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Journal articles on the topic 'Helix'

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Author: Grafiati
Published: 4 June 2021
Last updated: 31 January 2023

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1

Regan, L. "Helix is a helix is a helix?" Proceedings of the National Academy of Sciences 94, no. 7 (April 1, 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 (January 3, 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 (December 1, 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 (January 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 (September 28, 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 (December 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 (October 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 (December 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 (August 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 (August 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 (September 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 (June 2004): 7479–89. http://dx.doi.org/10.1021/jp037688x.

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15

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

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16

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

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17

Shao, X. "Common fold in helix-hairpin-helix proteins." Nucleic Acids Research 28, no. 14 (July 15, 2000): 2643–50. http://dx.doi.org/10.1093/nar/28.14.2643.

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18

Anthony-Cahill, S., P. Benfield, R. Fairman, Z. Wasserman, S. Brenner, W. Stafford, C. Altenbach, W. Hubbell, and W. DeGrado. "Molecular characterization of helix-loop-helix peptides." Science 255, no. 5047 (February 21, 1992): 979–83. http://dx.doi.org/10.1126/science.1312255.

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19

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

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20

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

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21

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

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22

Murre, Cornelis. "Helix-loop-helix proteins and lymphocyte development." Nature Immunology 6, no. 11 (October 27, 2005): 1079–86. http://dx.doi.org/10.1038/ni1260.

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23

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

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24

Rohl, Carol A., and 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, no. 8 (August 1996): 1687–96. http://dx.doi.org/10.1002/pro.5560050822.

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25

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

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26

Deodhar, Angelee. "Double Helix." Annals of Internal Medicine 130, no. 11 (June 1, 1999): 941. http://dx.doi.org/10.7326/0003-4819-130-11-199906010-00006.

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27

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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28

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

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29

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 (October 16, 2014): 217–28. http://dx.doi.org/10.1145/2678373.2665705.

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30

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

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31

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

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32

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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33

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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34

Auer, Manfred, Hans Ulrich Gremlich, Jan Marcus Seifert, Thomas J. Daly, Tristram G. Parslow, Georg Casari, and Hubert Gstach. "Helix-Loop-Helix Motif in HIV-1 Rev." Biochemistry 33, no. 10 (March 15, 1994): 2988–96. http://dx.doi.org/10.1021/bi00176a031.

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35

Ng, Derek P., and Charles M. Deber. "Terminal Residue Hydrophobicity Modulates Transmembrane Helix–Helix Interactions." Biochemistry 53, no. 23 (June 9, 2014): 3747–57. http://dx.doi.org/10.1021/bi500317h.

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36

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

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37

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

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38

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

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39

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

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40

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

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41

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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42

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

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43

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

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44

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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45

Antosiewicz, J., M. W. German, J. H. Van De Sande, and D. Porschke. "Helix-coil dynamics of a Z-helix hairpin." Biopolymers 27, no. 8 (August 1988): 1319–27. http://dx.doi.org/10.1002/bip.360270810.

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46

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

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47

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

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48

Murre, Cornelis, Gretchen Bain, Marc A. van Dijk, Isaac Engel, Beth A. Furnari, Mark E. Massari, James R. Matthews, Melanie W. Quong, Richard R. Rivera, and Maarten H. Stuiver. "Structure and function of helix-loop-helix proteins." Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1218, no. 2 (June 1994): 129–35. http://dx.doi.org/10.1016/0167-4781(94)90001-9.

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49

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

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50

Psachoulia, Emi, Philip W. Fowler, Peter J. Bond, and Mark S. P. Sansom. "Helix−Helix Interactions in Membrane Proteins: Coarse-Grained Simulations of Glycophorin A Helix Dimerization†." Biochemistry 47, no. 40 (October 7, 2008): 10503–12. http://dx.doi.org/10.1021/bi800678t.

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