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Journal articles on the topic 'From-to structure'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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1

Gupta, Vichitra. "State Structure and Education : From Athens to Modern Era." Contemporary Social Sciences 27, no. 2 (2018): 8–17. http://dx.doi.org/10.29070/27/57460.

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2

Fahmy, Hesham, Katerina Spyridaki, Bhimanna Kuppast, and George Liapakis. "The “homeostasis hormone” and its CRF1 receptor. From structure to function." HORMONES 11, no. 3 (2012): 254–71. http://dx.doi.org/10.14310/horm.2002.1355.

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3

Sokolova, Elena Cámara, Frank C. Hawthorne, and Yassir Abdu. "From structure topology to chemical composition. VII. Titanium silicates: the crystal structure and crystal chemistry of jinshajiangite." European Journal of Mineralogy 21, no. 4 (2009): 871–83. http://dx.doi.org/10.1127/0935-1221/2009/0021-1945.

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4

Sanna, Emanuele, Maria Chiara Iovine, and Giovanni Floris. "Evolution of marital structure in 20 Sardinian villages from 1800 to 1974." Anthropologischer Anzeiger 62, no. 2 (2004): 169–84. http://dx.doi.org/10.1127/anthranz/62/2004/169.

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5

Thomé, K. M., and A. B. P. Soares. "International market structure and competitiveness at the malted beer: from 2003 to 2012." Agricultural Economics (Zemědělská ekonomika) 61, No. 4 (2016): 166–78. http://dx.doi.org/10.17221/189/2014-agricecon.

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6

Liu, Keh-Fei. "From nuclear structure to nucleon structure." Nuclear Physics A 928 (August 2014): 99–109. http://dx.doi.org/10.1016/j.nuclphysa.2014.04.011.

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7

Vinson, Valda. "From phenotype to structure." Science 370, no. 6522 (2020): 1286.10–1288. http://dx.doi.org/10.1126/science.370.6522.1286-j.

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8

Welsh, Talia. "From Gestalt to Structure." Theory & Psychology 16, no. 4 (2006): 527–51. http://dx.doi.org/10.1177/0959354306066205.

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9

Palmer, Rex A. "From crystal to structure." Trends in Biochemical Sciences 25, no. 7 (2000): 346. http://dx.doi.org/10.1016/s0968-0004(00)01545-0.

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10

Strack, Rita. "From localizations to structure." Nature Methods 14, no. 10 (2017): 942. http://dx.doi.org/10.1038/nmeth.4453.

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11

de Souza, Natalie. "From structure to function." Nature Methods 4, no. 10 (2007): 771. http://dx.doi.org/10.1038/nmeth1007-771.

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12

Mandler, George. "From association to structure." Journal of Experimental Psychology: Learning, Memory, and Cognition 11, no. 3 (1985): 464–68. http://dx.doi.org/10.1037/0278-7393.11.3.464.

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13

Xu, Qiang, Henny W. Zandbergen, and Dirk Van Dyck. "Imaging from atomic structure to electronic structure." Micron 43, no. 4 (2012): 524–31. http://dx.doi.org/10.1016/j.micron.2011.10.024.

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14

Zhang, Le, Lilong Dang, Feng Luo, and Xuefeng Feng. "Solvent-controlled assembly of crystal structures: From centrosymmetric structure to noncentrosymmetric structure." Journal of Molecular Structure 1106 (February 2016): 114–20. http://dx.doi.org/10.1016/j.molstruc.2015.10.094.

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15

Yosef, Nir, and Lukas Käll. "From sequence to structure to networks." Genome Biology 9, no. 11 (2008): 326. http://dx.doi.org/10.1186/gb-2008-9-11-326.

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16

Mergelov, N. S., I. G. Shorkunov, A. V. Dolgikh, et al. "Endolithic and hypolithic soil-like systems: structure and composition from the macro- to submicro-levels." Dokuchaev Soil Bulletin 86 (December 15, 2016): 103–14. http://dx.doi.org/10.19047/0136-1694-2016-86-103-114.

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17

Nagerl, U. Valentin. "3SBA-04 STED imaging of synapses in living brain slices : from structure to function(3SBA Cutting-edge optical imaging approach to neuroscience-From single molecule to in vivo-,Symposium)." Seibutsu Butsuri 53, supplement1-2 (2013): S102. http://dx.doi.org/10.2142/biophys.53.s102_2.

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18

Zerkowski, Jonathan A. "Estolides: From structure and function to structured and functionalized." Lipid Technology 20, no. 11 (2008): 253–56. http://dx.doi.org/10.1002/lite.200800066.

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19

Nigou, J. "Lipoarabinomannans: from structure to biosynthesis." Biochimie 85, no. 1-2 (2003): 153–66. http://dx.doi.org/10.1016/s0300-9084(03)00048-8.

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20

Orengo, Christine A., Annabel E. Todd, and Janet M. Thornton. "From protein structure to function." Current Opinion in Structural Biology 9, no. 3 (1999): 374–82. http://dx.doi.org/10.1016/s0959-440x(99)80051-7.

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21

Colledge, Marcie, and John D. Scott. "AKAPs: from structure to function." Trends in Cell Biology 9, no. 6 (1999): 216–21. http://dx.doi.org/10.1016/s0962-8924(99)01558-5.

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22

Stock, Daniela, Petra M. Nederlof, Erika Seemüller, Wolfgang Baumeister, Robert Huber, and Jan Löwe. "Proteasome: from structure to function." Current Opinion in Biotechnology 7, no. 4 (1996): 376–85. http://dx.doi.org/10.1016/s0958-1669(96)80111-x.

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23

Wilkinson, C., G. B. Dijksterhuis, and M. Minekus. "From food structure to texture." Trends in Food Science & Technology 11, no. 12 (2000): 442–50. http://dx.doi.org/10.1016/s0924-2244(01)00033-4.

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24

de Veer, Simon J., Meng-Wei Kan, and David J. Craik. "Cyclotides: From Structure to Function." Chemical Reviews 119, no. 24 (2019): 12375–421. http://dx.doi.org/10.1021/acs.chemrev.9b00402.

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25

Zheng, Wei-Mou. "Proteins: From sequence to structure." Chinese Physics B 23, no. 7 (2014): 078705. http://dx.doi.org/10.1088/1674-1056/23/7/078705.

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26

Heller, Wendy. "From Neuropsychology to Mental Structure." Journal of Neuropsychiatry and Clinical Neurosciences 2, no. 3 (1990): 349–51. http://dx.doi.org/10.1176/jnp.2.3.349.

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27

Chergui, Majed. "From structure to structural dynamics." Acta Crystallographica Section A Foundations and Advances 74, a1 (2018): a439. http://dx.doi.org/10.1107/s0108767318095612.

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28

Jackson, Sophie E., Christine Queitsch, and David Toft. "Hsp90: from structure to phenotype." Nature Structural & Molecular Biology 11, no. 12 (2004): 1152–55. http://dx.doi.org/10.1038/nsmb1204-1152.

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29

Facelli, Julio C., and Marta B. Ferraro. "From NMR spectra to structure." Concepts in Magnetic Resonance Part A 42, no. 6 (2013): 261–89. http://dx.doi.org/10.1002/cmr.a.21291.

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30

Grande, Joseph P. "Polycystin: From structure to function." Kidney International 57, no. 4 (2000): 1770–71. http://dx.doi.org/10.1046/j.1523-1755.2000.00027.x.

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31

Gerke, Volker, and Stephen E. Moss. "Annexins: From Structure to Function." Physiological Reviews 82, no. 2 (2002): 331–71. http://dx.doi.org/10.1152/physrev.00030.2001.

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Annexins are Ca2+and phospholipid binding proteins forming an evolutionary conserved multigene family with members of the family being expressed throughout animal and plant kingdoms. Structurally, annexins are characterized by a highly α-helical and tightly packed protein core domain considered to represent a Ca2+-regulated membrane binding module. Many of the annexin cores have been crystallized, and their molecular structures reveal interesting features that include the architecture of the annexin-type Ca2+binding sites and a central hydrophilic pore proposed to function as a Ca2+channel. In addition to the conserved core, all annexins contain a second principal domain. This domain, which NH2-terminally precedes the core, is unique for a given member of the family and most likely specifies individual annexin properties in vivo. Cellular and animal knock-out models as well as dominant-negative mutants have recently been established for a number of annexins, and the effects of such manipulations are strikingly different for different members of the family. At least for some annexins, it appears that they participate in the regulation of membrane organization and membrane traffic and the regulation of ion (Ca2+) currents across membranes or Ca2+concentrations within cells. Although annexins lack signal sequences for secretion, some members of the family have also been identified extracellularly where they can act as receptors for serum proteases on the endothelium as well as inhibitors of neutrophil migration and blood coagulation. Finally, deregulations in annexin expression and activity have been correlated with human diseases, e.g., in acute promyelocytic leukemia and the antiphospholipid antibody syndrome, and the term annexinopathies has been coined.

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32

Sutton, Jeffrey P. "From neuropsychology to mental structure." Neural Networks 8, no. 2 (1995): 321–22. http://dx.doi.org/10.1016/0893-6080(95)90005-5.

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33

Hernandez-Verdun, Danièle. "Nucleolus: from structure to dynamics." Histochemistry and Cell Biology 125, no. 1-2 (2005): 127–37. http://dx.doi.org/10.1007/s00418-005-0046-4.

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34

Ye, Fengying, Weijie Chen, Yingle Pan, Sheng Hua Liu, and Jun Yin. "Benzobisthiadiazoles: From structure to function." Dyes and Pigments 171 (December 2019): 107746. http://dx.doi.org/10.1016/j.dyepig.2019.107746.

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35

Beaumont, J. Graham. "From neuropsychology to mental structure." Biological Psychology 29, no. 2 (1989): 196–98. http://dx.doi.org/10.1016/0301-0511(89)90038-0.

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36

Jennekens-Schinkel, A. "From neuropsychology to mental structure." Journal of the Neurological Sciences 91, no. 3 (1989): 354. http://dx.doi.org/10.1016/0022-510x(89)90066-x.

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37

Kazerounian, S., K. O. Yee, and J. Lawler. "Thrombospondins: from structure to therapeutics." Cellular and Molecular Life Sciences 65, no. 5 (2008): 700–712. http://dx.doi.org/10.1007/s00018-007-7486-z.

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38

Roberts, D. D. "Thrombospondins: from structure to therapeutics." Cellular and Molecular Life Sciences 65, no. 5 (2008): 667–71. http://dx.doi.org/10.1007/s00018-007-7483-2.

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39

Carlson, C. B., J. Lawler, and D. F. Mosher. "Thrombospondins: from structure to therapeutics." Cellular and Molecular Life Sciences 65, no. 5 (2008): 672–86. http://dx.doi.org/10.1007/s00018-007-7484-1.

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40

Posey, K. L., Y. Yang, A. C. Veerisetty, S. K. Sharan, and J. T. Hecht. "Thrombospondins: from structure to therapeutics." Cellular and Molecular Life Sciences 65, no. 5 (2008): 687–99. http://dx.doi.org/10.1007/s00018-007-7485-0.

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41

Bonnefoy, A., R. Moura, and M. F. Hoylaerts. "Thrombospondins: from structure to therapeutics." Cellular and Molecular Life Sciences 65, no. 5 (2008): 713–27. http://dx.doi.org/10.1007/s00018-007-7487-y.

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42

Isenberg, J. S., W. A. Frazier, and D. D. Roberts. "Thrombospondins: from structure to therapeutics." Cellular and Molecular Life Sciences 65, no. 5 (2008): 728–42. http://dx.doi.org/10.1007/s00018-007-7488-x.

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43

Siéroff, Eric. "From neuropsychology to mental structure." Neuropsychologia 30, no. 7 (1992): 675–77. http://dx.doi.org/10.1016/0028-3932(92)90074-v.

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44

Vladimirovich Zhuravlev, Aleksandr. "Four Theses About Qualia and Matter: From Quality to Structure, from Structure to Functions." International Journal of Philosophy 5, no. 3 (2017): 23. http://dx.doi.org/10.11648/j.ijp.20170503.11.

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45

Ressler, Antonia, Karla Zadro, Hrvoje Ivanković, et al. "From Bio-waste to Bone Substitute." Chemical & biochemical engineering quarterly 34, no. 2 (2020): 59–71. http://dx.doi.org/10.15255/cabeq.2020.1783.

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Nanocomposite structure of the bone can be mimicked by chitosan/hydroxyapatite (CS/HAp) composite scaffold. Biological hydroxyapatite (HAp) contains various ions, which have a crucial role in bone growth. The aim of the present work was to synthesize biomimetic hydroxyapatite and prepare composite scaffolds based on chitosan, where HAp was synthesised from hen eggshells, seashells and cuttlefish bone. The powders were composed of nano-structured calcium deficient HAp and amorphous calcium phosphate (ACP). In the as-prepared powders, Sr2+, Mg2+ and Na+ ions were detected as a result of using biogenic precursor of Ca2+ ions. Highly porous CS/HAp structures have been prepared by freeze-gelation technique. The CS/HAp scaffolds have shown highly porous structure with very well interconnected pores and homogeneously dispersed HAp particles. The MTT assay of CS/HAp scaffolds has shown no toxicity, and the live/dead assay has confirmed good viability and proliferation of seeded cells.

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46

Teichmann, Sarah A., and Nick V. Grishin. "Sequences and topology: from genome structure to protein structure." Current Opinion in Structural Biology 18, no. 3 (2008): 340–41. http://dx.doi.org/10.1016/j.sbi.2008.05.006.

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47

Galov, A., K. Byrne, T. Gomerčić, et al. "Genetic structure and admixture between the Posavina and Croatian Coldblood in contrast to Lipizzan horse from Croatia." Czech Journal of Animal Science 58, No. 2 (2013): 71–78. http://dx.doi.org/10.17221/6617-cjas.

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The Posavina and Croatian Coldblood are Croatian autochthonous horse breeds with interwoven breeding histories for which studbooks have only recently been established. The Lipizzan breed has the oldest formalized breeding and no record of recent genetic introgression from other breeds in Croatia. We analyzed the genetic structure, interbreeding, and breed characteristics by genotyping nine dinucleotide microsatellite loci for 53 Posavina, 37 Croatian Coldblood, and 33 Lipizzan horses and showed that differing breeding schemes and histories have had a strong and measurable impact on the population genetic structure within and between the three breeds. A Bayesian clustering method demonstrated that two population clusters best explain the genetic structure. Samples from the pre-defined breeds of the Posavina and Croatian Coldblood were assigned to a separate genetic cluster, while Lipizzan specimens were assigned to another distinct genetic group. Twelve samples of the Posavina/Croatian Coldblood cluster (13%) showed admixed ancestry with Lipizzan horses. A test for heterozygosity excess, allele frequency distribution mode-shift, and M-ratio test were used to detect genetic evidence of recent population bottlenecks, none of which provided evidence for bottlenecks in the Posavina and Croatian Coldblood populations. In contrast, although somewhat ambiguous, evidence suggests a genetic bottleneck in the Lipizzan population in Croatia.

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48

Ley, David. "FROM URBAN STRUCTURE TO URBAN LANDSCAPE." Urban Geography 9, no. 1 (1988): 98–105. http://dx.doi.org/10.2747/0272-3638.9.1.98.

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49

Santos-Buelga, Celestino, and Arturo San Feliciano. "Flavonoids: From Structure to Health Issues." Molecules 22, no. 3 (2017): 477. http://dx.doi.org/10.3390/molecules22030477.

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50

Ito, Masao. "The Cerebellum: From Structure to Control." Trends in Cognitive Sciences 2, no. 9 (1998): 371. http://dx.doi.org/10.1016/s1364-6613(98)01217-0.

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