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1

Hori, K., and T. Kurotsu. "Characterization of Gramicidin S Synthetase Aggregation Substance: Control of Gramicidin S Synthesis by Its Product, Gramicidin S." Journal of Biochemistry 122, no. 3 (1997): 606–15. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a021796.

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2

Drannikov, A. A., I. S. Vatlin, M. Е. Trusova, et al. "Investigation of Colloidal Structure and Biopharmaceutical Properties of New Antibacterial Composition of Gramicidin S." Drug development & registration 10, no. 4 (2021): 129–37. http://dx.doi.org/10.33380/2305-2066-2021-10-4-129-137.

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Introduction. Gramicidin S has been conventionally manufactured as buccal tablets. However, in the past decade, the interest in the development of spray formulations has been growing. Those formulations contain excipients that enhance the solubility of the antibiotic in water solutions. However, the real structure of gramicidin S containing sprays remains unrevealed.Aim. Investigation of colloidal structure and biopharmaceutical properties of new gramicidin S antibacterial composition.Materials and methods. The composition sample was obtained using gramicidin S dihydrochloride, propylene glyco
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3

Cox, J. A., M. Milos, and M. Comte. "High-affinity formation of a 2:1 complex between gramicidin S and calmodulin." Biochemical Journal 246, no. 2 (1987): 495–502. http://dx.doi.org/10.1042/bj2460495.

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Two molecules of gramicidin S, a very rigid cyclic decapeptide rich in beta-sheet structure, can bind in a Ca2+-dependent way to a calmodulin molecule in the presence as well as in the absence of 4 M-urea. The flow-microcalorimetric titration of 25 microM-calmodulin with gramicidin S at 25 degrees C is endothermic for 21.3 kJ.mol-1; the enthalpy change is strictly linear up to a ratio of 2, indicating that the affinity constant for binding of the second gramicidin S is at least 10(7) M-1. In 4 M-urea the peptide quantitatively displaces seminalplasmin from calmodulin, as monitored by tryptopha
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4

Nozaki, Sukekatsu, and Ichiro Muramatsu. "Natural Homologs of Gramicidin S. II. Synthesis of Gramicidin S-2 and S-3." Bulletin of the Chemical Society of Japan 58, no. 1 (1985): 331–35. http://dx.doi.org/10.1246/bcsj.58.331.

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5

Alabedalkarim, N. M., V. P. Berest, N. M. Moiseieva, G. A. Bozhok, and T. P. Bondarenko. "The antimicrobial peptide gramicidin S alters proliferation and inhibits adhesion of L929 cell line fibroblasts." 49, no. 49 (August 11, 2023): 43–60. http://dx.doi.org/10.26565/2075-3810-2023-49-04.

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Background: Natural antimicrobial peptides are used in the fight against pathogens resistant to existing synthetic antibiotics. The non-specific mechanism of cytostatic action of antimicrobial peptides, in particular gramicidin S, against bacteria is also effective for damaging the cells of neoplasms. The existence of such a property in a registered antibiotic will indicate its antineoplastic potential and can be used to expand the spectrum of its therapeutic application. Aim of work is to clarify the possible antitumor effect of the antimicrobial peptide gramicidin S. Materials and Methods: U
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6

Nagamurthi, G., and S. Rambhav. "Gramicidin-S: Structure-activity relationship." Journal of Biosciences 7, no. 3-4 (1985): 323–29. http://dx.doi.org/10.1007/bf02716794.

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7

Arai, Toru, Takashi Imachi, Tamaki Kato, H. Iyehara Ogawa, Tsutomu Fujimoto, and Norikazu Nishino. "Synthesis of [Hexafluorovalyl1,1′]gramicidin S." Bulletin of the Chemical Society of Japan 69, no. 5 (1996): 1383–89. http://dx.doi.org/10.1246/bcsj.69.1383.

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8

Kalyvas, John T., Yifei Wang, Ornella Romeo, John R. Horsley, and Andrew D. Abell. "Broad-Spectrum Gramicidin S Derivatives with Potent Activity Against Multidrug-Resistant Gram-Negative ESKAPE Pathogens." Antibiotics 14, no. 5 (2025): 423. https://doi.org/10.3390/antibiotics14050423.

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Background/Objectives: Multidrug-resistant Gram-negative ESKAPE pathogens, including E. coli, K. pneumoniae, P. aeruginosa, and A. baumannii, pose a significant global health threat. Gramicidin S, a potent cyclic antimicrobial peptide, is largely ineffective against these bacteria, and its high haemolytic toxicity limits its clinical usage. This study reports on several novel gramicidin S analogues with improved efficacy and safety profiles against multidrug-resistant Gram-negative bacteria. Methods: A total of 19 gramicidin S derivatives were synthesised using Fmoc-based solid-phase peptide s
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9

Zhang, Lijuan, Pawandeep Dhillon, Hong Yan, Susan Farmer, and Robert E. W. Hancock. "Interactions of Bacterial Cationic Peptide Antibiotics with Outer and Cytoplasmic Membranes ofPseudomonas aeruginosa." Antimicrobial Agents and Chemotherapy 44, no. 12 (2000): 3317–21. http://dx.doi.org/10.1128/aac.44.12.3317-3321.2000.

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ABSTRACT Polymyxins B and E1 and gramicidin S are bacterium-derived cationic antimicrobial peptides. The polymyxins were more potent than gramicidin S against Pseudomonas aeruginosa, with MICs of 0.125 to 0.25 and 8 μg/ml, respectively. These peptides differed in their affinities for binding to lipopolysaccharide, but all were able to permeabilize the outer membrane of wild-type P. aeruginosaPAO1 strain H103, suggesting differences in their mechanisms of self-promoted uptake. Gramicidin S caused rapid depolarization of the bacterial cytoplasmic membrane at concentrations at which no killing wa
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10

Kleinkauf, H., and H. Von Döhren. "Applications of peptide synthetases in the synthesis of peptide analogues." Acta Biochimica Polonica 44, no. 4 (1997): 839–47. http://dx.doi.org/10.18388/abp.1997_4389.

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Enzymatically formed peptides show positional variations as well as highly conserved amino acids. In the cases of gramicidin S, tyrocidine, linear gramicidins, enniatins, echinocandins and viridogrisein in vivo and in vitro studies indicate substrate selection at the level of amino acid activation as a major control step. Evidence for proof-reading steps beyond activation has been obtained in penicillin and cyclosporin biosynthesis. Activated substrate analogues may promote the formation of side products such as dipeptides and cyclodipeptides. Modifications of intermediates, such as N-methylat
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11

YONEZAWA, Hiroo, Koji OKAMOTO, Kazuhiko TOMOKIYO, and Nobuo IZUMIYA. "Mode of Antibacterial Action by Gramicidin S." Journal of Biochemistry 100, no. 5 (1986): 1253–59. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a121831.

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12

TAMAKI, MAKOTO. "Hybrid Analogues of Gramicidin S and Gratisin." Journal of Antibiotics 57, no. 9 (2004): 609–13. http://dx.doi.org/10.7164/antibiotics.57.609.

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13

Nir-Paz, Ran, Marie-Christine Prévost, Pierre Nicolas, Alain Blanchard, and Henri Wróblewski. "Susceptibilities of Mycoplasma fermentans and Mycoplasma hyorhinis to Membrane-Active Peptides and Enrofloxacin in Human Tissue Cell Cultures." Antimicrobial Agents and Chemotherapy 46, no. 5 (2002): 1218–25. http://dx.doi.org/10.1128/aac.46.5.1218-1225.2002.

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ABSTRACT Mycoplasmas, which are bacteria that are devoid of a cell wall and which belong to the class Mollicutes, are pathogenic for humans and animals and are frequent contaminants of tissue cell cultures. Although contamination of cultures with mycoplasma can easily be monitored with fluorescent dyes that stain DNA and/or with molecular probes, protection and decontamination of cultures remain serious challenges. In the present work, we investigated the susceptibilities of Mycoplasma fermentans and Mycoplasma hyorhinis to the membrane-active peptides alamethicin, dermaseptin B2, gramicidin S
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14

Chen, Daoyuan, Wenjing Qin, Gesi Wen та ін. "Dissociation of haemolytic and oligomer-preventing activities of gramicidin S derivatives targeting the amyloid-β N-terminus". Chemical Communications 53, № 100 (2017): 13340–43. http://dx.doi.org/10.1039/c7cc08180d.

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15

Fang, Shang-Ting, Shu-Hsiang Huang, Chin-Hao Yang, Jen-Wen Liou, Hemalatha Mani, and Yi-Cheng Chen. "Effects of Calcium Ions on the Antimicrobial Activity of Gramicidin A." Biomolecules 12, no. 12 (2022): 1799. http://dx.doi.org/10.3390/biom12121799.

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Gramicidin A (gA) is a linear antimicrobial peptide that can form a channel and specifically conduct monovalent cations such as H+ across the lipid membrane. The antimicrobial activity of gA is associated with the formation of hydroxyl free radicals and the imbalance of NADH metabolism, possibly a consequence caused by the conductance of cations. The ion conductivity of gramicidin A can be blocked by Ca2+ ions. However, the effect of Ca2+ ions on the antimicrobial activity of gA is unclear. To unveil the role of Ca2+ ions, we examined the effect of Ca2+ ions on the antimicrobial activity of gr
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16

Walsh, Christopher T. "Insights into the chemical logic and enzymatic machinery of NRPS assembly lines." Natural Product Reports 33, no. 2 (2016): 127–35. http://dx.doi.org/10.1039/c5np00035a.

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17

Kotmale, Amol S., Ekta Sangtani, Rajesh G. Gonnade, et al. "Conformational studies of Ant–Pro motif-incorporated cyclic peptides: gramicidin S and avellanin." New Journal of Chemistry 42, no. 2 (2018): 1197–201. http://dx.doi.org/10.1039/c7nj03701e.

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Conformational studies suggest that an Ant<sup>D</sup>Pro motif-incorporated synthetic gramicidin S analog retains β-sheet conformation, while its truncated analog avellanin disturbs the β-sheet conformation.
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18

VATER, Joachim, Wilhelm SCHLUMBOHM, Johann SALNIKOW, et al. "Proteinchemical and Kinetic Features of Gramicidin S Synthetase." Biological Chemistry Hoppe-Seyler 370, no. 2 (1989): 1013–18. http://dx.doi.org/10.1515/bchm3.1989.370.2.1013.

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19

Tanimoto, Yasusuke, Yuko Ichikawa, Yoko Yasuda, and Kunio Tochikubo. "Permeability of dormant spores ofBacillus subtilisto gramicidin S." FEMS Microbiology Letters 136, no. 2 (1996): 151–56. http://dx.doi.org/10.1111/j.1574-6968.1996.tb08041.x.

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20

Grotenbreg, Gijsbert M., Martin D. Witte, Peter A. V. van Hooft, et al. "Synthesis and biological evaluation of gramicidin S dimers." Org. Biomol. Chem. 3, no. 2 (2005): 233–38. http://dx.doi.org/10.1039/b414618b.

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21

Hackl, Ellen V., Vladimir P. Berest, and Sergey V. Gatash. "Interaction of polypeptide antibiotic gramicidin S with platelets." Journal of Peptide Science 18, no. 12 (2012): 748–54. http://dx.doi.org/10.1002/psc.2461.

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22

Kalinovych, Viacheslav, and Volodymyr Berest. "Similarity of Gramicidin S and Cryoprotectant Polyethylene Glycol Membranotropic Effects." Problems of Cryobiology and Cryomedicine 29, no. 2 (2019): 161. http://dx.doi.org/10.15407/cryo29.02.161.

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23

YAGI, YOSHIKO, SHUNSAKU KIMURA, and YUKIO IMANISHI. "Interaction of gramicidin S analogs with lipid bilayer membrane." International Journal of Peptide and Protein Research 36, no. 1 (2009): 18–25. http://dx.doi.org/10.1111/j.1399-3011.1990.tb00079.x.

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24

Niidome, Takuro, Hiroto Murakami, Masahito Kawazoe, et al. "Carbohydrate recognition of gramicidin S analogues in aqueous medium." Bioorganic & Medicinal Chemistry Letters 11, no. 14 (2001): 1893–96. http://dx.doi.org/10.1016/s0960-894x(01)00322-5.

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25

Fang, A., D. L. Pierson, S. K. Mishra, D. W. Koenig, and A. L. Demain. "Gramicidin S Production by Bacillus brevis in Simulated Microgravity." Current Microbiology 34, no. 4 (1997): 199–204. http://dx.doi.org/10.1007/s002849900168.

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26

Azuma, T., and A. L. Demain. "Interactions between gramicidin S and its producer,Bacillus brevis." Journal of Industrial Microbiology 17, no. 1 (1996): 56–61. http://dx.doi.org/10.1007/bf01570150.

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27

Tamaki, Makoto, Ichiro Sasaki, Yuki Nakao, Mitsuno Shindo, Masahiro Kimura, and Yoshiki Uchida. "Gramicidin S analogs having six basic amino acid residues." Journal of Antibiotics 62, no. 10 (2009): 597–99. http://dx.doi.org/10.1038/ja.2009.81.

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28

Babii, Oleg, Segrii Afonin, Marina Berditsch, et al. "Switching the Antimicrobial Activity of Gramicidin S by Light." Biophysical Journal 106, no. 2 (2014): 442a. http://dx.doi.org/10.1016/j.bpj.2013.11.2490.

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29

Buchweitz, Olaf, and C. Paul Bianchi. "Myocardial magnesium transport: effect of gramicidin S and epinephrine." Life Sciences 55, no. 23 (1994): 1853–61. http://dx.doi.org/10.1016/0024-3205(94)90096-5.

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30

Tuin, Adriaan Willem, Dimitrios Konstantinos Palachanis, Annelies Buizert, et al. "Synthesis and Biological Evaluation of Novel Gramicidin S Analogues." European Journal of Organic Chemistry 2009, no. 25 (2009): 4231–41. http://dx.doi.org/10.1002/ejoc.200900460.

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31

Yamada, K., K. Ando, Y. I. Takahashi, H. Yamamura, S. Araki, and M. Kawai. "Convenient preparation of [Orn(Tfa)2 ]- and [Orn(Boc)2 , Orn(Tfa)2′ ]gramicidin S, versatile unsymmetrically protected derivatives of gramicidin S." Journal of Peptide Research 54, no. 2 (1999): 168–73. http://dx.doi.org/10.1034/j.1399-3011.1999.00100.x.

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32

Богатов, Виктор, Victor Bogatov, Екатерина Кулаева, et al. "ANALYSIS TREATMENT OF EXPERIMENTAL ALVEOLITIS OF THE JAW IN RATS WITH THE USE OF NIZKOSOLEVA LASER RADIATION AND THE MEDICINAL PRODUCT ON THE BASIS OF "GRAMICIDIN S»." Actual problems in dentistry 15, no. 1 (2019): 74–79. http://dx.doi.org/10.18481/2077-7566-2019-15-1-74-79.

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Background. The article deals with the problem of jaw alveolitis on the background of alveolar sockets infection on the example of experimental alveolitis in rats. The authors obtained and analyzed the results of treatment of alveolitis with the use of light emitting diode radiation radiation and a medical based on "Gramicidin C" and the classical method of treatment of alveolitis by microscopy of histological material Objectives ― study and prove that the infection of the well is a significant factor in the development of the alveolitis of the alveolar sockets on the example of experimental a
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33

Azcona, Juan I., Rosario Martín, Miguel A. Asensio, Pablo E. Hernández, and Bernabé Sanz. "Heat stable proteinase fromPseudomonas fluorescensAH-70: purification by affinity chromatography on cyclopeptide antibiotics." Journal of Dairy Research 55, no. 2 (1988): 217–26. http://dx.doi.org/10.1017/s0022029900026042.

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SummaryA heat stable extracellular proteinase from the psychrotrophPseudomonas fluorescensAH-70 was purified to electrophoretic homogeneity by affinity chromatography on a gramicidin S–Sepharose-4B column. Bacitracin linked to Sepharose-4B was unable to retain any proteolytic activity, whereas the same antibiotic bound to AH-Sepharose-4B retained ~ 25% of the total activity. The purification procedure on the gramicidin S–Sepharose-4B column was easy to perform, fast and reproducible; it resulted in a 207-fold increase in the specific activity and a yield of 41% of the original activity. The pu
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34

Ishikawa, Fumihiro, Sho Konno, Hideaki Kakeya, and Genzoh Tanabe. "Development of a chemical scaffold for inhibiting nonribosomal peptide synthetases in live bacterial cells." Beilstein Journal of Organic Chemistry 20 (February 26, 2024): 445–51. http://dx.doi.org/10.3762/bjoc.20.39.

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The adenylation (A) domain is essential for non-ribosomal peptide synthetases (NRPSs), which synthesize various peptide-based natural products, including virulence factors, such as siderophores and genotoxins. Hence, the inhibition of A-domains could attenuate the virulence of pathogens. 5’-O-N-(Aminoacyl or arylacyl)sulfamoyladenosine (AA-AMS) is a bisubstrate small-molecule inhibitor of the A-domains of NRPSs. However, the bacterial cell permeability of AA-AMS is typically a problem owing to its high hydrophilicity. In this study, we investigated the influence of a modification of 2′-OH in t
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35

Radtsig, E. Yu, and A. V. Gurov. "Sore throat. Crossing problems and finding solutions." Russian Journal of Woman and Child Health 5, no. 3 (2022): 228–36. http://dx.doi.org/10.32364/2618-8430-2022-5-3-228-236.

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The article presents a brief review of the current issues relating to the treatment of acute infectious inflammatory diseases associated with sore throat. Painful throat is one of the most common reasons for the administration of systemic antibacterial drugs as a baseline therapy which, in turn, may facilitate a rise in antibiotic resistance. Recently the focus has shifted to the antibacterial therapy impact on the qualitative and quantitative composition of the microbiota. The review elucidates the opportunities of successful etiotropic therapy amid a low risk of the antibiotic resistance dev
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36

Asano, Akiko, Shiori Matsuoka, Chisato Minami, Takuma Kato та Mitsinobu Doi. "[Leu2]Gramicidin S preserves the structural properties of its parent peptide and forms helically aligned β-sheets". Acta Crystallographica Section C Structural Chemistry 75, № 10 (2019): 1336–43. http://dx.doi.org/10.1107/s2053229619011872.

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For crystallographic analysis, Leu was substituted for Orn in Gramicidin S (LGS) to suppress interactions with hydrophilic solvent molecules, which increased the flexibility of the Orn side chains, leading to disorder within the crystals. The asymmetric unit (C62H94N10O10·1.296C3H8O·1.403H2O) contains three LGS molecules (A, B and C) forming β-turn and intramolecular β-sheet structures. With the exception of one motif in molecule C, D-Phe-Pro turn motifs (Phe is phenylalanine and Pro is proline) were classed as type II′ β-turns. The peptide backbones twist slightly to the right along the long
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37

ASANO, Akiko, and Mitsunobu DOI. "Crystal Structure of Gramicidin S Hydrochloride at 1.1 Å Resolution." X-ray Structure Analysis Online 35 (January 10, 2019): 1–2. http://dx.doi.org/10.2116/xraystruct.35.1.

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38

Yamada, Keiichi, Shun-suke Shinoda, Hiroyuki Oku, Keiko Komagoe, Takashi Katsu, and Ryoichi Katakai. "Synthesis of Low-Hemolytic Antimicrobial Dehydropeptides Based on Gramicidin S." Journal of Medicinal Chemistry 49, no. 26 (2006): 7592–95. http://dx.doi.org/10.1021/jm061051v.

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39

Hoyer, Katharina M., Christoph Mahlert, and Mohamed A. Marahiel. "The Iterative Gramicidin S Thioesterase Catalyzes Peptide Ligation and Cyclization." Chemistry & Biology 14, no. 1 (2007): 13–22. http://dx.doi.org/10.1016/j.chembiol.2006.10.011.

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40

Katsu, Takashi, Hideki Kobayashi, and Yuzaburo Fujita. "Mode of action of gramicidin S on Escherichia coli membrane." Biochimica et Biophysica Acta (BBA) - Biomembranes 860, no. 3 (1986): 608–19. http://dx.doi.org/10.1016/0005-2736(86)90560-2.

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41

Katsu, Takashi, Hideki Kobayashi, Takashi Hirota, Yuzaburo Fujita, Kazuki Sato, and Ukon Nagai. "Structure-activity relationship of gramicidin S analogues on membrane permeability." Biochimica et Biophysica Acta (BBA) - Biomembranes 899, no. 2 (1987): 159–70. http://dx.doi.org/10.1016/0005-2736(87)90396-8.

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42

Swierstra, J., V. Kapoerchan, A. Knijnenburg, A. van Belkum, and M. Overhand. "Structure, toxicity and antibiotic activity of gramicidin S and derivatives." European Journal of Clinical Microbiology & Infectious Diseases 35, no. 5 (2016): 763–69. http://dx.doi.org/10.1007/s10096-016-2595-y.

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43

Smirnov, S., A. Belashov, and O. Demin. "Optimization of antimicrobial drug gramicidin S dosing regime using biosimulations." European Journal of Pharmaceutical Sciences 36, no. 1 (2009): 105–9. http://dx.doi.org/10.1016/j.ejps.2008.10.017.

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44

Ayres, Lee, Gijsbert M. Grotenbreg, Gijsbert A. van der Marel, Herman S. Overkleeft, Mark Overhand, and Jan C. M. van Hest. "Synthesis and Controlled Polymerisation of a Novel Gramicidin S Analogue." Macromolecular Rapid Communications 26, no. 16 (2005): 1336–40. http://dx.doi.org/10.1002/marc.200500303.

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45

MATSUSHIMA, SHINGO, and HITOSHI SHICHI. "Possible Mechanism of Immunosuppression by Gramicidin S of S Antigen-Induced Experimental Autoimmune Uveoretinitis." Journal of Ocular Pharmacology and Therapeutics 5, no. 3 (1989): 261–69. http://dx.doi.org/10.1089/jop.1989.5.261.

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46

Yamada, Keiichi, Masafumi Unno, Kyoko Kobayashi, et al. "Stereochemistry of Protected Ornithine Side Chains of Gramicidin S Derivatives: X-ray Crystal Structure of the Bis-Boc-tetra-N-methyl Derivative of Gramicidin S." Journal of the American Chemical Society 124, no. 43 (2002): 12684–88. http://dx.doi.org/10.1021/ja020307t.

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47

MacLeod, R. J., P. Lembessis, and J. R. Hamilton. "Effect of osmotic swelling on K+ conductance in jejunal crypt epithelial cells." American Journal of Physiology-Gastrointestinal and Liver Physiology 262, no. 6 (1992): G1021—G1026. http://dx.doi.org/10.1152/ajpgi.1992.262.6.g1021.

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To further elucidate differences in ion transport properties between jejunal crypt and villus cells, we compared the responses of purified cell suspensions to hypotonic stress using electronic cell sizing to evaluate volume changes and 86Rb and 36Cl efflux. After hypotonic swelling, villus enterocytes undergo a regulatory volume decrease (RVD) due to the loss of K+ and Cl- through volume-activated conductances. After 0.6x isotonic challenge in Na(+)-free medium, crypt cells exhibited only partial RVD, with t1/2 congruent to 15 min. The addition of a cation ionophore, gramicidin (0.25 microM),
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48

Datema, Klaas P., K. Peter Pauls, and Myer Bloom. "Deuterium nuclear magnetic resonance investigation of the exchangeable sites on gramicidin A and gramicidin S in multilamellar vesicles of dipalmitoylphosphatidylcholine." Biochemistry 25, no. 13 (1986): 3796–803. http://dx.doi.org/10.1021/bi00361a010.

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49

Tamaki, Makoto, Michiaki Takimoto, and Ichiro Muramatsu. "Synthesis of Gramicidin S Analogues Consisting of Fourteen Amino Acid Residues." Bulletin of the Chemical Society of Japan 61, no. 11 (1988): 3925–29. http://dx.doi.org/10.1246/bcsj.61.3925.

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50

Arai, Toru, Naoki Maruo, Yuko Sumida, Chie Korosue, and Norikazu Nishino. "Spatially close porphyrin pair linked by the cyclic peptide Gramicidin S." Chemical Communications, no. 16 (1999): 1503–4. http://dx.doi.org/10.1039/a902774b.

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