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Journal articles on the topic 'NTS2'

Author: Grafiati

Published: 4 June 2021

Last updated: 8 February 2022

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1

Boules, Mona, Paul Fredrickson, and Elliott Richelson. "An NTS2 Analog Enhances the Analgesic Effects of Morphine in an Animal Model of Persistent Pain and Does not Exhibit Tolerance." Open Pain Journal 7, no. 1 (November 14, 2014): 23–28. http://dx.doi.org/10.2174/1876386301407010023.

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The analgesic efficacy of neurotensin agonists depends on their activation of two receptor subtypes, NTS1 and/or NTS2. In this study we determined the role of NTS2 in an animal model of persistent pain (intraplantar injection of formalin) with the use of the NTS2-selective analog, NT79 and NTS2-knockout mice (NTS2-/-). Wild type (WT) and NTS2-/- mice were pretreated with NT79 and tested for formalin-induced lifting and biting. Additionally, the effect of repeated administration of NT79 and morphine alone and in combination was determined in WT mice. Intraplantar injection of formalin produced the typical biphasic nociceptive response of this persistent pain model. Formalin evoked lower pain intensity in NTS2-/- mice as compared to that for WT mice. Pretreatment with NT79 attenuated formalininduced nociception throughout phase II in the WT mice, and in early phase II in the NTS2-/- mice. Lifting and biting responses were attenuated, indicating spinal and supra-spinal modulation of persistent nociception. More importantly, repeated injection of NT79 enhanced, while that of morphine reduced their antinociceptive effects, respectively. Subchronic co-administration of NT79 and morphine enhanced the analgesic effect over either drug alone. These data support the role of NTS2 in modulating formalin-induced pain. Additionally, these data provide a rationale for the potential therapeutic role of NTS2-selective analogs in chronic pain management alone or in combination with morphine and without the development of tolerance.

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2

Schulz, Stefan, Christoph Röcken, Matthias P. A. Ebert, and Solveig Schulz. "Immunocytochemical identification of low-affinity NTS2 neurotensin receptors in parietal cells of human gastric mucosa." Journal of Endocrinology 191, no. 1 (October 2006): 121–28. http://dx.doi.org/10.1677/joe.1.06903.

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The biological effects of neurotensin (NT) are mediated by two distinct G protein-coupled receptors, NTS1 and NTS2. Although it is well established that neurotensin inhibits gastric acid secretion in man, the plasma membrane receptor mediating these effects has not been visualized yet. We developed and characterized a novel antipeptide antibody to the carboxy-terminal region of the human NTS2 receptor. The cellular and subcellular distribution of NTS2 receptors was evaluated in various human gastrointestinal tissues. Specificity of the antiserum was demonstrated by (1) detection of a broadband migrating at Mr 90 000–100 000 in Western blots of membranes from NTS2-expressing tissues; (2) cell-surface staining of NTS2-transfected cells; (3) translocation of NTS2 receptor immunostaining after agonist exposure; and (4) abolition of tissue immunostaining by preadsorbtion of the antibody with its immunizing peptide. In the gastrointestinal tract, NTS2 receptor immunoreactivity was highly abundant in parietal cells of the gastric mucosa, in neuroendocrine cells of the stomach small and large intestine, and in cells of the exocrine pancreas. NTS2 receptors were clearly located in the plasma membrane and uniformly present on nearly all target cells. The presence of NTS2 receptors was rarely detected in human tumors. This is the first localization of NTS2 receptors in human formalin-fixed, paraffin-embedded tissues at the cellular level. The abundant expression of low-affinity NTS2 receptors on the plasma membrane of human parietal cells provides a morphological substrate for the direct inhibition of gastric acid secretion observed after i.v. administration of neurotensin.

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3

Kobayashi, Takehiko, Masayasu Nomura, and Takashi Horiuchi. "Identification of DNA cis Elements Essential for Expansion of Ribosomal DNA Repeats inSaccharomyces cerevisiae." Molecular and Cellular Biology 21, no. 1 (January 1, 2001): 136–47. http://dx.doi.org/10.1128/mcb.21.1.136-147.2001.

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ABSTRACT Saccharomyces cerevisiae carries ∼150 ribosomal DNA (rDNA) copies in tandem repeats. Each repeat consists of the 35S rRNA gene, the NTS1 spacer, the 5S rRNA gene, and the NTS2 spacer. TheFOB1 gene was previously shown to be required for replication fork block (RFB) activity at the RFB site in NTS1, for recombination hot spot (HOT1) activity, and for rDNA repeat expansion and contraction. We have constructed a strain in which the majority of rDNA repeats are deleted, leaving two copies of rDNA covering the 5S-NTS2-35S region and a single intact NTS1, and whose growth is supported by a helper plasmid carrying, in addition to the 5S rRNA gene, the 35S rRNA coding region fused to the GAL7promoter. This strain carries a fob1 mutation, and an extensive expansion of chromosomal rDNA repeats was demonstrated by introducing the missing FOB1 gene by transformation. Mutational analysis using this system showed that not only the RFB site but also the adjacent ∼400-bp region in NTS1 (together called the EXP region) are required for the FOB1-dependent repeat expansion. This ∼400-bp DNA element is not required for the RFB activity or the HOT1 activity and therefore defines a function unique to rDNA repeat expansion (and presumably contraction) separate from HOT1 and RFB activities.

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4

Mazella, Jean, and Jean-Pierre Vincent. "Functional roles of the NTS2 and NTS3 receptors." Peptides 27, no. 10 (October 2006): 2469–75. http://dx.doi.org/10.1016/j.peptides.2006.04.026.

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5

Kitabgi, Patrick. "Inverse agonism at neurotensin receptors NTS1 and NTS2." International Congress Series 1249 (August 2003): 207–16. http://dx.doi.org/10.1016/s0531-5131(03)00604-6.

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6

Li, Shanshan, Jonathan D. Geiger, and Saobo Lei. "Neurotensin Enhances GABAergic Activity in Rat Hippocampus CA1 Region by Modulating L-Type Calcium Channels." Journal of Neurophysiology 99, no. 5 (May 2008): 2134–43. http://dx.doi.org/10.1152/jn.00890.2007.

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Neurotensin (NT) is a tridecapeptide that interacts with three NT receptors; NTS1, NTS2, and NTS3. Although NT has been reported to modulate GABAergic activity in the brain, the underlying cellular and molecular mechanisms of NT are elusive. Here, we examined the effects of NT on GABAergic transmission and the involved cellular and signaling mechanisms of NT in the hippocampus. Application of NT dose-dependently increased the frequency of spontaneous inhibitory postsynaptic currents (sIPSCs) recorded from CA1 pyramidal neurons with no effects on the amplitude of sIPSCs. NT did not change either the frequency or the amplitude of miniature (m)IPSCs recorded in the presence of tetrodotoxin. Triple immunofluorescent staining of recorded interneurons demonstrated the expression of NTS1 on GABAergic interneurons. NT increased the action potential firing rate but decreased the afterhyperpolarization (AHP) amplitude in identified CA1 interneurons. Application of L-type calcium channel blockers (nimodipine and nifedipine) abolished NT-induced increases in action potential firing rate and sIPSC frequency and reduction in AHP amplitude, suggesting that the effects of NT are mediated by interaction with L-type Ca2+ channels. NT-induced increase in sIPSC frequency was blocked by application of the specific NTS1 antagonist SR48692, the phospholipase C (PLC) inhibitor U73122, the IP3 receptor antagonist 2-APB, and the protein kinase C inhibitor GF109203X, suggesting that NT increases γ-aminobutyric acid release via a PLC pathway. Our results provide a cellular mechanism by which NT controls GABAergic neuronal activity in hippocampus.

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7

Nguyen, Huu-Vang, Andrea Pulvirenti, and Claude Gaillardin. "Rapid differentiation of the closely related Kluyveromyces lactis var. lactis and K. marxianus strains isolated from dairy products using selective media and PCR/RFLP of the rDNA non transcribed spacer 2." Canadian Journal of Microbiology 46, no. 12 (December 1, 2000): 1115–22. http://dx.doi.org/10.1139/w00-107.

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PCR/RFLP of the NTS2 (IGS2) of rDNA was applied to differentiate two closely related yeast species, Kluyveromyces lactis var. lactis (referred to as K. lactis) and K. marxianus. Using specific primers, the NTS2 region was amplified from DNA of both K. lactis and K. marxianus type and collection strains. AluI restriction of amplified fragments generated patterns characteristic for each species. The NTS2 region from K. lactis var. drosophilarum and related species K. aestuarii, K. africanus, K. dobzhanskii, and K. wickerhamii could also be amplified with the same primers, but AluI patterns generated were clearly different. PCR/RFLP of the NTS2 appears thus to be a convenient method for rapid identification of K. lactis and K. marxianus, frequently found in dairy products. This test was validated therefore on K. lactis and K. marxianus from natural habitats. We showed that all yeast strains collected from whey samples and scoring blue on X-gal glucose plates were either K. lactis or K. marxianus. For application purposes, we propose here an approach for quickly screening for K. lactis/marxianus and Saccharomyces cerevisiae in dairy products using X-gal coloured and lysine growth media.Key words: yeast, Kluyveromyces, ribosomal DNA, karyotype, taxonomy.

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8

Pulvirenti, Andrea, Lisa Solieri, Luciana De Vero, and Paolo Giudici. "Limitations on the use of polymerase chain reaction – restriction fragment length polymorphism analysis of the rDNA NTS2 region for the taxonomic classification of the speciesSaccharomyces cerevisiae." Canadian Journal of Microbiology 51, no. 9 (September 1, 2005): 759–64. http://dx.doi.org/10.1139/w05-062.

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Different molecular techniques were tested to determine which was the most effective in the identification of Saccharomyces cerevisiae strains. In particular, polymerase chain reaction – restriction fragment length polymorphism (PCR–RFLP) analysis of the internal transcribed spacer (ITS) regions and the nontranscribed spacer 2 (NTS2) region, sequencing of the D1/D2 domain, and electrophoretic karyotyping were applied to 123 yeast strains isolated from different sourdoughs and tentatively attributed to the species S. cerevisiae. All of the strains tested showed an identical PCR–RFLP pattern for the ITS regions, an identical nucleotide sequence of the D1/D2 domain, and the typical electrophoretic karyo type of S. cerevisiae. In contrast, 14 out of the 123 strains tested showed some polymorphism with BanI restriction analysis of the NTS2 region. Our results indicate that while the sequencing of the D1/D2 domain, the PCR–RFLP analysis of the ITS regions, and the electrophoretic karyotype can be employed successfully to identify S. cere visiae strains, PCR–RFLP analysis of the NTS2 region does not allow a consistent and accurate grouping for S. cere visiae strains. The fact that the NTS2 region of a small number of strains (8.78% of the total strains tested) is different from that of the other S. cerevisiae strains confirms that molecular methods should always be tested on a great number of strains.Key words: ribosomal DNA, Saccharomyces cerevisiae, yeast identification.

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9

Liang, Yanqi, Mona Boules, Zhimin Li, Katrina Williams, Tomofumi Miura, Alfredo Oliveros, and Elliott Richelson. "Hyperactivity of the dopaminergic system in NTS1 and NTS2 null mice." Neuropharmacology 58, no. 8 (June 2010): 1199–205. http://dx.doi.org/10.1016/j.neuropharm.2010.02.015.

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10

Perron, Amélie, Nadder Sharif, Philippe Sarret, Thomas Stroh, and Alain Beaudet. "NTS2 modulates the intracellular distribution and trafficking of NTS1 via heterodimerization." Biochemical and Biophysical Research Communications 353, no. 3 (February 2007): 582–90. http://dx.doi.org/10.1016/j.bbrc.2006.12.062.

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11

Reefman, D., J. Baak, H. B. Brom, and G. A. Wiegers. "Superconductivity in misfit layer compounds (MS)nTS2." Solid State Communications 75, no. 1 (July 1990): 47–51. http://dx.doi.org/10.1016/0038-1098(90)90155-5.

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12

Rossetti, Karina de Vares, José Frederico Centurion, and Eurico Lucas de Sousa Neto. "Physical quality of an Oxisol after different periods of management systems." Revista Brasileira de Ciência do Solo 37, no. 6 (December 2013): 1522–34. http://dx.doi.org/10.1590/s0100-06832013000600009.

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Management systems may lead to a loss of soil physical quality as a result of removal of the plant cover and excessive agricultural mechanization. The hypothesis of this study was that the soil aggregate stability, bulk density, macro- and microporosity, and the S index and saturated hydraulic conductivity may be used as indicators of the soil physical quality. The aim was to study the effects of different periods and managements on the physical attributes of a medium-textured Red Oxisol under soybean and corn for two growing seasons, and determine which layers are most susceptible to variations. A completely randomized experimental design was used with split plots (five treatments and four layers), with four replications. The treatments in 2008/09 consisted of: five years of no-tillage (NTS5), seven years of no-tillage (NTS7), nine years of no-tillage (NTS9), conventional tillage (CTS) and an adjacent area of native forest (NF). The treatments were extended for another year, identified in 2009/10 as: NTS6, NTS8, NTS10, CTS and NF. The soil layers 0-0.05, 0.05-0.10, 0.10-0.20 and 0.20-0.30 m were sampled. The highest S index values were observed in the treatment CTS in the 0-0.05 m layer (0.106) and the 0.05-0.10 m layer (0.099) in 2008/09, and in the 0-0.05 m layer (0.066) in 2009/10. This fact may be associated with soil turnover, resulting in high macroporosity in this treatment. In contrast, in the NTS, limiting macroporosity values were observed in some layers (below 0.10 m³ m-3). Highest aggregate stability as well as the highest saturated hydraulic conductivity (Kθ) values were observed in NF in relation to the other treatments. In 2009/10, the Kθ in NF differed only from NTS10. This study showed that the use of the S index alone cannot be recommended as an absolute indicator of the soil physical quality, even at values greater than 0.035.

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13

Lafrance, M., G. Roussy, K. Belleville, H. Maeno, N. Beaudet, K. Wada, and P. Sarret. "Involvement of NTS2 receptors in stress-induced analgesia." Neuroscience 166, no. 2 (March 2010): 639–52. http://dx.doi.org/10.1016/j.neuroscience.2009.12.042.

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14

Sarret, Philippe, Nicolas Beaudet, and Geneviève Roussy. "Le récepteur NTS2 : un frein à la douleur." médecine/sciences 23, no. 1 (January 2007): 11–12. http://dx.doi.org/10.1051/medsci/200723111.

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15

Simeth, Nadja A., Manuel Bause, Michael Dobmeier, Ralf C. Kling, Daniel Lachmann, Harald Hübner, Jürgen Einsiedel, Peter Gmeiner, and Burkhard König. "NTS2-selective neurotensin mimetics with tetrahydrofuran amino acids." Bioorganic & Medicinal Chemistry 25, no. 1 (January 2017): 350–59. http://dx.doi.org/10.1016/j.bmc.2016.10.039.

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16

Oliveros, A., M. G. Heckman, M. del Pilar Corena-McLeod, K. Williams, M. Boules, and E. Richelson. "Sensorimotor gating in NTS1 and NTS2 null mice: effects of d-amphetamine, dizocilpine, clozapine and NT69L." Journal of Experimental Biology 213, no. 24 (November 26, 2010): 4232–39. http://dx.doi.org/10.1242/jeb.046318.

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17

Smith, Kristin E., Mona Boules, Katrina Williams, and Elliott Richelson. "NTS1 and NTS2 mediate analgesia following neurotensin analog treatment in a mouse model for visceral pain." Behavioural Brain Research 232, no. 1 (June 2012): 93–97. http://dx.doi.org/10.1016/j.bbr.2012.03.044.

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18

Tétreault, Pascal, Nicolas Beaudet, Amélie Perron, Karine Belleville, Adeline René, Florine Cavelier, Jean Martinez, et al. "Spinal NTS2 receptor activation reverses signs of neuropathic pain." FASEB Journal 27, no. 9 (June 11, 2013): 3741–52. http://dx.doi.org/10.1096/fj.12-225540.

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19

Reefman, D., P. Koorevaar, H. B. Brom, and G. A. Wiegers. "Superconductivity and fluctuations in misfit layer compounds (MS)nTS2." Synthetic Metals 43, no. 3 (June 1991): 3775–80. http://dx.doi.org/10.1016/0379-6779(91)91679-5.

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20

Fanelli, Roberto, Nicolas Floquet, Élie Besserer-Offroy, Bartholomé Delort, Mélanie Vivancos, Jean-Michel Longpré, Pedro Renault, Jean Martinez, Philippe Sarret, and Florine Cavelier. "Use of Molecular Modeling to Design Selective NTS2 Neurotensin Analogues." Journal of Medicinal Chemistry 60, no. 8 (April 10, 2017): 3303–13. http://dx.doi.org/10.1021/acs.jmedchem.6b01848.

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21

Sarret, P. "Potent Spinal Analgesia Elicited through Stimulation of NTS2 Neurotensin Receptors." Journal of Neuroscience 25, no. 36 (September 7, 2005): 8188–96. http://dx.doi.org/10.1523/jneurosci.0810-05.2005.

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22

Perron, Amélie, Nadder Sharif, Louis Gendron, Mariette Lavallée, Thomas Stroh, Jean Mazella, and Alain Beaudet. "Sustained neurotensin exposure promotes cell surface recruitment of NTS2 receptors." Biochemical and Biophysical Research Communications 343, no. 3 (May 2006): 799–808. http://dx.doi.org/10.1016/j.bbrc.2006.03.047.

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23

Held, Cornelia, Manuel Plomer, Harald Hübner, Jasmin Meltretter, Monika Pischetsrieder, and Peter Gmeiner. "Development of a Metabolically Stable Neurotensin Receptor 2 (NTS2) Ligand." ChemMedChem 8, no. 1 (October 24, 2012): 75–81. http://dx.doi.org/10.1002/cmdc.201200376.

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24

Asselin, Marie-Liesse, Isabelle Dubuc, Antoine Coquerel, and Jean Costentin. "Localization of neurotensin NTS2 receptors in rat brain, using [3H]levocabastine." Neuroreport 12, no. 5 (April 2001): 1087–91. http://dx.doi.org/10.1097/00001756-200104170-00044.

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25

Tóth, Fanni, Jayapal Reddy Mallareddy, Dirk Tourwé, Andrzej W. Lipkowski, Magdalena Bujalska-Zadrozny, Sándor Benyhe, Steven Ballet, Géza Tóth, and Patrycja Kleczkowska. "Synthesis and binding characteristics of [3H]neuromedin N, a NTS2 receptor ligand." Neuropeptides 57 (June 2016): 15–20. http://dx.doi.org/10.1016/j.npep.2015.12.004.

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26

Sarret, Philippe, Am�lie Perron, Thomas Stroh, and Alain Beaudet. "Immunohistochemical distribution of NTS2 neurotensin receptors in the rat central nervous system." Journal of Comparative Neurology 461, no. 4 (May 8, 2003): 520–38. http://dx.doi.org/10.1002/cne.10718.

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27

Sarret, Philippe, Louis Gendron, Peter Kilian, Ha Minh Ky Nguyen, Nicole Gallo-Payet, Marcel-Daniel Payet, and Alain Beaudet. "Pharmacology and Functional Properties of NTS2 Neurotensin Receptors in Cerebellar Granule Cells." Journal of Biological Chemistry 277, no. 39 (June 25, 2002): 36233–43. http://dx.doi.org/10.1074/jbc.m202586200.

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28

Gutnisky, Alicia, María Graciela López Ordieres, and Georgina Rodríguez de Lores Arnaiz. "The Administration of Levocabastine, a NTS2 Receptor Antagonist, Modifies Na+, K+-ATPase Properties." Neurochemical Research 41, no. 6 (January 7, 2016): 1274–80. http://dx.doi.org/10.1007/s11064-015-1823-7.

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29

Lisowski, Pawel, Adrian Stankiewicz, Grzegorz Juszczak, Marek Wieczorek, and Artur H. Swiergiel. "Hippocampal transcriptome associated with stress-induced analgesia phenotype in mice – involvement of nts2 receptors." Pharmacological Reports 63, no. 1 (January 2011): 247. http://dx.doi.org/10.1016/s1734-1140(11)70471-6.

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30

Roussy, Geneviève, Marc-André Dansereau, Stéphanie Baudisson, Faouzi Ezzoubaa, Karine Belleville, Nicolas Beaudet, Jean Martinez, Elliott Richelson, and Philippe Sarret. "Evidence for a Role of NTS2 Receptors in the Modulation of Tonic Pain Sensitivity." Molecular Pain 5 (January 2009): 1744–8069. http://dx.doi.org/10.1186/1744-8069-5-38.

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31

Chartier, Magali, Michael Desgagné, Marc Sousbie, Charles Rumsby, Lucie Chevillard, Léa Théroux, Lounès Haroune, et al. "Pharmacodynamic and pharmacokinetic profiles of a neurotensin receptor type 2 (NTS2) analgesic macrocyclic analog." Biomedicine & Pharmacotherapy 141 (September 2021): 111861. http://dx.doi.org/10.1016/j.biopha.2021.111861.

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32

Gendron, Louis, Amélie Perron, Marcel Daniel Payet, Nicole Gallo-Payet, Philippe Sarret, and Alain Beaudet. "Low-Affinity Neurotensin Receptor (NTS2) Signaling: Internalization-Dependent Activation of Extracellular Signal-Regulated Kinases 1/2." Molecular Pharmacology 66, no. 6 (September 10, 2004): 1421–30. http://dx.doi.org/10.1124/mol.104.002303.

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33

Held, Cornelia, Harald Hübner, Ralf Kling, Yvonne A. Nagel, Helma Wennemers, and Peter Gmeiner. "Impact of the Proline Residue on Ligand Binding of Neurotensin Receptor 2 (NTS2)-Selective Peptide-Peptoid Hybrids." ChemMedChem 8, no. 5 (March 26, 2013): 772–78. http://dx.doi.org/10.1002/cmdc.201300054.

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34

Belmeguenai, Amor, Hubert Vaudry, Jérôme Leprince, Bertrand Vivet, Florine Cavelier, Jean Martinez, and Estelle Louiset. "Neurotensin Modulates the Electrical Activity of Frog Pituitary Melanotropes via Activation of a G-Protein-Coupled Receptor Pharmacologically Related to Both the NTS1 and nts2 Receptors of Mammals." Neuroendocrinology 72, no. 6 (2000): 379–91. http://dx.doi.org/10.1159/000054607.

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35

Bredeloux, Pierre, Jean Costentin, and Isabelle Dubuc. "Interactions between NTS2 neurotensin and opioid receptors on two nociceptive responses assessed on the hot plate test in mice." Behavioural Brain Research 175, no. 2 (December 2006): 399–407. http://dx.doi.org/10.1016/j.bbr.2006.09.016.

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36

Gressier, P., P. Rabu, A. Meerschaut, L. Guemas, and J. Rouxel. "Misfit layer compounds family (MS)nTS2(M = Sn, Pb, Bi, rare earth element;T= Nb, Ta;n= 1.08–1.19)." Phase Transitions 30, no. 1-4 (April 1991): 39–47. http://dx.doi.org/10.1080/01411599108207962.

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37

Smith, Kristin E., Mona Boules, Katrina Williams, Abdul H. Fauq, and Elliott Richelson. "The role of NTS2 in the development of tolerance to NT69L in mouse models for hypothermia and thermal analgesia." Behavioural Brain Research 224, no. 2 (October 2011): 344–49. http://dx.doi.org/10.1016/j.bbr.2011.06.014.

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38

Eiselt, Emilie, Simon Gonzalez, Charlotte Martin, Magali Chartier, Cecilia Betti, Jean-Michel Longpré, Florine Cavelier, et al. "Neurotensin Analogues Containing Cyclic Surrogates of Tyrosine at Position 11 Improve NTS2 Selectivity Leading to Analgesia without Hypotension and Hypothermia." ACS Chemical Neuroscience 10, no. 11 (October 7, 2019): 4535–44. http://dx.doi.org/10.1021/acschemneuro.9b00390.

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39

Perron, Amélie, Philippe Sarret, Louis Gendron, Thomas Stroh, and Alain Beaudet. "Identification and Functional Characterization of a 5-Transmembrane Domain Variant Isoform of the NTS2 Neurotensin Receptor in Rat Central Nervous System." Journal of Biological Chemistry 280, no. 11 (January 6, 2005): 10219–27. http://dx.doi.org/10.1074/jbc.m410557200.

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40

Ruscher, C. H., C. Haas, S. van Smaalen, and G. A. Wiegers. "Investigation of the optical reflectivity of misfit layer compounds: (MS)nTS2(T=Ta, Nb; M=Sn, Pb, Sm, Tb, La; 1.08." Journal of Physics: Condensed Matter 6, no. 10 (March 7, 1994): 2117–28. http://dx.doi.org/10.1088/0953-8984/6/10/029.

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41

Wiegers, G. A., and A. Meerschaut. "Structures of misfit layer compounds (MS)nTS2 (M Sn, Pb, Bi, rare earth metals; TNb, Ta, Ti, V, Cr; 1.08." Journal of Alloys and Compounds 178, no. 1-2 (February 1992): 351–68. http://dx.doi.org/10.1016/0925-8388(92)90276-f.

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42

Rüscher, C. H. "Optical Reflectivity and Transmissivity of Misfit Layer Compounds (MS)nTS2 (T  Ta, Nb; M  Pb, Sm, Tb; 1.08 < n < 1.23)." physica status solidi (b) 198, no. 2 (December 1, 1996): 889–904. http://dx.doi.org/10.1002/pssb.2221980234.

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43

Wiegers, G. A., A. Meetsma, S. van Smaalen, R. J. Haange, J. Wulff, T. Zeinstra, J. L. de Boer, et al. "Misfit layer compounds (MS)nTS2 (M = Sn, Pb, Bi, rare earth elements; T = Nb, Ta ; n = 1.08 – 1.19), a new class of layer compounds." Solid State Communications 70, no. 4 (March 1989): 409–13. http://dx.doi.org/10.1016/0038-1098(89)91069-7.

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44

Hou, I.-Ching, Chihiro Suzuki, Norimasa Kanegawa, Ayako Oda, Ayako Yamada, Masaaki Yoshikawa, Daisuke Yamada, et al. "β-Lactotensin derived from bovine β-lactoglobulin exhibits anxiolytic-like activity as an agonist for neurotensin NTS2 receptor via activation of dopamine D1 receptor in mice." Journal of Neurochemistry 119, no. 4 (October 10, 2011): 785–90. http://dx.doi.org/10.1111/j.1471-4159.2011.07472.x.

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45

WIEGERS, G. A., and A. MEERSCHAUT. "ChemInform Abstract: Structures of Misfit Layer Compounds (MS)nTS2 (M: Sn, Pb, Bi, Rare Earth Metals; T: Nb, Ta, Ti, V, Cr; 1.08 < n < 1.23)." ChemInform 23, no. 18 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199218299.

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Wiegers, G. A., A. Meetsma, S. van Smaalen, R. J. Haange, and J. L. de Boer. "Structural relationship between the orthorhombic, monoclinic and triclinic misfit layer compounds (MS)nTS2 (M = Sn, Pb, rare earth metals, T = Ti, V, Cr, Nb, Ta; 1.13 < n < 1.21)." Solid State Communications 75, no. 9 (September 1990): 689–92. http://dx.doi.org/10.1016/0038-1098(90)90227-3.

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Steggerda, Susanne M., Ben E. Black, and Bryce M. Paschal. "Monoclonal Antibodies to NTF2 Inhibit Nuclear Protein Import by Preventing Nuclear Translocation of the GTPase Ran." Molecular Biology of the Cell 11, no. 2 (February 2000): 703–19. http://dx.doi.org/10.1091/mbc.11.2.703.

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Nuclear transport factor 2 (NTF2) is a soluble transport protein originally identified by its ability to stimulate nuclear localization signal (NLS)-dependent protein import in digitonin-permeabilized cells. NTF2 has been shown to bind nuclear pore complex proteins and the GDP form of Ran in vitro. Recently, it has been reported that NTF2 can stimulate the accumulation of Ran in digitonin-permeabilized cells. Evidence that NTF2 directly mediates Ran import or that NTF2 is required to maintain the nuclear concentration of Ran in living cells has not been obtained. Here we show that cytoplasmic injection of anti-NTF2 mAbs resulted in a dramatic relocalization of Ran to the cytoplasm. This provides the first evidence that NTF2 regulates the distribution of Ran in vivo. Moreover, anti-NTF2 mAbs inhibited nuclear import of both Ran and NLS-containing protein in vitro, suggesting that NTF2 stimulates NLS-dependent protein import by driving the nuclear accumulation of Ran. We also show that biotinylated NTF2-streptavidin microinjected into the cytoplasm accumulated at the nuclear envelope, indicating that NTF2 can target a binding partner to the nuclear pore complex. Taken together, our data show that NTF2 is an essential regulator of the Ran distribution in living cells and that NTF2-mediated Ran nuclear import is required for NLS-dependent protein import.

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Jugulam and Shyam. "Non-Target-Site Resistance to Herbicides: Recent Developments." Plants 8, no. 10 (October 15, 2019): 417. http://dx.doi.org/10.3390/plants8100417.

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Non-target-site resistance (NTSR) to herbicides in weeds can be conferred as a result of the alteration of one or more physiological processes, including herbicide absorption, translocation, sequestration, and metabolism. The mechanisms of NTSR are generally more complex to decipher than target-site resistance (TSR) and can impart cross-resistance to herbicides with different modes of action. Metabolism-based NTSR has been reported in many agriculturally important weeds, although reduced translocation and sequestration of herbicides has also been found in some weeds. This review focuses on summarizing the recent advances in our understanding of the physiological, biochemical, and molecular basis of NTSR mechanisms found in weed species. Further, the importance of examining the co-existence of TSR and NTSR for the same herbicide in the same weed species and influence of environmental conditions in the altering and selection of NTSR is also discussed. Knowledge of the prevalence of NTSR mechanisms and co-existing TSR and NTSR in weeds is crucial for designing sustainable weed management strategies to discourage the further evolution and selection of herbicide resistance in weeds.

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Tsai, Rong-Tzong, Chi-Kang Tseng, Pei-Jung Lee, Hsin-Chou Chen, Ru-Huei Fu, Kae-jiun Chang, Fu-Lung Yeh, and Soo-Chen Cheng. "Dynamic Interactions of Ntr1-Ntr2 with Prp43 and with U5 Govern the Recruitment of Prp43 To Mediate Spliceosome Disassembly." Molecular and Cellular Biology 27, no. 23 (September 24, 2007): 8027–37. http://dx.doi.org/10.1128/mcb.01213-07.

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ABSTRACT The Saccharomyces cerevisiae splicing factors Ntr1 (also known as Spp382) and Ntr2 form a stable complex and can further associate with DExD/H-box RNA helicase Prp43 to form a functional complex, termed the NTR complex, which catalyzes spliceosome disassembly. We show that Prp43 interacts with Ntr1-Ntr2 in a dynamic manner. The Ntr1-Ntr2 complex can also bind to the spliceosome first, before recruiting Prp43 to catalyze disassembly. Binding of Ntr1-Ntr2 or Prp43 does not require ATP, but disassembly of the spliceosome requires hydrolysis of ATP. The NTR complex also dynamically interacts with U5 snRNP. Ntr2 interacts with U5 component Brr2 and is essential for both interactions of NTR with U5 and with the spliceosome. Ntr2 alone can also bind to U5 and to the spliceosome, suggesting a role of Ntr2 in mediating the binding of NTR to the spliceosome through its interaction with U5. Our results demonstrate that dynamic interactions of NTR with U5, through the interaction of Ntr2 with Brr2, and interactions of Ntr1 and Prp43 govern the recruitment of Prp43 to the spliceosome to mediate spliceosome disassembly.

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Al-Jamrah, Khaled Mohammed, Basheer Abdulgalil Al Nabehi, Khaled Abdullah Almoayed, Labiba Saeed Anam, and Yousef S. Khader. "Performance of the Neonatal Tetanus Surveillance System (NTSS) in Sana'a, Yemen: Evaluation Study." JMIR Public Health and Surveillance 7, no. 5 (May 4, 2021): e27606. http://dx.doi.org/10.2196/27606.

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Background The Neonatal Tetanus Surveillance System (NTSS) in Yemen was established in 2009 to identify high-risk areas, determine trends, and evaluate elimination activities. Since its launch, the NTSS had never been evaluated. Objective This study aimed to assess the performance of NTSS and determine its strengths and weaknesses to recommend improvements. Methods The US Centers for Disease Control and Prevention (CDC) guidelines were used for evaluating the NTSS. Stakeholders at the central, district, and facility levels were interviewed to rate the attributes of the NTSS. The percentage scores for attributes were ranked as poor (<60%), average (≥60% to <80%) and good (≥80%). Results The overall usefulness score percentage was 38%, which indicates a poor performance. The performance of the NTSS was rated as average on flexibility (score percent: 68%) and acceptability (score percent: 64%) attributes and poor on stability (score percentage: 33%), simplicity (score percentage: 57%), and representativeness (score percentage: 39%) attributes. About 65% of investigation forms were completed within 48 hours of notification date. Data quality was poor, as 41% of the core variables were missing. Conclusions The overall performance of the NTSS was poor. Most of the system attributes require improvement, including stability, simplicity, quality of data, and completeness of investigation. To improve the performance of NTSS, the following are recommended: capacity building of staff (focal points), strengthening NTSS through technical support and government funding to ensure its sustainability, establishing electronic investigation forms for improving the system data quality, and expansion of NTSS coverage to include all private health care facilities.

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