9/1/014109 · Cited by 759

The binding of thioflavin-T to amyloid fibrils: localisation and implications

Krebs, M. R. H., Bromley, E. H. C., & Donald, A. M. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.08.002 · Cited by 754

Advantages of RGD peptides for directing cell association with biomaterials

Bellis, S. L. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.02.029 · Cited by 745

Telomeres in cancer: tumour suppression and genome instability

Maciejowski, J., & de Lange, T. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.171 · Cited by 745

Self-assembled monolayers with different terminating groups as model substrates for cell adhesion studies

Faucheux, N., Schweiss, R., Lützow, K., Werner, C., & Groth, T. (2004) · Biomaterials · doi:10.1016/j.biomaterials.2003.09.069 · Cited by 729

The physical properties of supramolecular peptide assemblies: from building block association to technological applications

Adler-Abramovich, L., & Gazit, E. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00164h · Cited by 714

Chiral Sign Induction by Vortices During the Formation of Mesophases in Stirred Solutions

Ribó, J. M., Crusats, J., Sagués, F., Claret, J., & Rubires, R. (2001) · Science · doi:10.1126/science.1060835 · Cited by 710

Supramolecular gels formed from multi-component low molecular weight species

Buerkle, L. E., & Rowan, S. J. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35106d · Cited by 700

Coiled Coil Domains: Stability, Specificity, and Biological Implications

Mason, J. M., & Arndt, K. M. (2004) · ChemBioChem · doi:10.1002/cbic.200300781 · Cited by 700

The Collagen-binding A-domains of Integrins α1β1 and α2β1Recognize the Same Specific Amino Acid Sequence, GFOGER, in Native (Triple-helical) Collagens

Knight, C. G., Morton, L. F., Peachey, A. R., Tuckwell, D. S., Farndale, R. W., & Barnes, M. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.35 · Cited by 695

Porphyrins at interfaces

Auwärter, W., Écija, D., Klappenberger, F., & Barth, J. V. (2015) · Nature Chemistry · doi:10.1038/nchem.2159 · Cited by 685

Dynamic reassembly of peptide RADA16 nanofiber scaffold

Yokoi, H., Kinoshita, T., & Zhang, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407843102 · Cited by 679

Self-assembled peptide-based hydrogels as scaffolds for anchorage-dependent cells

Zhou, M., Smith, A. M., Das, A. K., Hodson, N. W., Collins, R. F., Ulijn, R. V., & Gough, J. E. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.01.010 · Cited by 673

The Structure of α-Helical Coiled Coils

Lupas, A. N., & Gruber, M. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70003-6 · Cited by 667

Multi-hierarchical self-assembly of a collagen mimetic peptide from triple helix to nanofibre and hydrogel

O'Leary, L. E. R., Fallas, J. A., Bakota, E. L., Kang, M. K., & Hartgerink, J. D. (2011) · Nature Chemistry · doi:10.1038/nchem.1123 · Cited by 667

Advances in Experimental Medicine and Biology

Berry, C. L. (1973) · Journal of Medical Genetics · doi:10.1136/jmg.10.4.401-a · Cited by 661

Enzymatic Hydrogelation of Small Molecules

Yang, Z., Liang, G., & Xu, B. (2008) · Accounts of Chemical Research · doi:10.1021/ar7001914 · Cited by 661

Melittin: a Membrane-active Peptide with Diverse Functions

Raghuraman, H., & Chattopadhyay, A. (2007) · Bioscience Reports · doi:10.1007/s10540-006-9030-z · Cited by 651

Controlling hydrogelation kinetics by peptide design for three-dimensional encapsulation and injectable delivery of cells

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

Advanced transfection with Lipofectamine 2000 reagent: Primary neurons, siRNA, and high-throughput applications

Dalby, B. (2004) · Methods · doi:10.1016/j.ymeth.2003.11.023 · Cited by 619

Comprehensive Inorganic Chemistry II

(2013) · Elsevier eBooks · doi:10.1016/c2009-0-63454-1 · Cited by 614

Designer Self-Assembling Peptide Nanofiber Scaffolds for Adult Mouse Neural Stem Cell 3-Dimensional Cultures

Gelain, F., Bottai, D., Vescovi, A., & Zhang, S. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000119 · Cited by 613

Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif

D'Souza, S. E., Ginsberg, M. H., & Plow, E. F. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90096-e · Cited by 605

Enzymatic Formation of Supramolecular Hydrogels

Yang, Z., Gu, H., Fu, D., Gao, P., Lam, J. K., & Xu, B. (2004) · Advanced Materials · doi:10.1002/adma.200400340 · Cited by 602

Self-Assembly of Large and Small Molecules into Hierarchically Ordered Sacs and Membranes

Capito, R. M., Azevedo, H. S., Velichko, Y. S., Mata, A., & Stupp, S. I. (2008) · Science · doi:10.1126/science.1154586 · Cited by 601

Supramolecular Assembly of Peptide Amphiphiles

Hendricks, M. P., Sato, K., Palmer, L. C., & Stupp, S. I. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00297 · Cited by 597

Hyaluronic acid for anticancer drug and nucleic acid delivery

Dosio, F., Arpicco, S., Stella, B., & Fattal, E. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.011 · Cited by 596

Synthesis and properties of crosslinked recombinant pro-resilin

Elvin, C. M., Carr, A. G., Huson, M. G., Maxwell, J. M., Pearson, R. D., Vuocolo, T., Liyou, N. E., Wong, D. C. C., Merritt, D. J., & Dixon, N. E. (2005) · Nature · doi:10.1038/nature04085 · Cited by 594

Design and Application of Self‐Assembled Low Molecular Weight Hydrogels

de Loos, M., Feringa, B. L., & van Esch, J. H. (2005) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200400723 · Cited by 586

The Design of Coiled-Coil Structures and Assemblies

Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585

RISKS OF INTRAVITREOUS INJECTION: A COMPREHENSIVE REVIEW

JAGER, R. D., AIELLO, L. P., PATEL, S. C., & CUNNINGHAM, E. T. (2004) · Retina · doi:10.1097/00006982-200410000-00002 · Cited by 572

Polyproline-II Helix in Proteins: Structure and Function

Adzhubei, A. A., Sternberg, M. J. E., & Makarov, A. A. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.018 · Cited by 547

Controlled patterning of aligned self-assembled peptide nanotubes

Reches, M., & Gazit, E. (2006) · Nature Nanotechnology · doi:10.1038/nnano.2006.139 · Cited by 547

Supramolecular design of self-assembling nanofibers for cartilage regeneration

Shah, R. N., Shah, N. A., Del Rosario Lim, M. M., Hsieh, C., Nuber, G., & Stupp, S. I. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906501107 · Cited by 543

Manufacturing of hydrogel biomaterials with controlled mechanical properties for tissue engineering applications

Vedadghavami, A., Minooei, F., Mohammadi, M. H., Khetani, S., Rezaei Kolahchi, A., Mashayekhan, S., & Sanati-Nezhad, A. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.07.028 · Cited by 540

Supramolecular Chemistry: From Molecules to Nanomaterials

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Enzyme-assisted self-assembly under thermodynamic control

Williams, R. J., Smith, A. M., Collins, R. F., Hodson, N. W., Das, A. K., & Ulijn, R. V. (2008) · Nature Nanotechnology · doi:10.1038/nnano.2008.378 · Cited by 527

Molecular structure of amyloid fibrils: insights from solid-state NMR

Tycko, R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004173 · Cited by 527

A self-assembling peptide acting as an immune adjuvant

Rudra, J. S., Tian, Y. F., Jung, J. P., & Collier, J. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912124107 · Cited by 523

Protein Misfolding Diseases

Hartl, F. U. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044518 · Cited by 520

The importance of the self-assembly process to control mechanical properties of low molecular weight hydrogels

Raeburn, J., Zamith Cardoso, A., & Adams, D. J. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60030k · Cited by 515

Enzyme-Triggered Self-Assembly of Peptide Hydrogels via Reversed Hydrolysis

Toledano, S., Williams, R. J., Jayawarna, V., & Ulijn, R. V. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056549l · Cited by 512

Simple Peptide‐Tuned Self‐Assembly of Photosensitizers towards Anticancer Photodynamic Therapy

Liu, K., Xing, R., Zou, Q., Ma, G., Möhwald, H., & Yan, X. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201509810 · Cited by 503

Self-assembling peptide scaffolds for regenerative medicine

Matson, J. B., & Stupp, S. I. (2012) · Chem. Commun. · doi:10.1039/c1cc15551b · Cited by 501

Encapsulation of curcumin in self-assembling peptide hydrogels as injectable drug delivery vehicles

Altunbas, A., Lee, S. J., Rajasekaran, S. A., Schneider, J. P., & Pochan, D. J. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.04.069 · Cited by 497

Rational design of hydrogels for tissue engineering: Impact of physical factors on cell behavior

Brandl, F., Sommer, F., & Goepferich, A. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2006.09.017 · Cited by 496

Self-Assembling Cages from Coiled-Coil Peptide Modules

Fletcher, J. M., Harniman, R. L., Barnes, F. R. H., Boyle, A. L., Collins, A., Mantell, J., Sharp, T. H., Antognozzi, M., Booth, P. J., Linden, N., et al. (2013) · Science · doi:10.1126/science.1233936 · Cited by 490

Fmoc-modified amino acids and short peptides: simple bio-inspired building blocks for the fabrication of functional materials

Tao, K., Levin, A., Adler-Abramovich, L., & Gazit, E. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00889a · Cited by 482

Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells

Simeoni, F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg385 · Cited by 480

Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold

Koutsopoulos, S., Unsworth, L. D., Nagai, Y., & Zhang, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807506106 · Cited by 475

Self-assembly of short peptides to form hydrogels: Design of building blocks, physical properties and technological applications

Fichman, G., & Gazit, E. (2014) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.08.013 · Cited by 464

Self-assembling materials for therapeutic delivery

Branco, M. C., & Schneider, J. P. (2009) · Acta Biomaterialia · doi:10.1016/j.actbio.2008.09.018 · Cited by 462

Enzymatic Formation of Supramolecular Hydrogels

Yang, Z., Gu, H., Fu, D., Gao, P., Lam, J. K., & Xu, B. (2006) · Advanced Materials · doi:10.1002/adma.200690020 · Cited by 452

Biological Designer Self-Assembling Peptide Nanofiber Scaffolds Significantly Enhance Osteoblast Proliferation, Differentiation and 3-D Migration

Horii, A., Wang, X., Gelain, F., & Zhang, S. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000190 · Cited by 449

Optical Rotation And The Conformation Of Polypeptides And Proteins

Urnes, P., & Doty, P. (1962) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60033-9 · Cited by 448

Formation of Closed-Cage Nanostructures by Self-Assembly of Aromatic Dipeptides

Reches, M., & Gazit, E. (2004) · Nano Letters · doi:10.1021/nl035159z · Cited by 447

Natural and Synthetic Biomedical Polymers

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