Academic literature on the topic 'PySC2'

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Journal articles on the topic "PySC2"

1

Dowd, S., A. A. Sneddon, and S. M. Keyse. "Isolation of the human genes encoding the pyst1 and Pyst2 phosphatases: characterisation of Pyst2 as a cytosolic dual-specificity MAP kinase phosphatase and its catalytic activation by both MAP and SAP kinases." Journal of Cell Science 111, no. 22 (November 15, 1998): 3389–99. http://dx.doi.org/10.1242/jcs.111.22.3389.

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We have isolated the human genes encoding the Pyst1 (MKP-3) and Pyst2 (MKP-X) MAP kinase phosphatases. Both genes consist of three exons interrupted by two introns and lack an intron which is conserved in all the other members of this gene family characterised to date. This reinforces the conclusion that Pyst1 and Pyst2 are members of a distinct and structurally homologous subfamily of dual-specificity (Thr/Tyr) MAP kinase phosphatases. We find that Pyst2 mRNA is constitutively expressed in a wide variety of human cell lines including those derived from ovarian, bladder and breast cancers. While there is no evidence for inducible expression of Pyst2 mRNA in human skin fibroblasts in response to cellular stress, Pyst2 mRNA levels are moderately increased in response to serum stimulation. Pyst2 protein is predominantly cytosolic when expressed in COS-1 cells. In common with Pyst1, Pyst2 shows substrate selectivity for the classical p42 (ERK2) isoform of MAP kinase both in vitro and in vivo, displaying much reduced activity towards stress activated MAP kinase isoforms such as JNK-1 and p38/RK. Pyst2 binds p42 MAP kinase in vivo and both MAP kinase binding and substrate selectivity correlate with the ability of different recombinant MAP and SAP kinases to cause catalytic activation of the Pyst2 phosphatase in vitro.
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Deng, Ji-Hua, Gui-Quan Guo, and Di-Chang Zhong. "Bis[N-aminocarbonyl-N′-(3-pyridylmethylene-κN)hydrazine]diaquabis(thiocyanato-κN)zinc(II)." Acta Crystallographica Section E Structure Reports Online 63, no. 11 (October 10, 2007): m2696—m2697. http://dx.doi.org/10.1107/s1600536807048908.

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The Zn atom of the title complex, [Zn(NCS)2(C7H8N4O)2(H2O)2] or [Zn(SCN)2(H-Pysc)2(H2O)2] [H-Pysc = N-aminocarbonyl-N′-(3-pyridylmethylene)hydrazine], derived from the condensation of pyridine-3-carbaldehyde and semicarbazone, is located at a crystallographic centre of inversion and is octahedrally coordinated by two thiocyanate anions, two aqua molecules and two molecules of the neutral Schiff base ligand H-Pysc. The Schiff base molecules act as monodentate ligands coordinating the metal through the pyridyl N atom, whereas the amide O and imine N atoms remain uncoordinated. The crystal packing is stabilized by intermolecular hydrogen bonds involving H-Pysc ligands, thiocyanate anions and water molecules.
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3

Val, D. L., A. Chapman-Smith, M. E. Walker, J. E. Cronan, and J. C. Wallace. "Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: effects on protein biotinylation." Biochemical Journal 312, no. 3 (December 15, 1995): 817–25. http://dx.doi.org/10.1042/bj3120817.

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In Saccharomyces cerevisiae there are two isoenzymes of pyruvate carboxylase (Pyc) encoded by separate genes designated PYC1 and PYC2. We report the isolation and sequencing of a PYC2 gene, and the localization of both genes on the physical map of S. cerevisiae. Comparison with the previously reported sequence [Stucka, Dequin, Salmon and Gancedo (1991) Mol. Gen. Genet. 229, 307-315] revealed significant differences within the open reading frame. The most notable difference was near the 3′ end, where we found a single base deletion reducing the open reading frame by 15 bases. We have confirmed the C-terminus of Pyc2 encoded by the gene isolated here by expressing and purifying an 86-amino-acid biotin-domain peptide. In addition, we investigated the effects of the two changes in the Pyc2 biotin domain (K1155R substitution and Q1178P/five-amino-acid extension) on the extent of biotinylation in vivo by Escherichia coli biotin ligase, and compared the biotinylation of peptides containing these changes with that of two different-length Pyc1 biotin-domain peptides. The K1155R substitution had very little effect on biotinylation, but the five-amino-acid C-terminal extension to Pyc2 and the N-terminal extension to Pycl both improved biotinylation in vivo.
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Yu, Zhaojun, Peng Jiang, and Yanmei Chen. "Crystal structure of poly[[hexaqua-1κ4O,2κ2O-bis(μ3-pyridine-2,4-dicarboxylato-1κO2:2κ2N,O2′;1′κO4)cobalt(II)strontium(II)] dihydrate]." Acta Crystallographica Section E Crystallographic Communications 71, no. 9 (August 15, 2015): m167—m168. http://dx.doi.org/10.1107/s2056989015014942.

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In the title polymeric complex, {[CoSr(C7H3NO4)2(H2O)6]·2H2O}n, the CoIIion, which is situated on a crystallographic centre of inversion, is six-coordinated by two O atoms and two N atoms from two pyridine-2,4-dicarboxylate (pydc2−) ligands and two terminal water molecules in a slightly distorted octahedral geometry, to form atrans-[Co(pydc)2(H2O)2]2−unit. The SrIIion, situated on aC2axis, is coordinated by four O atoms from four pydc2−ligands and four water molecules. The coordination geometry of the SrIIatom can be best described as a distorted dodecahedron. Each SrIIion bridges four [Co(pydc)2(H2O)2]2−units by four COO−groups of four pydc2−ligands to form a three-dimensional network structure. Two additional solvent water molecules are observed in the crystal structure and are connected to the three-dimensional coordination polymer by O—H...O hydrogen bonds. Further intra- and intermolecular O—H...O hydrogen bonds consolidate the overall structure.
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5

Yang, Yongfeng, Tao Li, and Yanmei Chen. "The first three-dimensional FeIII–SrIIheterometallic coordination polymer: poly[[diaquatetrakis(μ3-pyridine-2,3-dicarboxylato)diiron(III)strontium(II)] dihydrate]." Acta Crystallographica Section C Structural Chemistry 71, no. 10 (September 18, 2015): 903–7. http://dx.doi.org/10.1107/s2053229615016617.

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The title compound, poly[[diaqua-1κ2O-tetrakis(μ3-pyridine-2,3-dicarboxylato)-2:1:2′κ10N,O2:O2′,O3:O3′;2:1:2′κ8O3:O3′:N,O2-diiron(III)strontium(II)] dihydrate], {[Fe2Sr(C7H3O4)4(H2O)2]·2H2O}n, which has triclinic (P\overline{1}) symmetry, was prepared by the reaction of pyridine-2,3-dicarboxylic acid, SrCl2·6H2O and Fe(OAc)2(OH) (OAc is acetate) in the presence of imidazole in water at 363 K. In the crystal structure, the pyridine-2,3-dicarboxylate (pydc2−) ligand exhibits μ3-η1,η1:η1:η1and μ3-η1,η1:η1,η1:η1coordination modes, bridging two FeIIIcations and one SrIIcation. The SrIIcation, which is located on an inversion centre, is eight-coordinated by six O atoms of four pydc2−ligands and two water molecules. The coordination geometry of the SrIIcation can be best described as distorted dodecahedral. The FeIIIcation is six-coordinated by O and N atoms of four pydc2−ligands in a slightly distorted octahedral geometry. Each FeIIIcation bridges two neighbouring FeIIIcations to form a one-dimensional [Fe2(pydc)4]nchain. The chains are connected by SrIIcations to form a three-dimensional framework. The topology type of this framework istfj. The structure displays O—H...O and C—H...O hydrogen bonding.
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Sun, Qiming, Xing Zhang, Samragni Banerjee, Peng Bao, Marc Barbry, Nick S. Blunt, Nikolay A. Bogdanov, et al. "Recent developments in the PySCF program package." Journal of Chemical Physics 153, no. 2 (July 14, 2020): 024109. http://dx.doi.org/10.1063/5.0006074.

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7

Von Poelhsitz, G., B. L. Rodrigues, and A. A. Batista. "Partially oxidized ruthenium phosphine thiolates: [Ru(pySO2)0.33(pyS)1.67(dppe)] and [Ru(pySO2)0.355(pyS)1.645(dppp)]." Acta Crystallographica Section C Crystal Structure Communications 62, no. 9 (August 23, 2006): m424—m427. http://dx.doi.org/10.1107/s0108270106027491.

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Yousefi, Zakieh, Hossein Eshtiagh-Hosseini, Alireza Salimi, and Janet Soleimannejad. "(2-Aminopyrimidine-κN1)aqua(pyridine-2,6-dicarboxylato-κ3O2,N,O6)copper(II): X-ray and DFT calculated structure." Acta Crystallographica Section C Structural Chemistry 71, no. 5 (April 15, 2015): 386–93. http://dx.doi.org/10.1107/s2053229615005331.

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In the title compound, [Cu(C7H3N2O4)(C4H5N2)(H2O)], (I), pyridine-2,6-dicarboxylate (pydc2−), 2-aminopyrimidine and aqua ligands coordinate the CuIIcentre through two N atoms, two carboxylate O atoms and one water O atom, respectively, to give a nominally distorted square-pyramidal coordination geometry, a common arrangement for copper complexes containing the pydc2−ligand. Because of the presence of Cu...Xbridgedcontacts (X= N or O) between adjacent molecules in the crystal structures of (I) and three analogous previously reported compounds, and the corresponding uncertainty about the effective coordination number of the CuIIcentre, density functional theory (DFT) calculations were used to elucidate the degree of covalency in these contacts. The calculated Wiberg and Mayer bond-order indices reveal that the Cu...O contact can be considered as a coordination bond, whereas the amine group forming a Cu...N contact is not an effective participant in the coordination environment.
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Herzberg, Wiebke, and Kolja Glogowski. "Pysca – Automated frequency extraction from photometric time series." Proceedings of the International Astronomical Union 9, S301 (August 2013): 421–22. http://dx.doi.org/10.1017/s1743921313014853.

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Levy-Nissenbaum, Orlev, Shlomit Ben-Menachem, Orit Sagi-Assif, and Isaac P. Witz. "The Pyst2-L phosphatase is involved in cell-crowding." Immunology Letters 104, no. 1-2 (April 2006): 138–45. http://dx.doi.org/10.1016/j.imlet.2005.11.013.

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Dissertations / Theses on the topic "PySC2"

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Krušina, Jan. "Zlepšování systému pro automatické hraní hry Starcraft II v prostředí PySC2." Master's thesis, Vysoké učení technické v Brně. Fakulta informačních technologií, 2018. http://www.nusl.cz/ntk/nusl-385883.

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The aim of this thesis is to create an automated system for playing a real-time strategy game Starcraft II. Learning from replays via supervised learning and reinforcement learning techniques are used for improving bot's behavior. The proposed system should be capable of playing the whole game utilizing PySC2 framework for machine learning. Performance of the bot is evaluated against the built-in scripted AI in the game.
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Tschampl, Mark A. "The use of Ki to "pysch-up" and increase strength." [Ames, Iowa : Iowa State University], 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:1464399.

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Pysch, Damian [Verfasser]. "Assembly and Analysis of Alternative Emitter Systems for Silicon Solar Cells / Damian Pysch." München : Verlag Dr. Hut, 2011. http://d-nb.info/1015608159/34.

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4

Ho, Christine Kuo. "Expression, purification and characterization of the structural properties of recombinant Pysp1 and Pysp2 spidroins." Scholarly Commons, 2013. https://scholarlycommons.pacific.edu/uop_etds/846.

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Spider silk is a natural high-performance biopolymer with superior mechanical propetiies. Although these fibers out perfmm several man-made and natural biomaterials, there are cha llenges to be circumvented before commercialization. One of the silkproducing glands warranting further study is the pyrifonn gland, which produces gluelike threads functioning to cement dragline silk to substrates. We focused on the molecular properties of PySp 1, the major component of pyrifonn silk from Latrodectus hersperus, and its putative Oiiholog, PySp2, from Nephi/a clavipes. To date, there are no reports describing the secondary structure of PySp internal block repeats. Moreover, because the PySp C-terminus amino acid residues are distinct from MaSp C-terminus and the morphology of these glands is different, we hypothesized that PySp C-terminal domains form distinct secondary structures. The MaSp C-terminus has been shown to regulate the silk assembly process and whether the PySp C-terminus performs a similar function is unknown. In order to test this supposition, we used the following experimental approaches: I) we developed a series of PySp prokaryotic expression constructs carrying various block repeat modules representative of the internal iterations found within the protein chain; 2) we constructed prokaryotic expression vectors coding for the PySp C-terminal domains; 3) we expressed and purified the PySp C-terminal domains from bacteria; 4) we performed structural analyses of the purified PySp C-terminal domains using cd spectroscopy and atomic force microscopy. After expression and purification of the PySp C-tennini proteins, our studies support that this domain displays a predominantly ~-sheet structure, distinctive from the NMR-determined ahelical nature of MaSp C-tennini. The difference in secondary structure implies the MA and pyriform glands use different biochemical mechanisms during fiber extrusion to control protein folding and assembly. By investigating protein folding and fiber formation for different spider silk types, its characteristics can be customized for spinning different materials for industrial applications.
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Ho, Christine Kuo. "Expression, purification and characterization of the structural properties of recombinant Pysp1 and Pysp2 spidroins : a thesis." Scholarly Commons, 2001. https://scholarlycommons.pacific.edu/uop_etds/846.

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Spider silk is a natural high-performance biopolymer with superior mechanical propetiies. Although these fibers out perfmm several man-made and natural biomaterials, there are cha llenges to be circumvented before commercialization. One of the silkproducing glands warranting further study is the pyrifonn gland, which produces gluelike threads functioning to cement dragline silk to substrates. We focused on the molecular properties of PySp 1, the major component of pyrifonn silk from Latrodectus hersperus, and its putative Oiiholog, PySp2, from Nephi/a clavipes. To date, there are no reports describing the secondary structure of PySp internal block repeats. Moreover, because the PySp C-terminus amino acid residues are distinct from MaSp C-terminus and the morphology of these glands is different, we hypothesized that PySp C-terminal domains form distinct secondary structures. The MaSp C-terminus has been shown to regulate the silk assembly process and whether the PySp C-terminus performs a similar function is unknown. In order to test this supposition, we used the following experimental approaches: I) we developed a series of PySp prokaryotic expression constructs carrying various block repeat modules representative of the internal iterations found within the protein chain; 2) we constructed prokaryotic expression vectors coding for the PySp C-terminal domains; 3) we expressed and purified the PySp C-terminal domains from bacteria; 4) we performed structural analyses of the purified PySp C-terminal domains using cd spectroscopy and atomic force microscopy. After expression and purification of the PySp C-tennini proteins, our studies support that this domain displays a predominantly ~-sheet structure, distinctive from the NMR-determined ahelical nature of MaSp C-tennini. The difference in secondary structure implies the MA and pyriform glands use different biochemical mechanisms during fiber extrusion to control protein folding and assembly. By investigating protein folding and fiber formation for different spider silk types, its characteristics can be customized for spinning different materials for industrial applications.
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Brewster, Neil Kenneth. "Studies on the regulation of pyruvate carboxylase isozyme (PYC1 PYC2) gene expression in Saccharomyces cerevisiae /." Title page, abstract and contents only, 1994. http://web4.library.adelaide.edu.au/theses/09PH/09phb848.pdf.

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Val, Dale Lloyd Henry. "Yeast pyruvate carboxylase 2 gene (PYC2) and structure-function studies on yeast pyc isozymes / by Dale Lloyd Henry Val." 1995. http://hdl.handle.net/2440/21609.

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Books on the topic "PySC2"

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Kaplan, Harold I. Comprehensive Textbook of Pysch Volume 2. Williams Wilkins, 1985.

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Sattler, David N. Developmental Pysch In Context Plus Lifespan Development Study Guide 2nd Edition. Houghton Mifflin Company, 2006.

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Book chapters on the topic "PySC2"

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Levy-Nissenbaum, Orlev, Orit Sagi-Assif, Pia Raanani, Abraham Avigdor, Isaac Ben-Bassat, and Isaac P. Witz. "cDNA Microarray Analysis Reveals an Overexpression of the Dual-Specificity MAPK Phosphatase PYST2 in Acute Leukemia." In Methods in Enzymology, 103–13. Elsevier, 2003. http://dx.doi.org/10.1016/s0076-6879(03)66009-x.

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