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Journal articles on the topic 'Helix'

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1

Regan, L. "Helix is a helix is a helix?" Proceedings of the National Academy of Sciences 94, no. 7 (1997): 2796–97. http://dx.doi.org/10.1073/pnas.94.7.2796.

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2

Ciarapica, Roberta, Jessica Rosati, Gianni Cesareni, and Sergio Nasi. "Molecular Recognition in Helix-Loop-Helix and Helix-Loop-Helix-Leucine Zipper Domains." Journal of Biological Chemistry 278, no. 14 (2003): 12182–90. http://dx.doi.org/10.1074/jbc.m211991200.

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3

Walther, Dirk, Clayton Springer, and Fred E. Cohen. "Helix-helix packing angle preferences for finite helix axes." Proteins: Structure, Function, and Genetics 33, no. 4 (1998): 457–59. http://dx.doi.org/10.1002/(sici)1097-0134(19981201)33:4<457::aid-prot1>3.0.co;2-l.

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4

Gibson, Toby J., Peter R. Sibbald, and Peter Rice. "Rop/Helix-loop-helix similarity." DNA Sequence 1, no. 3 (1991): 213–15. http://dx.doi.org/10.3109/10425179109020773.

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5

Croom, Anna, Kylie B. Manning, and Marcus Weck. "Supramolecular Helix–Helix Block Copolymers." Macromolecules 49, no. 19 (2016): 7117–28. http://dx.doi.org/10.1021/acs.macromol.6b01410.

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6

Camps-fabrer, H. "Helix." Encyclopédie berbère, no. 22 (January 1, 2000): 3426–28. http://dx.doi.org/10.4000/encyclopedieberbere.1712.

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7

Xin, Doris, Stephen Macke, Litian Ma, Jialin Liu, Shuchen Song, and Aditya Parameswaran. "HELIX." Proceedings of the VLDB Endowment 12, no. 4 (2018): 446–60. http://dx.doi.org/10.14778/3297753.3297763.

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8

Stefankiewicz, Artur R., André De Cian, and Jack Harrowfield. "Helix-helix interactions – homochirality and heterochirality." CrystEngComm 13, no. 24 (2011): 7207. http://dx.doi.org/10.1039/c1ce06081c.

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9

Preissner, R., A. Goede, and C. Frömmel. "Spare parts for helix–helix interaction." Protein Engineering, Design and Selection 12, no. 10 (1999): 825–32. http://dx.doi.org/10.1093/protein/12.10.825.

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10

Ben-Tal, N., and B. Honig. "Helix-helix interactions in lipid bilayers." Biophysical Journal 71, no. 6 (1996): 3046–50. http://dx.doi.org/10.1016/s0006-3495(96)79498-5.

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11

Kurochkina, Natalya, and Tsering Choekyi. "Helix–helix interfaces and ligand binding." Journal of Theoretical Biology 283, no. 1 (2011): 92–102. http://dx.doi.org/10.1016/j.jtbi.2011.05.014.

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12

Lemmon, Mark A., and Donald M. Engelman. "Helix-helix interactions inside lipid bilayers." Current Opinion in Structural Biology 2, no. 4 (1992): 511–18. http://dx.doi.org/10.1016/0959-440x(92)90080-q.

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13

Brennan, Richard G. "The winged-helix DNA-binding motif: Another helix-turn-helix takeoff." Cell 74, no. 5 (1993): 773–76. http://dx.doi.org/10.1016/0092-8674(93)90456-z.

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14

Zhang, Wei, Hongxing Lei, Shibasish Chowdhury, and Yong Duan. "Fs-21 Peptides Can Form Both Single Helix and Helix−Turn−Helix." Journal of Physical Chemistry B 108, no. 22 (2004): 7479–89. http://dx.doi.org/10.1021/jp037688x.

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15

Sundari, Sri, and Ahmad Ahsin Kusuma Mawardi. "Interaksi Penta-Helix terhadap Keinovasian Organisasi Startup dan Kinerja Inovasi Produk Agribisnis Berbasis Kopi." Jurnal Ilmiah Inovasi 24, no. 1 (2024): 15–20. http://dx.doi.org/10.25047/jii.v24i1.4068.

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Startup agribisnis berbasis produk turunan kopi Jember penting untuk ditumbuhkembangkan. Salah satu cara untuk mewujudkan startup agribisnis berbasis produk turunan kopi yakni memastikan kreativitas industri starup, inovasi dan penciptaan nilai melalui terintegrasinya 5 unsur konsep penta helix mulai dari akademisi, bisnis, pemerintahan, media dan komunitas. Penelitian ini bertujuan untuk mengkaji pengaruh interaksi penta helix terhadap kinerja inovasi produk agribisnis baik secara langsung maupun melalui keinovatifan organisasi startup agribisnis berbasis produk turunan kopi. Metode penelitia
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16

Tan, Zhi-Jie, and Shi-Jie Chen. "Ion-Mediated Nucleic Acid Helix-Helix Interactions." Biophysical Journal 91, no. 2 (2006): 518–36. http://dx.doi.org/10.1529/biophysj.106.084285.

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17

Jiang, Sulin, and Ilya A. Vakser. "Shorter side chains optimize helix-helix packing." Protein Science 13, no. 5 (2004): 1426–29. http://dx.doi.org/10.1110/ps.03505804.

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18

Shao, X. "Common fold in helix-hairpin-helix proteins." Nucleic Acids Research 28, no. 14 (2000): 2643–50. http://dx.doi.org/10.1093/nar/28.14.2643.

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19

Anthony-Cahill, S., P. Benfield, R. Fairman, et al. "Molecular characterization of helix-loop-helix peptides." Science 255, no. 5047 (1992): 979–83. http://dx.doi.org/10.1126/science.1312255.

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20

Brennan, R. G., and B. W. Matthews. "The helix-turn-helix DNA binding motif." Journal of Biological Chemistry 264, no. 4 (1989): 1903–6. http://dx.doi.org/10.1016/s0021-9258(18)94115-3.

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21

Goldfarb, Adam N., Kristine Lewandowska, and Menachem Shoham. "Determinants of Helix-Loop-Helix Dimerization Affinity." Journal of Biological Chemistry 271, no. 5 (1996): 2683–88. http://dx.doi.org/10.1074/jbc.271.5.2683.

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22

Rosinski, James A., and William R. Atchley. "Molecular Evolution of Helix–Turn–Helix Proteins." Journal of Molecular Evolution 49, no. 3 (1999): 301–9. http://dx.doi.org/10.1007/pl00006552.

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23

Murre, Cornelis. "Helix-loop-helix proteins and lymphocyte development." Nature Immunology 6, no. 11 (2005): 1079–86. http://dx.doi.org/10.1038/ni1260.

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24

Kaleta, David T., and Martin F. Jarrold. "Helix−Turn−Helix Motifs in Unsolvated Peptides." Journal of the American Chemical Society 125, no. 24 (2003): 7186–87. http://dx.doi.org/10.1021/ja0353006.

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25

Rum, Mokh. "Halal Industry in Madura: Development Model and Strategy." Dinar: Jurnal Ekonomi dan Keuangan Islam 10, no. 1 (2023): 48–60. http://dx.doi.org/10.21107/dinar.v10i1.20668.

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Madura has potential for Halal products. The four districts each have superior products with export potential. The development of the halal industry is an alternative to increasing the contribution of superior products to the regional economy and people's income. Its development requires the synergy of stakeholders through the Penta Helix model. This research aims to: 1). formulating the Penta Helix synergy model in the development of the halal industry in Madura; 2). formulate strategic priorities for the development of the halal industry in Madura. This research was conducted in Bangkalan Re
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26

Rohl, Carol A., та Andrew J. Doig. "Models for the 310-helix/coil, π-helix/coil, and α-helix/310-helix/coil transitions in isolated peptides". Protein Science 5, № 8 (1996): 1687–96. http://dx.doi.org/10.1002/pro.5560050822.

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27

Coombes, Sarah, and Steven AR Murphy. "Helix Health." Personalized Medicine 5, no. 2 (2008): 175–77. http://dx.doi.org/10.2217/17410541.5.2.175.

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28

Deodhar, Angelee. "Double Helix." Annals of Internal Medicine 130, no. 11 (1999): 941. http://dx.doi.org/10.7326/0003-4819-130-11-199906010-00006.

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29

Gorodentsev, A., and S. Kuleshov. "Helix Theory." Moscow Mathematical Journal 4, no. 2 (2004): 377–440. http://dx.doi.org/10.17323/1609-4514-2004-4-2-377-440.

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30

&NA;. "Double Helix." Infectious Diseases in Clinical Practice 23, no. 3 (2015): 166–67. http://dx.doi.org/10.1097/ipc.0000000000000280.

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31

Campanoni, Simone, Kevin Brownell, Svilen Kanev, Timothy M. Jones, Gu-Yeon Wei, and David Brooks. "HELIX-RC." ACM SIGARCH Computer Architecture News 42, no. 3 (2014): 217–28. http://dx.doi.org/10.1145/2678373.2665705.

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32

Aurora, Rajeev, and George D. Rosee. "Helix capping." Protein Science 7, no. 1 (1998): 21–38. http://dx.doi.org/10.1002/pro.5560070103.

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33

Ożga, Katarzyna, Magda Drewniak‐Świtalska, Ewa Rudzińska‐Szostak, and Łukasz Berlicki. "Towards Foldameric Miniproteins: A Helix‐Turn‐Helix Motif." ChemPlusChem 86, no. 4 (2021): 646–49. http://dx.doi.org/10.1002/cplu.202100090.

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34

Kang, Philjae, and Hyojong Yoo. "Coordinative helix–helix association of heteroleptic metallosupramolecular helicates." Inorganic Chemistry Frontiers 7, no. 4 (2020): 905–10. http://dx.doi.org/10.1039/c9qi01381d.

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35

Zhang, Yi, Jane Babin, Andrew L. Feldhaus, Harinder Singh, Phillip A. Sharp, and Minou Bina. "HTF4: a new human helix-loop-helix protein." Nucleic Acids Research 19, no. 16 (1991): 4555. http://dx.doi.org/10.1093/nar/19.16.4555.

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36

Auer, Manfred, Hans Ulrich Gremlich, Jan Marcus Seifert, et al. "Helix-Loop-Helix Motif in HIV-1 Rev." Biochemistry 33, no. 10 (1994): 2988–96. http://dx.doi.org/10.1021/bi00176a031.

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37

Ng, Derek P., and Charles M. Deber. "Terminal Residue Hydrophobicity Modulates Transmembrane Helix–Helix Interactions." Biochemistry 53, no. 23 (2014): 3747–57. http://dx.doi.org/10.1021/bi500317h.

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38

Lee, Jacqueline E. "Basic helix-loop-helix genes in neural development." Current Opinion in Neurobiology 7, no. 1 (1997): 13–20. http://dx.doi.org/10.1016/s0959-4388(97)80115-8.

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39

Ross, Sarah E., Michael E. Greenberg, and Charles D. Stiles. "Basic Helix-Loop-Helix Factors in Cortical Development." Neuron 39, no. 1 (2003): 13–25. http://dx.doi.org/10.1016/s0896-6273(03)00365-9.

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40

Bernan, Richard G. "DNA recognition by the helix-turn-helix motif." Current Biology 2, no. 3 (1992): 126. http://dx.doi.org/10.1016/0960-9822(92)90245-6.

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41

Lins, L., R. Brasseur, M. De Pauw, et al. "Helix-helix interactions in reconstituted high-density lipoproteins." Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism 1258, no. 1 (1995): 10–18. http://dx.doi.org/10.1016/0005-2760(95)00080-v.

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42

Prodöhl, Alexander, Mathias Weber, Carolin Dreher, and Dirk Schneider. "A mutational study of transmembrane helix–helix interactions." Biochimie 89, no. 11 (2007): 1433–37. http://dx.doi.org/10.1016/j.biochi.2007.06.006.

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43

Visvader, Jane, and C. Glenn Begley. "Helix-loop-helix genes translocated in lymphoid leukemia." Trends in Biochemical Sciences 16 (January 1991): 330–33. http://dx.doi.org/10.1016/0968-0004(91)90137-k.

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44

Deber, Charles M., and Derek P. Ng. "Helix-Helix Interactions: Is the Medium the Message?" Structure 23, no. 3 (2015): 437–38. http://dx.doi.org/10.1016/j.str.2015.02.004.

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45

Kurochkina, N. "Amino acid composition of parallel helix–helix interfaces." Journal of Theoretical Biology 247, no. 1 (2007): 110–21. http://dx.doi.org/10.1016/j.jtbi.2007.02.001.

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46

Banerjee, Arindam, S. Raghothama, and P. Balaram. "Peptide design. Helix–helix motifs in synthetic sequences." Journal of the Chemical Society, Perkin Transactions 2, no. 10 (1997): 2087–94. http://dx.doi.org/10.1039/a700624a.

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47

Brennan, Richard G. "Interactions of the helix-turn-helix binding domain." Current Opinion in Structural Biology 1, no. 1 (1991): 80–88. http://dx.doi.org/10.1016/0959-440x(91)90015-l.

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48

Brennan, Richard G. "DNA recognition by the helix-turn-helix motif." Current Opinion in Structural Biology 2, no. 1 (1992): 100–108. http://dx.doi.org/10.1016/0959-440x(92)90184-9.

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49

Murre, Cornelis, Gretchen Bain, Marc A. van Dijk, et al. "Structure and function of helix-loop-helix proteins." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1218, no. 2 (1994): 129–35. http://dx.doi.org/10.1016/0167-4781(94)90001-9.

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50

Mingarro, Ismael, Arne Elofsson, and Gunnar von Heijne. "Helix-helix packing in a membrane-like environment." Journal of Molecular Biology 272, no. 4 (1997): 633–41. http://dx.doi.org/10.1006/jmbi.1997.1276.

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