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For: Wu Y, Collier JH. α-Helical coiled-coil peptide materials for biomedical applications. Wiley Interdiscip Rev Nanomed Nanobiotechnol 2017;9. [PMID: 27597649 DOI: 10.1002/wnan.1424] [Cited by in Crossref: 34] [Cited by in F6Publishing: 35] [Article Influence: 5.7] [Reference Citation Analysis]
Number Citing Articles
1 Then A, Zhang H, Ibrahim B, Schuster S. Bioinformatics Analysis of the Periodicity in Proteins with Coiled-Coil Structure—Enumerating All Decompositions of Sequence Periods. IJMS 2022;23:8692. [DOI: 10.3390/ijms23158692] [Reference Citation Analysis]
2 Qing R, Hao S, Smorodina E, Jin D, Zalevsky A, Zhang S. Protein Design: From the Aspect of Water Solubility and Stability. Chem Rev 2022. [PMID: 35921495 DOI: 10.1021/acs.chemrev.1c00757] [Cited by in Crossref: 1] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
3 Li Y, Champion JA. Self-assembling Nanocarriers from Engineered Proteins: Design, Functionalization, and Application for Drug Delivery. Advanced Drug Delivery Reviews 2022. [DOI: 10.1016/j.addr.2022.114462] [Reference Citation Analysis]
4 Hao Z, Li H, Wang Y, Hu Y, Chen T, Zhang S, Guo X, Cai L, Li J. Supramolecular Peptide Nanofiber Hydrogels for Bone Tissue Engineering: From Multihierarchical Fabrications to Comprehensive Applications. Adv Sci (Weinh) 2022;9:e2103820. [PMID: 35128831 DOI: 10.1002/advs.202103820] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 7.0] [Reference Citation Analysis]
5 Gray VP, Amelung CD, Duti IJ, Laudermilch EG, Letteri RA, Lampe KJ. Biomaterials via peptide assembly: Design, characterization, and application in tissue engineering. Acta Biomater 2022;140:43-75. [PMID: 34710626 DOI: 10.1016/j.actbio.2021.10.030] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 8.0] [Reference Citation Analysis]
6 Chu S, Wang AL, Bhattacharya A, Montclare JK. Protein Based Biomaterials for Therapeutic and Diagnostic Applications. Prog Biomed Eng (Bristol) 2022;4:012003. [PMID: 34950852 DOI: 10.1088/2516-1091/ac2841] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
7 Wong KM, Robang AS, Lint AH, Wang Y, Dong X, Xiao X, Seroski DT, Liu R, Shao Q, Hudalla GA, Hall CK, Paravastu AK. Engineering β-Sheet Peptide Coassemblies for Biomaterial Applications. J Phys Chem B 2021;125:13599-609. [PMID: 34905370 DOI: 10.1021/acs.jpcb.1c04873] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
8 Dhankher A, Lv W, Studstill WT, Champion JA. Coiled coil exposure and histidine tags drive function of an intracellular protein drug carrier. J Control Release 2021;339:248-58. [PMID: 34563592 DOI: 10.1016/j.jconrel.2021.09.026] [Cited by in Crossref: 4] [Cited by in F6Publishing: 5] [Article Influence: 4.0] [Reference Citation Analysis]
9 O'Neill CL, Shrimali PC, Clapacs ZP, Files MA, Rudra JS. Peptide-based supramolecular vaccine systems. Acta Biomater 2021;133:153-67. [PMID: 34010691 DOI: 10.1016/j.actbio.2021.05.003] [Cited by in Crossref: 9] [Cited by in F6Publishing: 10] [Article Influence: 9.0] [Reference Citation Analysis]
10 Gil-Garcia M, Ventura S. Coiled-Coil Based Inclusion Bodies and Their Potential Applications. Front Bioeng Biotechnol 2021;9:734068. [PMID: 34485264 DOI: 10.3389/fbioe.2021.734068] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
11 Babi J, Zhu L, Lin A, Uva A, El‐haddad H, Peloewetse A, Tran H. Self‐assembled free‐floating nanomaterials from sequence‐defined polymers. Journal of Polymer Science 2021;59:2378-404. [DOI: 10.1002/pol.20210366] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
12 Harder-Viddal C, Heide F, Roshko RM, Stetefeld J. Molecular dynamics simulations of ortho-carborane nano-diamond storage within the nonpolar channel cavities of a right-handed coiled-coil tetrabrachion nanotube. Comput Struct Biotechnol J 2021;19:3531-41. [PMID: 34194676 DOI: 10.1016/j.csbj.2021.06.010] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
13 Shen MJ, Olsthoorn RCL, Zeng Y, Bakkum T, Kros A, Boyle AL. Magnetic-Activated Cell Sorting Using Coiled-Coil Peptides: An Alternative Strategy for Isolating Cells with High Efficiency and Specificity. ACS Appl Mater Interfaces 2021;13:11621-30. [PMID: 33656313 DOI: 10.1021/acsami.0c22185] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
14 Nguyen QD, Kikuchi K, Maity B, Ueno T. The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design. Int J Mol Sci 2021;22:1934. [PMID: 33669238 DOI: 10.3390/ijms22041934] [Cited by in Crossref: 11] [Cited by in F6Publishing: 12] [Article Influence: 11.0] [Reference Citation Analysis]
15 Thota CK, Mikolajczak DJ, Roth C, Koksch B. Enhancing Antimicrobial Peptide Potency through Multivalent Presentation on Coiled-Coil Nanofibrils. ACS Med Chem Lett 2021;12:67-73. [PMID: 33488966 DOI: 10.1021/acsmedchemlett.0c00425] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
16 Curtis RW, Chmielewski J. A comparison of the collagen triple helix and coiled‐coil peptide building blocks on metal ion‐mediated supramolecular assembly. Peptide Science 2021;113. [DOI: 10.1002/pep2.24190] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 2.5] [Reference Citation Analysis]
17 Gupta S, Singh I, Sharma AK, Kumar P. Ultrashort Peptide Self-Assembly: Front-Runners to Transport Drug and Gene Cargos. Front Bioeng Biotechnol 2020;8:504. [PMID: 32548101 DOI: 10.3389/fbioe.2020.00504] [Cited by in Crossref: 23] [Cited by in F6Publishing: 25] [Article Influence: 11.5] [Reference Citation Analysis]
18 Park WM. Coiled-Coils: the Molecular Zippers that Self-Assemble Protein Nanostructures. Int J Mol Sci 2020;21:E3584. [PMID: 32438665 DOI: 10.3390/ijms21103584] [Cited by in Crossref: 9] [Cited by in F6Publishing: 10] [Article Influence: 4.5] [Reference Citation Analysis]
19 Zhou W, Šmidlehner T, Jerala R. Synthetic biology principles for the design of protein with novel structures and functions. FEBS Lett 2020;594:2199-212. [PMID: 32324903 DOI: 10.1002/1873-3468.13796] [Cited by in Crossref: 12] [Cited by in F6Publishing: 12] [Article Influence: 6.0] [Reference Citation Analysis]
20 More SH, Ganesh KN. Spiegelmeric 4 R / S ‐hydroxy/amino‐L/D‐prolyl collagen peptides: conformation and morphology of self‐assembled structures. Pept Sci 2020;112. [DOI: 10.1002/pep2.24140] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.7] [Reference Citation Analysis]
21 Israeli B, Vaserman L, Amiram M. Multi‐Site Incorporation of Nonstandard Amino Acids into Protein‐Based Biomaterials. Isr J Chem 2020;60:1118-28. [DOI: 10.1002/ijch.201900043] [Cited by in Crossref: 7] [Cited by in F6Publishing: 7] [Article Influence: 2.3] [Reference Citation Analysis]
22 Sis MJ, Webber MJ. Drug Delivery with Designed Peptide Assemblies. Trends in Pharmacological Sciences 2019;40:747-62. [DOI: 10.1016/j.tips.2019.08.003] [Cited by in Crossref: 49] [Cited by in F6Publishing: 43] [Article Influence: 16.3] [Reference Citation Analysis]
23 Nesterenko Y, Hill CJ, Fleming JR, Murray P, Mayans O. The ZT Biopolymer: A Self-Assembling Protein Scaffold for Stem Cell Applications. Int J Mol Sci 2019;20:E4299. [PMID: 31484291 DOI: 10.3390/ijms20174299] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.3] [Reference Citation Analysis]
24 Fry HC, Silveira GDQ, Cohn HM, Lee B. Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide. Langmuir 2019;35:8961-7. [DOI: 10.1021/acs.langmuir.9b00424] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 1.3] [Reference Citation Analysis]
25 Liu R, Hudalla GA. Using Self-Assembling Peptides to Integrate Biomolecules into Functional Supramolecular Biomaterials. Molecules 2019;24:E1450. [PMID: 31013712 DOI: 10.3390/molecules24081450] [Cited by in Crossref: 28] [Cited by in F6Publishing: 28] [Article Influence: 9.3] [Reference Citation Analysis]
26 Roth A, Murschel F, Latreille P, Martinez VA, Liberelle B, Banquy X, De Crescenzo G. Coiled Coil Affinity-Based Systems for the Controlled Release of Biofunctionalized Gold Nanoparticles from Alginate Hydrogels. Biomacromolecules 2019;20:1926-36. [DOI: 10.1021/acs.biomac.9b00137] [Cited by in Crossref: 15] [Cited by in F6Publishing: 15] [Article Influence: 5.0] [Reference Citation Analysis]
27 Rink WM, Thomas F. De Novo Designed α-Helical Coiled-Coil Peptides as Scaffolds for Chemical Reactions. Chem Eur J 2019;25:1665-77. [DOI: 10.1002/chem.201802849] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 2.0] [Reference Citation Analysis]
28 Xu D, Tang X, Wu X, Yu D, Tang P, Wang X. Anti-Breast Cancer Activity of Latroeggtoxin-V Mined from the Transcriptome of Spider Latrodectus tredecimguttatus Eggs. Toxins (Basel) 2018;10:E451. [PMID: 30400202 DOI: 10.3390/toxins10110451] [Cited by in Crossref: 2] [Cited by in F6Publishing: 3] [Article Influence: 0.5] [Reference Citation Analysis]
29 Mehrban N, Bowen J, Tait A, Darbyshire A, Virasami AK, Lowdell MW, Birchall MA. Silsesquioxane polymer as a potential scaffold for laryngeal reconstruction. Mater Sci Eng C Mater Biol Appl 2018;92:565-74. [PMID: 30184783 DOI: 10.1016/j.msec.2018.07.003] [Cited by in Crossref: 8] [Cited by in F6Publishing: 7] [Article Influence: 2.0] [Reference Citation Analysis]
30 Yin L, Agustinus AS, Yuvienco C, Minashima T, Schnabel NL, Kirsch T, Montclare JK. Engineered Coiled-Coil Protein for Delivery of Inverse Agonist for Osteoarthritis. Biomacromolecules 2018;19:1614-24. [PMID: 29601728 DOI: 10.1021/acs.biomac.8b00158] [Cited by in Crossref: 11] [Cited by in F6Publishing: 13] [Article Influence: 2.8] [Reference Citation Analysis]
31 Oba M, Ito C, Tanaka M. Effects of five-membered ring amino acid incorporation into peptides for coiled coil formation. Bioorg Med Chem Lett 2018;28:875-7. [PMID: 29433922 DOI: 10.1016/j.bmcl.2018.02.002] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis]
32 Fujita S, Matsuura K. Self-assembled artificial viral capsids bearing coiled-coils at the surface. Org Biomol Chem 2017;15:5070-7. [PMID: 28574073 DOI: 10.1039/c7ob00998d] [Cited by in Crossref: 17] [Cited by in F6Publishing: 18] [Article Influence: 4.3] [Reference Citation Analysis]
33 Thomas F, Niitsu A, Oregioni A, Bartlett GJ, Woolfson DN. Conformational Dynamics of Asparagine at Coiled-Coil Interfaces. Biochemistry 2017;56:6544-54. [PMID: 29166010 DOI: 10.1021/acs.biochem.7b00848] [Cited by in Crossref: 19] [Cited by in F6Publishing: 19] [Article Influence: 3.8] [Reference Citation Analysis]
34 Wu Y, Norberg PK, Reap EA, Congdon KL, Fries CN, Kelly SH, Sampson JH, Conticello VP, Collier JH. A Supramolecular Vaccine Platform Based on α-Helical Peptide Nanofibers. ACS Biomater Sci Eng 2017;3:3128-32. [PMID: 30740520 DOI: 10.1021/acsbiomaterials.7b00561] [Cited by in Crossref: 54] [Cited by in F6Publishing: 57] [Article Influence: 10.8] [Reference Citation Analysis]