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For: 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: 4.0] [Reference Citation Analysis]
Number Citing Articles
1 Colberg M, Schofield J. Configurational entropy, transition rates, and optimal interactions for rapid folding in coarse-grained model proteins. J Chem Phys 2022;157:125101. [PMID: 36182418 DOI: 10.1063/5.0098612] [Reference Citation Analysis]
2 Naudin EA, Albanese KI, Smith AJ, Mylemans B, Baker EG, Weiner OD, Andrews DM, Tigue N, Savery NJ, Woolfson DN. From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles.. [DOI: 10.1101/2022.08.04.502660] [Reference Citation Analysis]
3 Tobola F, Wiltschi B. One, two, many: Strategies to alter the number of carbohydrate binding sites of lectins. Biotechnol Adv 2022;:108020. [PMID: 35868512 DOI: 10.1016/j.biotechadv.2022.108020] [Reference Citation Analysis]
4 Tenorio CA, Parker JB, Blaber M. Functionalization of a symmetric protein scaffold: Redundant folding nuclei and alternative oligomeric folding pathways. Protein Science 2022;31. [DOI: 10.1002/pro.4301] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
5 D'Alessandro-Gabazza CN, Yasuma T, Kobayashi T, Toda M, Abdel-Hamid AM, Fujimoto H, Hataji O, Nakahara H, Takeshita A, Nishihama K, Okano T, Saiki H, Okano Y, Tomaru A, Fridman D'Alessandro V, Shiraishi M, Mizoguchi A, Ono R, Ohtsuka J, Fukumura M, Nosaka T, Mi X, Shukla D, Kataoka K, Kondoh Y, Hirose M, Arai T, Inoue Y, Yano Y, Mackie RI, Cann I, Gabazza EC. Inhibition of lung microbiota-derived proapoptotic peptides ameliorates acute exacerbation of pulmonary fibrosis. Nat Commun 2022;13:1558. [PMID: 35322016 DOI: 10.1038/s41467-022-29064-3] [Reference Citation Analysis]
6 Madhavan M, Mustafa S. Systems biology–the transformative approach to integrate sciences across disciplines: Systems Biology: Integrating Biological Sciences. Physical Sciences Reviews 2022;0. [DOI: 10.1515/psr-2021-0102] [Reference Citation Analysis]
7 Heling LWHJ, Banijamali SE, Satarifard V, Mashaghi A. Programmed Polymer Folding. Topological Polymer Chemistry 2022. [DOI: 10.1007/978-981-16-6807-4_11] [Reference Citation Analysis]
8 Naudin EA, Albanese KI, Smith AJ, Mylemans B, Baker EG, Weiner OD, Andrews DM, Tigue N, Savery NJ, Woolfson DN. From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles. Chem Sci . [DOI: 10.1039/d2sc04479j] [Reference Citation Analysis]
9 Mills EM, Barlow VL, Jones AT, Tsai Y. Development of mammalian cell logic gates controlled by unnatural amino acids. Cell Reports Methods 2021;1:100073. [DOI: 10.1016/j.crmeth.2021.100073] [Cited by in Crossref: 1] [Article Influence: 0.5] [Reference Citation Analysis]
10 Rhys GG, Dawson WM, Beesley JL, Martin FJO, Brady RL, Thomson AR, Woolfson DN. How Coiled-Coil Assemblies Accommodate Multiple Aromatic Residues. Biomacromolecules 2021;22:2010-9. [PMID: 33881308 DOI: 10.1021/acs.biomac.1c00131] [Cited by in Crossref: 1] [Cited by in F6Publishing: 3] [Article Influence: 0.5] [Reference Citation Analysis]
11 Božič Abram S, Gradišar H, Aupič J, Round AR, Jerala R. Triangular in Vivo Self-Assembling Coiled-Coil Protein Origami. ACS Chem Biol 2021;16:310-5. [PMID: 33476117 DOI: 10.1021/acschembio.0c00812] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 2.0] [Reference Citation Analysis]
12 Rhys GG, Dawson WM, Beesley JL, Martin FJO, Brady RL, Thomson AR, Woolfson DN. How coiled-coil assemblies accommodate multiple aromatic residues.. [DOI: 10.1101/2021.02.01.429152] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]