Journal articles: 'Structural diversity'

1

Szuromi, Phil. "Modulating structural diversity." Science 371, no. 6526 (January 14, 2021): 249.2–249. http://dx.doi.org/10.1126/science.371.6526.249-b.

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Boerner, Leigh Krietsch. "Diversity: Structural approach." Nature 515, no. 7528 (November 2014): 597–98. http://dx.doi.org/10.1038/nj7528-597a.

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Vinson, V. J. "GPCR Structural Diversity." Science Signaling 1, no. 47 (November 25, 2008): ec409-ec409. http://dx.doi.org/10.1126/scisignal.147ec409.

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ter Beek, Josy, Albert Guskov, and Dirk Jan Slotboom. "Structural diversity of ABC transporters." Journal of General Physiology 143, no. 4 (March 17, 2014): 419–35. http://dx.doi.org/10.1085/jgp.201411164.

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ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.

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Shaw, A. Jonathan. "Structural Diversity of Bryophytes." Bryologist 106, no. 2 (June 2003): 343. http://dx.doi.org/10.1639/0007-2745(2003)106[0343:r]2.0.co;2.

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Schmid, Rudolf, and Howard Crum. "Structural Diversity of Bryophytes." Taxon 50, no. 4 (November 2001): 1292. http://dx.doi.org/10.2307/1224764.

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Mannella, Carmen A. "Structural Diversity of Mitochondria." Annals of the New York Academy of Sciences 1147, no. 1 (December 8, 2008): 171–79. http://dx.doi.org/10.1196/annals.1427.020.

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HASEGAWA, Morifumi. "Structural Diversity of Phytoalexins." KAGAKU TO SEIBUTSU 55, no. 8 (July 20, 2017): 547–52. http://dx.doi.org/10.1271/kagakutoseibutsu.55.547.

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Maurya, Ashish, and Piali Sengupta. "Generating ciliary structural diversity." Mechanisms of Development 145 (July 2017): S65—S66. http://dx.doi.org/10.1016/j.mod.2017.04.145.

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Gregoryanz, E., L. F. Lundegaard, M. I. McMahon, C. Guillaume, R. J. Nelmes, and M. Mezouar. "Structural Diversity of Sodium." Science 320, no. 5879 (May 23, 2008): 1054–57. http://dx.doi.org/10.1126/science.1155715.

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Park, Juhan, Hyun Seok Kim, Hyun Kook Jo, and II Bin Jung. "The Influence of Tree Structural and Species Diversity on Temperate Forest Productivity and Stability in Korea." Forests 10, no. 12 (December 6, 2019): 1113. http://dx.doi.org/10.3390/f10121113.

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Research Highlights: Using a long-term dataset on temperate forests in South Korea, we established the interrelationships between tree species and structural diversity and forest productivity and stability, and identified a strong, positive effect of structural diversity, rather than tree species diversity, on productivity and stability. Background and Objectives: Globally, species diversity is positively related with forest productivity. However, temperate forests often show a negative or neutral relationship. In those forests, structural diversity, instead of tree species diversity, could control the forest function. Materials and Methods: This study tested the effects of tree species and structural diversity on temperate forest productivity. The basal area increment and relative changes in stand density were used as proxies for forest productivity and stability, respectively. Results: Here we show that structural diversity, but not species diversity, had a significant, positive effect on productivity, whereas species diversity had a negative effect, despite a positive effect on diversity. Structural diversity also promoted fewer changes in stand density between two periods, whereas species diversity showed no such relation. Structurally diverse forests might use resources efficiently through increased canopy complexity due to canopy plasticity. Conclusions: These results indicate reported species diversity effects could be related to structural diversity. They also highlight the importance of managing structurally diverse forests to improve productivity and stability in stand density, which may promote sustainability of forests.

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Talanov, Mikhail V., and Valeriy M. Talanov. "Structural Diversity of Ordered Pyrochlores." Chemistry of Materials 33, no. 8 (April 9, 2021): 2706–25. http://dx.doi.org/10.1021/acs.chemmater.0c04864.

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McManus, Simon A., and Yingfu Li. "The Structural Diversity of Deoxyribozymes." Molecules 15, no. 9 (September 6, 2010): 6269–84. http://dx.doi.org/10.3390/molecules15096269.

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Müller, Dennis, Lars F. Klepzig, Anja Schlosser, Dirk Dorfs, and Nadja C. Bigall. "Structural Diversity in Cryoaerogel Synthesis." Langmuir 37, no. 17 (April 22, 2021): 5109–17. http://dx.doi.org/10.1021/acs.langmuir.0c03619.

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Machado, N. F. L., and M. P. M. Marques. "Bioactive Chromone Derivatives – Structural Diversity." Current Bioactive Compounds 6, no. 2 (June 1, 2010): 76–89. http://dx.doi.org/10.2174/157340710791184859.

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Makowski, L. "Structural diversity in filamentous bacteriophages." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C481. http://dx.doi.org/10.1107/s0108767396080270.

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James, M., A. Linden, B. James, J. Liesegang, and V. Zuzich. "Structural diversity in thallium chemistry." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C327. http://dx.doi.org/10.1107/s0108767396086448.

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Voelker, Heike, Dieter Labahn, Frank Michael Bohnen, Regine Herbst-Irmer, Herbert W. Roesky, Dietmar Stalke, and Frank T. Edelmann. "Structural diversity in nonafluoromesityl chemistry." New Journal of Chemistry 23, no. 9 (1999): 905–9. http://dx.doi.org/10.1039/a903798e.

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Misra, Rajneesh, and Tavarekere K. Chandrashekar. "Structural Diversity in Expanded Porphyrins." Accounts of Chemical Research 41, no. 2 (February 2008): 265–79. http://dx.doi.org/10.1021/ar700091k.

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Koyama, Masako, and Hitoshi Kurumizaka. "Structural diversity of the nucleosome." Journal of Biochemistry 163, no. 2 (November 17, 2017): 85–95. http://dx.doi.org/10.1093/jb/mvx081.

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Golinelli-Pimpaneau, Béatrice. "Structural diversity of antibody catalysts." Journal of Immunological Methods 269, no. 1-2 (November 2002): 157–71. http://dx.doi.org/10.1016/s0022-1759(02)00240-5.

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Linden, Anthony, Margaret A. James, Mary B. Millikan, Loretta M. Kivlighon, Alexander Petridis, and Bruce D. James. "Structural diversity in thallium chemistry." Inorganica Chimica Acta 284, no. 2 (January 1999): 215–22. http://dx.doi.org/10.1016/s0020-1693(98)00289-8.

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Linden, Anthony, Kerry W. Nugent, Alexander Petridis, and Bruce D. James. "Structural diversity in thallium chemistry." Inorganica Chimica Acta 285, no. 1 (February 1999): 122–28. http://dx.doi.org/10.1016/s0020-1693(98)00339-9.

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Grala, Agnieszka, Małgorzata Wolska-Pietkiewicz, Anna Wojewódzka, Monika Dabergut, Iwona Justyniak, and Janusz Lewiński. "Structural Diversity of Ethylzinc Carboxylates." Organometallics 34, no. 20 (September 21, 2015): 4959–64. http://dx.doi.org/10.1021/acs.organomet.5b00557.

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Glabe, Charles. "Structural Diversity of Amyloid Oligomers." Biophysical Journal 98, no. 3 (January 2010): 3a. http://dx.doi.org/10.1016/j.bpj.2009.12.017.

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Nakamura, Aline M., Alessandro S. Nascimento, and Igor Polikarpov. "Structural diversity of carbohydrate esterases." Biotechnology Research and Innovation 1, no. 1 (January 2017): 35–51. http://dx.doi.org/10.1016/j.biori.2017.02.001.

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Giocondi, Marie-Cécile, Sylvie Boichot, Thomas Plénat, and Christian Le Grimellec. "Structural diversity of sphingomyelin microdomains." Ultramicroscopy 100, no. 3-4 (August 2004): 135–43. http://dx.doi.org/10.1016/j.ultramic.2003.11.002.

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Wang, Yanting, and Harro J. Bouwmeester. "Structural diversity in the strigolactones." Journal of Experimental Botany 69, no. 9 (March 7, 2018): 2219–30. http://dx.doi.org/10.1093/jxb/ery091.

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Ugander, J., L. Backstrom, C. Marlow, and J. Kleinberg. "Structural diversity in social contagion." Proceedings of the National Academy of Sciences 109, no. 16 (April 2, 2012): 5962–66. http://dx.doi.org/10.1073/pnas.1116502109.

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30

Cowley, Alan H., François P. Gabbaï, Harold S. Isom, Andreas Decken, and Robert D. Culp. "Structural Diversity in Organoindium Iodides." Main Group Chemistry 1, no. 1 (September 1995): 9–19. http://dx.doi.org/10.1080/13583149512331338225.

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31

Klepov, Vladislav V., Anna V. Vologzhanina, Evgeny V. Alekseev, Denis V. Pushkin, Larisa B. Serezhkina, Olga A. Sergeeva, Aleksandr V. Knyazev, and Viktor N. Serezhkin. "Structural diversity of uranyl acrylates." CrystEngComm 18, no. 10 (2016): 1723–31. http://dx.doi.org/10.1039/c5ce01957e.

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32

Synytsya, Andriy, and Miroslav Novák. "Structural diversity of fungal glucans." Carbohydrate Polymers 92, no. 1 (January 2013): 792–809. http://dx.doi.org/10.1016/j.carbpol.2012.09.077.

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33

Agbetu, Toyin. "Doing Diversity, Being Diversity." Teaching Anthropology 10, no. 1 (July 2, 2021): 8–15. http://dx.doi.org/10.22582/ta.v10i1.587.

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For many public institutions, ‘doing diversity’ exists as a performative act; a dance choreographed through acts of policy espousing a laudable song based on equality. The reality is somewhat different when it comes to implementation, as lofty ambitions give way to impermanent initiatives that are both strategically and tonally off-key. Today, many universities across the UK express their egalitarian aims based on progressive and sometimes decolonising theories of change, but all fail to deliver the pragmatic praxis demanded by their staff, students and collaborative research partners. This should not be so, especially for British anthropology departments which have sufficient authority to implement the structural changes required to make themselves representative of the worlds they study. Looking at this matter from the perspective of ‘race’, this paper calls for a pedagogical rebalancing of our discipline. It suggests a revaluation of the utility of meritocratic systems of evaluation and the employment of permanent ‘native’ staff in strategic roles to displace structural enclaves of hegemonic ‘whiteness’ could be enough to transform anthropology departments from doing diversity - into being it.

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34

Gregorius, Hans-Rolf, and Evsey Kosman. "Structural type diversity: measuring structuredness of communities by type diversity." Theoretical Ecology 11, no. 4 (January 15, 2018): 383–94. http://dx.doi.org/10.1007/s12080-017-0363-y.

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Naryzhny, S. N., and O. K. Legina. "Structural-functional diversity of p53 proteoforms." Biomeditsinskaya Khimiya 65, no. 4 (August 2019): 263–76. http://dx.doi.org/10.18097/pbmc20196504263.

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Protein p53 is one of the most studied proteins. This attention is primarily due to its key role in the cellular mechanisms associated with carcinogenesis. Protein p53 is a transcription factor involved in a wide variety of processes: cell cycle regulation and apoptosis, signaling inside the cell, DNA repair, coordination of metabolic processes, regulation of cell interactions, etc. This multifunctionality is apparently determined by the fact that p53 is a vivid example of how the same protein can be represented by numerous proteoforms bearing completely different functional loads. By alternative splicing, using different promoters and translation initiation sites, the TP53 gene gives rise to at least 12 isoforms, which can additionally undergo numerous (>200) post-translational modifications. Proteoforms generated due to numerous point mutations in the TP53 gene are adding more complexity to this picture. The proteoforms produced are involved in various processes, such as the regulation of p53 transcriptional activity in response to various factors. This review is devoted to the description of the currently known p53 proteoforms, as well as their possible functionality.

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36

Ueno, Kotomi, Hirosato Takikawa, and Yukihiro Sugimoto. "Structural and configurational diversity of strigolactones." Japanese Journal of Pesticide Science 46, no. 2 (August 20, 2021): 136–42. http://dx.doi.org/10.1584/jpestics.w21-28.

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Dürvanger, Zsolt, and Veronika Harmat. "Structural Diversity in Calmodulin - Peptide Interactions." Current Protein & Peptide Science 20, no. 11 (October 24, 2019): 1102–11. http://dx.doi.org/10.2174/1389203720666190925101937.

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Calmodulin (CaM) is a highly conserved eukaryotic Ca2+ sensor protein that is able to bind a large variety of target sequences without a defined consensus sequence. The recognition of this diverse target set allows CaM to take part in the regulation of several vital cell functions. To fully understand the structural basis of the regulation functions of CaM, the investigation of complexes of CaM and its targets is essential. In this minireview we give an outline of the different types of CaM - peptide complexes with 3D structure determined, also providing an overview of recently determined structures. We discuss factors defining the orientations of peptides within the complexes, as well as roles of anchoring residues. The emphasis is on complexes where multiple binding modes were found.

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Toma-Fukai, Sachiko, and Toshiyuki Shimizu. "Structural Diversity of Ubiquitin E3 Ligase." Molecules 26, no. 21 (November 4, 2021): 6682. http://dx.doi.org/10.3390/molecules26216682.

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The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.

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39

SHIHOYA, Wataru. "Structural Diversity of Non-canonical Rhodopsins." Seibutsu Butsuri 61, no. 4 (2021): 251–52. http://dx.doi.org/10.2142/biophys.61.251.

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40

Orr, Melissa, Glen R. Hebberd, Emma E. McCabe, and Robin T. Macaluso. "Structural Diversity of Rare-Earth Oxychalcogenides." ACS Omega 7, no. 10 (March 5, 2022): 8209–18. http://dx.doi.org/10.1021/acsomega.2c00186.

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41

Harmon, Robert M., and Kathleen J. Green. "Structural and Functional Diversity of Desmosomes." Cell Communication & Adhesion 20, no. 6 (November 8, 2013): 171–87. http://dx.doi.org/10.3109/15419061.2013.855204.

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42

von Platz, Jeppe, and David A. Reidy. "The Structural Diversity of Historical Injustices." Journal of Social Philosophy 37, no. 3 (September 2006): 360–76. http://dx.doi.org/10.1111/j.1467-9833.2006.00342.x.

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43

Suzuki, Mitsuo, and Hideaki Ohba. "Wood Structural Diversity among Himalayan Rhododendron." IAWA Journal 9, no. 4 (1988): 317–26. http://dx.doi.org/10.1163/22941932-90001090.

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The wood anatomy of nine species of Himalayan Rhododendron is compared. All share the characters: growth rings present, but indistinct; pores evenly distributed, numerous; intervessel pits alternate; perforation plates scalariform with 10 to 30 bars; wood parenchyma diffuse or diffuse-in-aggregates; rays heterogeneous uniseriate and multiseriate. However, pore size, occurrence of spiral thickenings and frequency of multi seriate rays are variable among the species studied. Our investigation shows that these characters vary according to the habit of plants. The woods of trees have wider vessels, distinct spirals in both vessels and fibre-tracheids, and numerous multiseriate rays, while those of shrubs have narrower vessels with indistinct or restricted spirals and less frequent multiseriate rays.

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44

Stewart, James R., and Daniel G. Blackburn. "Reptilian Placentation: Structural Diversity and Terminology." Copeia 1988, no. 4 (December 28, 1988): 839. http://dx.doi.org/10.2307/1445706.

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Smits, J., C. Guguta, I. Eeuwijk, and R. de Gelder. "Structural diversity of synthetic estrogen solvates." Acta Crystallographica Section A Foundations of Crystallography 63, a1 (August 22, 2007): s208—s209. http://dx.doi.org/10.1107/s0108767307095256.

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46

Taylor, Richard E., Michael J. Schmitt, and Haiqing Yuan. "Structural Diversity Based on Cyclopropane Scaffolds." Organic Letters 2, no. 5 (March 2000): 601–3. http://dx.doi.org/10.1021/ol9913542.

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Linden, A., B. D. James, J. Liesegang, and N. Gonis. "Structural diversity in chloromercury(II) salts." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C290. http://dx.doi.org/10.1107/s0108767396087934.

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48

Wiederschain, G. Ya. "Polysaccharides. Structural diversity and functional versatility." Biochemistry (Moscow) 72, no. 6 (June 2007): 675. http://dx.doi.org/10.1134/s0006297907060120.

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49

Shevchenko, Elena V., Dmitri V. Talapin, Nicholas A. Kotov, Stephen O'Brien, and Christopher B. Murray. "Structural diversity in binary nanoparticle superlattices." Nature 439, no. 7072 (January 2006): 55–59. http://dx.doi.org/10.1038/nature04414.

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50

Chen, Songye, Morgan Beeby, Gavin E. Murphy, Jared R. Leadbetter, David R. Hendrixson, Ariane Briegel, Zhuo Li, et al. "Structural diversity of bacterial flagellar motors." EMBO Journal 30, no. 14 (June 14, 2011): 2972–81. http://dx.doi.org/10.1038/emboj.2011.186.

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Journal articles on the topic 'Structural diversity'

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