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Journal articles on the topic 'Structural studies'

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Published: 4 June 2021
Last updated: 11 March 2023

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1

Tan, Song, and Curt A. Davey. "Nucleosome structural studies." Current Opinion in Structural Biology 21, no. 1 (February 2011): 128–36. http://dx.doi.org/10.1016/j.sbi.2010.11.006.

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2

Shigematsu, T., F. Krok, and W. Bogusz. "Structural Studies on BICOVOX." Solid State Phenomena 39-40 (December 1994): 75–80. http://dx.doi.org/10.4028/www.scientific.net/ssp.39-40.75.

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3

Al-Amoudi, Ashraf, and Achilleas S. Frangakis. "Structural studies on desmosomes." Biochemical Society Transactions 36, no. 2 (March 20, 2008): 181–87. http://dx.doi.org/10.1042/bst0360181.

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Desmosomes are cadherin-based intercellular junctions that primarily provide mechanical stability to tissues such as epithelia and cardiac muscle. Desmosomal cadherins, which are Ca2+-dependent adhesion molecules, are of central importance in mediating direct intercellular interaction. The close association of these proteins, with intracellular components of desmosomes ultimately linked to the cytoskeleton, is believed to play an important role in tissue morphogenesis during development and wound healing. Elucidation of the binding mechanism of adhesive interfaces between the extracellular domains of cadherins has been approached by structural, biophysical and biochemical methods. X-ray crystal structures of isolated extracellular domains of cadherins have provided compelling evidence of the mutual binding of the highly conserved N-terminal residue, Trp2, from opposing proteins. This binding interface was also implicated by biochemical and cell-adhesion assays and mutagenesis data to be the primary adhesive interface between cells. Recent results based on electron tomography of epidermal desmosomes were consistent with this view, showing cadherin molecules interacting at their N-terminal tips. An integrative structural approach involving X-ray crystallography, cryo-electron tomography and immuno-electron microscopy should give the complete picture of the architecture of this important junction; identifying its various proteins and showing their arrangements and binding interfaces under native conditions. Together with these ‘static’ approaches, live-cell imaging of cultured keratinocytes should provide important insights into the dynamic property of the assembly and disassembly of desmosomes.
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4

Elsegood, M. R. J., and C. Redshaw. "Structural studies of boracalixarenes." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c310. http://dx.doi.org/10.1107/s0108767305086770.

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5

Kerfeld, C. A., M. R. Sawaya, S. Tanaka, M. Beeby, J. Laidman, and T. O. Yeates. "Structural studies on carboxysomes." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c92. http://dx.doi.org/10.1107/s010876730509611x.

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6

Eisenberg, D., R. Nelson, M. R. Sawaya, M. Balbirnie, A. Ø. Madsen, C. Riekel, S. Sambashivan, Y. Liu, M. Gingery, and R. Grothe. "Structural studies of amyloid." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c8. http://dx.doi.org/10.1107/s0108767305099666.

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7

Malik, Sohail, and Klaus Albert. "Structural Studies on Vindolinine." Zeitschrift für Naturforschung B 41, no. 3 (March 1, 1986): 386–92. http://dx.doi.org/10.1515/znb-1986-0316.

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19-S-Vindolinine has been found to undergo an interesting isomerisation in chloroform to 19-R-vindolinine at room temperature. NOEDS measurements have been carried out on both isomers and a 13C solid state CP-MAS spectrum recorded for 19-S-vindolininc. The structure assigned as 16-epi-19-S-vindolinine to an alkaloid isolated previously from Catharanthus roseus has been revised in the light of corrected 13C NMR values for 19-S- and 19-R-vindolinine.
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8

Grimes, J., P. Gouet, A. Basak, G. Sutton, P. Roy, N. Burroughs, B. V. V. Prasad, P. Mertens, and D. Stuart. "Structural studies on orbiviruses." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C179. http://dx.doi.org/10.1107/s0108767396092136.

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9

BENEDETTI, E., A. BAVOSO, B. BLASIO, V. PAVONE, C. PEDONE, L. PAOLILLO, and M. D'ALAGNI. "Structural studies of cyclopeptides." International Journal of Peptide and Protein Research 31, no. 2 (January 12, 2009): 220–24. http://dx.doi.org/10.1111/j.1399-3011.1988.tb00026.x.

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10

Kozlov, G., A. Y. Denisov, J. F. Trempe, H. Pande, M. Girard, M. J. Dicaire, P. S. McPherson, B. Brais, and K. Gehring. "Structural studies of sacsin." Acta Crystallographica Section A Foundations of Crystallography 68, a1 (August 7, 2012): s163. http://dx.doi.org/10.1107/s0108767312096869.

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11

Davies, G. J. "Structural studies on cellulases." Biochemical Society Transactions 26, no. 2 (May 1, 1998): 167–72. http://dx.doi.org/10.1042/bst0260167.

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12

SUNDAR, C., Y. HARIHARAN, A. BHARATHI, M. PREMILA, V. SASTRY, G. RAO, J. JANAKI, D. NATARAJAN, K. DEVADHASAN, and T. RADHAKRISHNAN. "Structural studies on fullerenes." Progress in Crystal Growth and Characterization of Materials 34, no. 1-4 (1997): 11–23. http://dx.doi.org/10.1016/s0960-8974(97)00002-8.

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13

Yurtsever, Mine, and Ersin Yurtsever. "Structural studies of polypyrroles." Synthetic Metals 98, no. 3 (January 1999): 221–27. http://dx.doi.org/10.1016/s0379-6779(98)00195-7.

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14

Yurtsever, Ersin, Okan Esentürk, H. Önder Pamuk, and Mine Yurtsever. "Structural studies of polypyrroles." Synthetic Metals 98, no. 3 (January 1999): 229–36. http://dx.doi.org/10.1016/s0379-6779(98)00196-9.

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15

Helliwell, J. R. "Time-resolved structural studies." Acta Crystallographica Section A Foundations of Crystallography 49, s1 (August 21, 1993): c8. http://dx.doi.org/10.1107/s010876737809978x.

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16

Vishnyakova, Elena, Gaowei Chen, Bruce E. Brinson, Lawrence B. Alemany, and W. Edward Billups. "Structural Studies of Hydrographenes." Accounts of Chemical Research 50, no. 6 (May 9, 2017): 1351–58. http://dx.doi.org/10.1021/acs.accounts.6b00588.

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17

Albert, Arlene D., and Philip L. Yeagle. "Structural studies on rhodopsin." Biochimica et Biophysica Acta (BBA) - Biomembranes 1565, no. 2 (October 2002): 183–95. http://dx.doi.org/10.1016/s0005-2736(02)00568-0.

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18

NOREUS, D., P. WERNER, K. ALASAFI, and E. SCHMIDTIHN. "Structural studies of TiNiH." International Journal of Hydrogen Energy 10, no. 7-8 (1985): 547–50. http://dx.doi.org/10.1016/0360-3199(85)90086-2.

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19

Barabas, O., Zs Dubrovay, V. Harmat, J. Kovari, E. Takacs, I. Zagyva, G. Naray-Szabo, and B. G. Vertessy. "Structural studies ofDrosophila melanogasterdUTPase." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (August 6, 2002): c96. http://dx.doi.org/10.1107/s0108767302088852.

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20

Toomer, Carol A., Carl H. Schwalbe, Neil S. Ringan, Peter A. Lambert, Philip R. Lowe, and Ving J. Lee. "Structural studies on tazobactam." Journal of Medicinal Chemistry 34, no. 7 (July 1991): 1944–47. http://dx.doi.org/10.1021/jm00111a003.

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21

PORTER, RODNEY R. "Structural Studies of Immunoglobulins." Scandinavian Journal of Immunology 34, no. 4 (October 1991): 382–88. http://dx.doi.org/10.1111/j.1365-3083.1991.tb01560.x.

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22

Kiliç, Gülşen Baci, Levent Toppare, and Ersin Yurtsever. "Structural studies of polythiophenes." Synthetic Metals 78, no. 1 (March 1996): 19–25. http://dx.doi.org/10.1016/0379-6779(95)03560-5.

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23

Daly, Norelle L., and David J. Craik. "Structural studies of conotoxins." IUBMB Life 61, no. 2 (February 2009): 144–50. http://dx.doi.org/10.1002/iub.158.

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24

Kohn, Harold, Syed Abuzar, James D. Korp, Andrew S. Zektzer, and Gary E. Martin. "Structural studies of bicyclomycin." Journal of Heterocyclic Chemistry 25, no. 5 (September 1988): 1511–17. http://dx.doi.org/10.1002/jhet.5570250548.

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25

Koch-Müller, Monika, Irmgard Abs-Wurmbach, Klaus Langer, Cuff Shaw, Richard Wirth, and Matthias Gottschalk. "Synthetic and natural Fe-Mg chloritoid: structural, spectroscopic and thermodynamic studies." European Journal of Mineralogy 12, no. 2 (March 29, 2000): 293–314. http://dx.doi.org/10.1127/ejm/12/2/0293.

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26

Havrlík, Michal, and Iveta Klicmanová. "Structural Studies of Nanofiber Membranes." Key Engineering Materials 714 (September 2016): 137–42. http://dx.doi.org/10.4028/www.scientific.net/kem.714.137.

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Recently, the modeling of physical properties of nanofiber textiles has attracted a lot of attention. Since standard macroscopic models cannot satisfactorily explain the observed properties of such materials, it is necessary to develop models based on the knowledge of exact microscopic structure of nanotextiles. In this paper, we study the microscopic structure of two types of polymer membranes, made of PVDF (polyvinylidene fluoride) and PUR (polyurethane). The membranes were bought from Technical University of Liberec, where they have been were produced on NanospiderTM - NS 4S1000U setup. The samples were produced at various speeds of substrate (10, 25 and 50 mm/min). By the gravimetric analysis we have found the linear dependence of grammage (mass per square meter) on inversed speed of substrate. The nanofiber structure was observed by electron scanning microscope (SEM) Tescan Maia 3. Subsequently cross sections of the sample were obtained by various methods. The thickness and internal structure of the membrane was determined from these cross sections. It was found that the internal structure is very similar to the surface structure. Based on these observations we have determined parameters important for development of a 3D model of the nanofiber network.
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27

Batra, Renu, Reza Khayat, and Liang Tong. "Structural Studies of Herpesvirus Proteases." Protein & Peptide Letters 8, no. 5 (October 1, 2001): 333–42. http://dx.doi.org/10.2174/0929866013409229.

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28

Depmeier, W. "Structural studies on aluminate sodalites." Acta Crystallographica Section A Foundations of Crystallography 43, a1 (August 12, 1987): C148. http://dx.doi.org/10.1107/s0108767387081492.

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29

Srikrishnan, T. "Structural studies on immuno-modulators." Acta Crystallographica Section A Foundations of Crystallography 43, a1 (August 12, 1987): C60. http://dx.doi.org/10.1107/s0108767387083909.

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30

Soriano, E., E. Settembre, T. P. Begley, and S. E. Ealick. "Structural studies of quinolinate synthase." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c251. http://dx.doi.org/10.1107/s0108767305089300.

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31

Kuzel, R. "Structural studies of nanocrystalline metals." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c79. http://dx.doi.org/10.1107/s0108767305096686.

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32

Englert, U., I. Kalf, and R. Wang. "Structural studies of chiral resolution." Acta Crystallographica Section A Foundations of Crystallography 62, a1 (August 6, 2006): s169. http://dx.doi.org/10.1107/s0108767306096620.

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33

Walls, Andrew F. "Structural Problems in Mission Studies." International Bulletin of Missionary Research 15, no. 4 (October 1991): 146–55. http://dx.doi.org/10.1177/239693939101500401.

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34

LESLIE, ANDREW G. W., and WILLIAM V. SHAW. "Structural studies of chloramphenicol acetyltransferase." Biochemical Society Transactions 14, no. 6 (December 1, 1986): 1224–25. http://dx.doi.org/10.1042/bst0141224a.

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35

Randazzo, Antonio, Veronica Esposito, Oliver Ohlenschläger, Ramadurai Ramachandran, Antonella Virgilio, and Luciano Mayol. "STRUCTURAL STUDIES ON LNA QUADRUPLEXES." Nucleosides, Nucleotides & Nucleic Acids 24, no. 5-7 (April 1, 2005): 795–800. http://dx.doi.org/10.1081/ncn-200060279.

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36

GUSTAFSSON, T., E. GARFUNKEL, E. P. GUSEV, P. HÄBERLE, H. C. LU, and J. B. ZHOU. "STRUCTURAL STUDIES OF OXIDE SURFACES." Surface Review and Letters 03, no. 04 (August 1996): 1561–65. http://dx.doi.org/10.1142/s0218625x96002552.

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We review some recent ion scattering experiments on the structure of oxide surfaces. We show that the MgO(100) surface exhibits very small surface distortions, in agreement with recent theoretical work. For the case of the oxidation of Si(100), we show that the oxidation proceeds in three different spatially separate regions, something which disagrees with the conventional model for silicon oxidation.
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37

Barrett, P. A., and R. H. Jones. "Structural studies of DAF-4." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C401. http://dx.doi.org/10.1107/s0108767396083456.

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38

Suwalsky, M., F. Villena, B. Ungerer, and C. P. Sotomayor. "Structural studies on phospholipid bilayers." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C273. http://dx.doi.org/10.1107/s0108767396088563.

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39

Heine, A., E. A. Stura, K. D. Janda, C. F. Barbas III, R. A. Lerner, and I. A. Wilson. "Structural studies of catalytic antibodies." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C220. http://dx.doi.org/10.1107/s0108767396090587.

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40

WU, H., Y. C. PARK, H. YE, and L. TONG. "Structural Studies of Human TRAF2." Cold Spring Harbor Symposia on Quantitative Biology 64 (January 1, 1999): 541–50. http://dx.doi.org/10.1101/sqb.1999.64.541.

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41

Jedrzejas, Mark J., and Laurent Chantalat. "Structural studies ofStreptococcus agalactiaehyaluronate lyase." Acta Crystallographica Section D Biological Crystallography 56, no. 4 (April 1, 2000): 460–63. http://dx.doi.org/10.1107/s0907444900000706.

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42

Battisti, A. J., Y. K. Chu, P. R. Chipman, B. Kaufmann, C. B. Jonsson, and M. G. Rossmann. "Structural Studies of Hantaan Virus." Journal of Virology 85, no. 2 (November 10, 2010): 835–41. http://dx.doi.org/10.1128/jvi.01847-10.

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43

Mondragón, Alfonso. "Structural Studies of RNase P." Annual Review of Biophysics 42, no. 1 (May 6, 2013): 537–57. http://dx.doi.org/10.1146/annurev-biophys-083012-130406.

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44

Amano, Ken-ichi, and Yoshiko Shibata. "Structural Studies of Peptidoglycans inCampylobacterSpecies." Microbiology and Immunology 36, no. 9 (September 1992): 961–67. http://dx.doi.org/10.1111/j.1348-0421.1992.tb02099.x.

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45

GOTO, KASHIKO, NORIKO TAKAHASHI, and TAKASHI MURACHI. "STRUCTURAL STUDIES ON STEM BROMELAIN." International Journal of Peptide and Protein Research 15, no. 4 (January 12, 2009): 335–41. http://dx.doi.org/10.1111/j.1399-3011.1980.tb02910.x.

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46

Wong, Kathy, Yinglu Zhang, Guennadi Kozlov, and Kalle Gehring. "Structural studies of Legionella effectors." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C583. http://dx.doi.org/10.1107/s2053273314094169.

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Legionella pneumophila is a gram-negative bacterium that causes Legionnaires' disease. It uses a Dot/Icm type IV secretion system to inject effector proteins into the host cell to manipulate host processes. Currently, about 300 Icm/Dot dependent effectors of L.pneumophila have been identified. Lpg1496 is an effector protein, which contains a conserved domain from the SidE family. To date, the middle domain and the conserved SidE domain have been crystallized and the structure solved at a resolution of 1.15Å and 2.3Å, respectively. A structural homology search using the middle domain suggested a similarity to phosphoribosylaminoimidazolesuccinocarboxamide (SAICAR) synthase, an ATPase involved in purine nucleotide synthesis. We performed 1H–15N HSQC NMR titrations to show that this domain binds ATP, ADP and AMP, with the highest binding affinity for ADP. A structural homology search using the SidE domain showed a similarity to cyclic nucleotide phosphodiesterases. To further elucidate the function of lpg1496, other fragments have been cloned, expressed, and subjected to crystallization trials. Currently, we have successfully crystallized the N-terminal domain, with crystals diffracting to <2.0Å. Obtaining the crystal structure of lpg1496 and revealing its function will not only lead to a better understanding of the virulence of L. pneumophila, but also contribute to the development of novel therapeutic treatments of Legionnaires' disease.
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47

Peek, James, and Dinesh Christendat. "Structural studies on dehydroshikimate dehydratase." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C475. http://dx.doi.org/10.1107/s2053273314095242.

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The soil bacterium, Pseudomonas putida, is capable of using the alicyclic compound quinate as a sole carbon source. During this process, quinate is converted to 3-dehydroshikimate, which subsequently undergoes a dehydration to form protocatechuate. The latter transformation is performed by the enzyme dehydroshikimate dehydratase (DSD). We have recombinantly produced DSD from P. putida and are currently performing x-ray crystallographic studies on the enzyme to gain structural insight into its catalytic mechanism and mode of substrate recognition. Initial crystals of DSD diffracted to 2.7 Ä resolution, but exhibited strong twinning. A redesigned construct has recently yielded crystals that diffract to similar resolution, but with a significantly reduced tendency toward twinning. Interestingly, sequence analysis of P. putida DSD reveals that the protein is in fact a fusion of two distinct domains: an N-terminal sugar phosphate isomerase-like domain associated with DSD activity, and a C-terminal hydroxyphenylpyruvate dioxygenase (HPPD)-like domain with unknown functional significance. Structural characterization of the protein may provide novel insight into the functional relevance of the unusual HPPD-like domain.
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48

Wu, Guojie, Adam J. Quek, Tom T. Caradoc-Davies, Sue M. Ekkel, Blake Mazzitelli, James C. Whisstock, and Ruby H. P. Law. "Structural studies of plasmin inhibition." Biochemical Society Transactions 47, no. 2 (March 5, 2019): 541–57. http://dx.doi.org/10.1042/bst20180211.

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Abstract Plasminogen (Plg) is the zymogen form of the serine protease plasmin (Plm), and it plays a crucial role in fibrinolysis as well as wound healing, immunity, tissue remodeling and inflammation. Binding to the targets via the lysine-binding sites allows for Plg activation by plasminogen activators (PAs) present on the same target. Cellular uptake of fibrin degradation products leads to apoptosis, which represents one of the pathways for cross-talk between fibrinolysis and tissue remodeling. Therapeutic manipulation of Plm activity plays a vital role in the treatments of a range of diseases, whereas Plm inhibitors are used in trauma and surgeries as antifibrinolytic agents. Plm inhibitors are also used in conditions such as angioedema, menorrhagia and melasma. Here, we review the rationale for the further development of new Plm inhibitors, with a particular focus on the structural studies of the active site inhibitors of Plm. We compare the binding mode of different classes of inhibitors and comment on how it relates to their efficacy, as well as possible future developments.
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49

Nelson, D. D., W. Klemperer, G. T. Fraser, F. J. Lovas, and R. D. Suenram. "Ammonia dimer: Further structural studies." Journal of Chemical Physics 87, no. 11 (December 1987): 6364–72. http://dx.doi.org/10.1063/1.453466.

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50

Klapproth, A., E. Goreshnik, D. Staykova, H. Klein, and W. F. Kuhs. "Structural studies of gas hydrates." Canadian Journal of Physics 81, no. 1-2 (January 1, 2003): 503–18. http://dx.doi.org/10.1139/p03-024.

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An overview of recent structural work focusing on the gas hydrates of methane and carbon dioxide is given. Both the crystal structure and the microstructure are considered. We report on the pressure-dependent molecular structure of methane clathrate hydrate using laboratory-made hydrogenous and deuterated samples investigated by neutron and hard-X-ray synchrotron diffraction experiments. The isothermal compressibilities are determined for hydrogenated and deuterated CH4 hydrate, and isotopic differences between both compounds are established for the first time. The cage filling of carbon dioxide and methane hydrate is determined and compared with predictions from statistical thermodynamic theory. In the case of small cages in methane hydrate, experimental results and predictions do not agree. Field-emission scanning electron microscopy reveals the meso- to macro-porous nature of gas hydrates formed with an excess of free gas. Furthermore, in situ measurements of the formation kinetics of porous hydrates are reported in which differences between methane and carbon dioxide are established quantitatively and the transient existence of a type II carbon dioxide structure is found. PACS Nos.: 82.75-z, 61.10Nz, 61.12Ld, 68.37Hk
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