Artykuły w czasopismach na temat „Phosphoesterase”
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Ogden, Kristen M., Liya Hu, Babal K. Jha, Banumathi Sankaran, Susan R. Weiss, Robert H. Silverman, John T. Patton i B. V. Venkataram Prasad. "Structural Basis for 2′-5′-Oligoadenylate Binding and Enzyme Activity of a Viral RNase L Antagonist". Journal of Virology 89, nr 13 (15.04.2015): 6633–45. http://dx.doi.org/10.1128/jvi.00701-15.
Pełny tekst źródłaYin, Yue, David Frank, Weijie Zhou, Neena Kaur, Jarrod B. French i Nick Carpino. "An unexpected 2-histidine phosphoesterase activity of suppressor of T-cell receptor signaling protein 1 contributes to the suppression of cell signaling". Journal of Biological Chemistry 295, nr 25 (5.05.2020): 8514–23. http://dx.doi.org/10.1074/jbc.ra120.013482.
Pełny tekst źródłaKatz, Michael J., Su-Young Moon, Joseph E. Mondloch, M. Hassan Beyzavi, Casey J. Stephenson, Joseph T. Hupp i Omar K. Farha. "Exploiting parameter space in MOFs: a 20-fold enhancement of phosphate-ester hydrolysis with UiO-66-NH2". Chemical Science 6, nr 4 (2015): 2286–91. http://dx.doi.org/10.1039/c4sc03613a.
Pełny tekst źródłaHan, Gye Won, Jaeju Ko, Carol L. Farr, Marc C. Deller, Qingping Xu, Hsiu-Ju Chiu, Mitchell D. Miller i in. "Crystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity". Proteins: Structure, Function, and Bioinformatics 79, nr 7 (2.05.2011): 2146–60. http://dx.doi.org/10.1002/prot.23035.
Pełny tekst źródłaLi, Xiao-Yu. "Clinical application of phosphoesterase complex in liver diseases". World Chinese Journal of Digestology 22, nr 29 (2014): 4424. http://dx.doi.org/10.11569/wcjd.v22.i29.4424.
Pełny tekst źródłaGold, Matthew G., F. Donelson Smith, John D. Scott i David Barford. "AKAP18 Contains a Phosphoesterase Domain that Binds AMP". Journal of Molecular Biology 375, nr 5 (luty 2008): 1329–43. http://dx.doi.org/10.1016/j.jmb.2007.11.037.
Pełny tekst źródłaBressan, Debra A., Heidi A. Olivares, Benjamin E. Nelms i John H. J. Petrini. "Alteration of N-Terminal Phosphoesterase Signature Motifs Inactivates Saccharomyces cerevisiae Mre11". Genetics 150, nr 2 (1.10.1998): 591–600. http://dx.doi.org/10.1093/genetics/150.2.591.
Pełny tekst źródłaAravind, L., i E. V. Koonin. "Phosphoesterase domains associated with DNA polymerases of diverse origins". Nucleic Acids Research 26, nr 16 (1.08.1998): 3746–52. http://dx.doi.org/10.1093/nar/26.16.3746.
Pełny tekst źródłaQuist, Eugene. "Ca2+-stimulated phospholipid phosphoesterase activities in rabbit erythrocyte membranes". Archives of Biochemistry and Biophysics 236, nr 1 (styczeń 1985): 140–49. http://dx.doi.org/10.1016/0003-9861(85)90613-7.
Pełny tekst źródłaBreaker, Ronald R., i Gerald F. Joyce. "A DNA enzyme with Mg2+-dependent RNA phosphoesterase activity". Chemistry & Biology 2, nr 10 (październik 1995): 655–60. http://dx.doi.org/10.1016/1074-5521(95)90028-4.
Pełny tekst źródłaFritsky, Igor O, Reina Ott i Roland Krämer. "Allosteric Regulation of Artificial Phosphoesterase Activity by Metal Ions". Angewandte Chemie 39, nr 18 (15.09.2000): 3255–58. http://dx.doi.org/10.1002/1521-3773(20000915)39:18<3255::aid-anie3255>3.0.co;2-7.
Pełny tekst źródłaMitsutomi, Shuhei, Nobuyoshi Akimitsu, Kazuhisa Sekimizu i Chikara Kaito. "Identification of 2H phosphoesterase superfamily proteins with 2′-CPDase activity". Biochimie 165 (październik 2019): 235–44. http://dx.doi.org/10.1016/j.biochi.2019.08.008.
Pełny tekst źródłaYoung, Hayley E., Matthew P. Donohue, Tatyana I. Smirnova, Alex I. Smirnov i Pei Zhou. "The UDP-diacylglucosamine Pyrophosphohydrolase LpxH in Lipid A Biosynthesis Utilizes Mn2+ Cluster for Catalysis". Journal of Biological Chemistry 288, nr 38 (29.07.2013): 26987–7001. http://dx.doi.org/10.1074/jbc.m113.497636.
Pełny tekst źródłaNair, P. A., P. Smith i S. Shuman. "Structure of bacterial LigD 3'-phosphoesterase unveils a DNA repair superfamily". Proceedings of the National Academy of Sciences 107, nr 29 (29.06.2010): 12822–27. http://dx.doi.org/10.1073/pnas.1005830107.
Pełny tekst źródłaVASILIEV, A. O., A. V. GOVOROV, G. R. KASYAN i D. Y. PUSHKAR. "BENIGN PROSTATIC HYPERPLASIA: A POSSIBILITY TO USE TYPE 5 PHOSPHOESTERASE INHIBITORS". Medical Council, nr 19 (1.01.2016): 109–13. http://dx.doi.org/10.21518/2079-701x-2016-19-109-113.
Pełny tekst źródłaDaumann, Lena J., Peter Comba, James A. Larrabee, Gerhard Schenk, Robert Stranger, German Cavigliasso i Lawrence R. Gahan. "Synthesis, Magnetic Properties, and Phosphoesterase Activity of Dinuclear Cobalt(II) Complexes". Inorganic Chemistry 52, nr 4 (luty 2013): 2029–43. http://dx.doi.org/10.1021/ic302418x.
Pełny tekst źródłaJeong, Byeong C., Hyun-Won Klm, Stephen Owen, R. Elaine Dick i Lynne E. Macaskie. "Phosphoesterase activity and phosphate release from tributyl phosphate by aCitrobacter sp." Applied Biochemistry and Biotechnology 47, nr 1 (kwiecień 1994): 21–32. http://dx.doi.org/10.1007/bf02788672.
Pełny tekst źródłaMyllykoski, Matti, i Petri Kursula. "Structural aspects of nucleotide ligand binding by a bacterial 2H phosphoesterase". PLOS ONE 12, nr 1 (31.01.2017): e0170355. http://dx.doi.org/10.1371/journal.pone.0170355.
Pełny tekst źródłaSutera, Vincent A., Eugene S. Han, Luis A. Rajman i Susan T. Lovett. "Mutational Analysis of the RecJ Exonuclease ofEscherichia coli: Identification of Phosphoesterase Motifs". Journal of Bacteriology 181, nr 19 (1.10.1999): 6098–102. http://dx.doi.org/10.1128/jb.181.19.6098-6102.1999.
Pełny tekst źródłaTymecki, Łukasz, Kamil Strzelak i Robert Koncki. "Biparametric multicommutated flow analysis system for determination of human serum phosphoesterase activity". Analytica Chimica Acta 797 (październik 2013): 57–63. http://dx.doi.org/10.1016/j.aca.2013.08.047.
Pełny tekst źródłaChambert, R. "Purification and Characterization of YfkN, a Trifunctional Nucleotide Phosphoesterase Secreted by Bacillus Subtilis". Journal of Biochemistry 134, nr 5 (1.11.2003): 655–60. http://dx.doi.org/10.1093/jb/mvg189.
Pełny tekst źródłaShin, Dong Hae, Michael Proudfoot, Hyo Jin Lim, In‐Kyu Choi, Hisao Yokota, Alexander F. Yakunin, Rosalind Kim i Sung‐Hou Kim. "Structural and enzymatic characterization of DR1281: A calcineurin‐like phosphoesterase from Deinococcus radiodurans". Proteins: Structure, Function, and Bioinformatics 70, nr 3 (2.01.2008): 1000–1009. http://dx.doi.org/10.1002/prot.21584.
Pełny tekst źródłaNatarajan, Aswin, Kaushik Dutta, Deniz B. Temel, Pravin A. Nair, Stewart Shuman i Ranajeet Ghose. "Solution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase D". Nucleic Acids Research 40, nr 5 (14.11.2011): 2076–88. http://dx.doi.org/10.1093/nar/gkr950.
Pełny tekst źródłaMa, Di, Jie Hu, Wenqi Xu, Yan Wang, Juan Wang, Liang Li, Sheng Wang, Huiping Zhou, Yuhua Li i Li Liu. "Phosphoesterase complex modulates microflora and chronic inflammation in rats with alcoholic fatty liver disease". Life Sciences 262 (grudzień 2020): 118509. http://dx.doi.org/10.1016/j.lfs.2020.118509.
Pełny tekst źródłaMazumder, R. "Detection of novel members, structure-function analysis and evolutionary classification of the 2H phosphoesterase superfamily". Nucleic Acids Research 30, nr 23 (1.12.2002): 5229–43. http://dx.doi.org/10.1093/nar/gkf645.
Pełny tekst źródłaCollins, B. M., C. F. Skinner, M. N. J. Seaman, P. R. Evans i D. J. Owen. "Vps29: a phosphoesterase fold that acts as an interaction scaffold in the assembly of retromer". Acta Crystallographica Section A Foundations of Crystallography 61, a1 (23.08.2005): c51—c52. http://dx.doi.org/10.1107/s0108767305097837.
Pełny tekst źródłaCollins, Brett M., Claire F. Skinner, Peter J. Watson, Matthew N. J. Seaman i David J. Owen. "Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly". Nature Structural & Molecular Biology 12, nr 7 (19.06.2005): 594–602. http://dx.doi.org/10.1038/nsmb954.
Pełny tekst źródłaSmith, Paul, Pravin A. Nair, Ushati Das, Hui Zhu i Stewart Shuman. "Structures and activities of archaeal members of the LigD 3′-phosphoesterase DNA repair enzyme superfamily". Nucleic Acids Research 39, nr 8 (5.01.2011): 3310–20. http://dx.doi.org/10.1093/nar/gkq1163.
Pełny tekst źródłaLi, Dan, Cong Liu, Yu-He Liang, Lan-Fen Li i Xiao-Dong Su. "Crystal structure of B. subtilis YjcG characterizing the YjcG-like group of 2H phosphoesterase superfamily". Proteins: Structure, Function, and Bioinformatics 72, nr 3 (12.05.2008): 1071–76. http://dx.doi.org/10.1002/prot.22093.
Pełny tekst źródłaGarcía-Cano, Israel, Diana Rocha-Mendoza, Erica Kosmerl i Rafael Jiménez-Flores. "Purification and characterization of a phospholipid-hydrolyzing phosphoesterase produced by Pediococcus acidilactici isolated from Gouda cheese". Journal of Dairy Science 103, nr 5 (maj 2020): 3912–23. http://dx.doi.org/10.3168/jds.2019-17965.
Pełny tekst źródłaZhang, Zhisheng, Xiaoming Yu, Larry K. Fong i Lawrence D. Margerum. "Ligand effects on the phosphoesterase activity of Co(II) Schiff base complexes built on PAMAM dendrimers". Inorganica Chimica Acta 317, nr 1-2 (maj 2001): 72–80. http://dx.doi.org/10.1016/s0020-1693(01)00424-8.
Pełny tekst źródłaBetti, Marco, Stefania Petrucco, Angelo Bolchi, Giorgio Dieci i Simone Ottonello. "A Plant 3′-Phosphoesterase Involved in the Repair of DNA Strand Breaks Generated by Oxidative Damage". Journal of Biological Chemistry 276, nr 21 (27.02.2001): 18038–45. http://dx.doi.org/10.1074/jbc.m010648200.
Pełny tekst źródłaPathak, Ritu, Lydia M. Bogomolnaya, Jinbai Guo i Michael Polymenis. "Gid8p (Dcr1p) and Dcr2p Function in a Common Pathway To Promote START Completion in Saccharomyces cerevisiae". Eukaryotic Cell 3, nr 6 (grudzień 2004): 1627–38. http://dx.doi.org/10.1128/ec.3.6.1627-1638.2004.
Pełny tekst źródłaSeto, Marian, Marc Whitlow, Margaret A. McCarrick, Subha Srinivasan, Ying Zhu, Rene Pagila, Robert Mintzer, David Light, Anthony Johns i Janet A. Meurer-Ogden. "A model of the acid sphingomyelinase phosphoesterase domain based on its remote structural homolog purple acid phosphatase". Protein Science 13, nr 12 (1.01.2009): 3172–86. http://dx.doi.org/10.1110/ps.04966204.
Pełny tekst źródłaZhu, Hui, Li Kai Wang i Stewart Shuman. "Essential Constituents of the 3′-Phosphoesterase Domain of Bacterial DNA Ligase D, a Nonhomologous End-joining Enzyme". Journal of Biological Chemistry 280, nr 40 (25.07.2005): 33707–15. http://dx.doi.org/10.1074/jbc.m506838200.
Pełny tekst źródłaKota, Swathi, C. Vijaya Kumar i Hari S. Misra. "Characterization of an ATP-regulated DNA-processing enzyme and thermotolerant phosphoesterase in the radioresistant bacterium Deinococcus radiodurans". Biochemical Journal 431, nr 1 (14.09.2010): 149–57. http://dx.doi.org/10.1042/bj20100446.
Pełny tekst źródłaZhuo, S., J. C. Clemens, R. L. Stone i J. E. Dixon. "Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis". Journal of Biological Chemistry 269, nr 42 (październik 1994): 26234–38. http://dx.doi.org/10.1016/s0021-9258(18)47184-0.
Pełny tekst źródłaDuran-Meza, Eva, i Rodrigo Diaz-Espinoza. "Catalytic Amyloids as Novel Synthetic Hydrolases". International Journal of Molecular Sciences 22, nr 17 (25.08.2021): 9166. http://dx.doi.org/10.3390/ijms22179166.
Pełny tekst źródłaBjerregaard-Andersen, Kaare, Ellen Østensen, John D. Scott, Kjetil Taskén i Jens Preben Morth. "Malonate in the nucleotide-binding site traps human AKAP18γ/δ in a novel conformational state". Acta Crystallographica Section F Structural Biology Communications 72, nr 8 (13.07.2016): 591–97. http://dx.doi.org/10.1107/s2053230x16010189.
Pełny tekst źródłaKrogh, Berit O., Bertrand Llorente, Alicia Lam i Lorraine S. Symington. "Mutations in Mre11 Phosphoesterase Motif I That ImpairSaccharomyces cerevisiaeMre11-Rad50-Xrs2 Complex Stability in Addition to Nuclease Activity". Genetics 171, nr 4 (2.09.2005): 1561–70. http://dx.doi.org/10.1534/genetics.105.049478.
Pełny tekst źródłaCai, Yongfang, Jiao Qi, Chun Li, Kehui Miao, Baixue Jiang, Xiaoshuang Yang, Wenyu Han, Yang Wang, Jing Gao i Xiangshu Dong. "Genome-Wide Analysis of Purple Acid Phosphatase Genes in Brassica rapa and Their Association with Pollen Development and Phosphorus Deprivation Stress". Horticulturae 7, nr 10 (5.10.2021): 363. http://dx.doi.org/10.3390/horticulturae7100363.
Pełny tekst źródłaYang, Qiya, Dhanasekaran Solairaj, Maurice Tibiru Apaliya, Mandour Abdelhai, Marui Zhu, Yuan Yan i Hongyin Zhang. "Protein Expression Profile and Transcriptome Characterization of Penicillium expansum Induced by Meyerozyma guilliermondii". Journal of Food Quality 2020 (11.02.2020): 1–12. http://dx.doi.org/10.1155/2020/8056767.
Pełny tekst źródłaLosev, Eugene, Effrosyni Papanikou, Olivia W. Rossanese i Benjamin S. Glick. "Cdc1p Is an Endoplasmic Reticulum-Localized Putative Lipid Phosphatase That Affects Golgi Inheritance and Actin Polarization by Activating Ca2+ Signaling". Molecular and Cellular Biology 28, nr 10 (10.03.2008): 3336–43. http://dx.doi.org/10.1128/mcb.00567-07.
Pełny tekst źródłaBurroughs, A. Max, i L. Aravind. "Innate immunity and bacterial conflict: the deep origins of cGAS-STING signaling and discovery of uncharacterized animal immunity pathways". Journal of Immunology 204, nr 1_Supplement (1.05.2020): 68.25. http://dx.doi.org/10.4049/jimmunol.204.supp.68.25.
Pełny tekst źródłaWilson, S., M. Tavassoli i F. Z. Watts. "Schizosaccharomyces pombe Rad32 protein: a phosphoprotein with an essential phosphoesterase motif required for repair of DNA double strand breaks". Nucleic Acids Research 26, nr 23 (1.12.1998): 5261–69. http://dx.doi.org/10.1093/nar/26.23.5261.
Pełny tekst źródłaDas, Ushati, Paul Smith i Stewart Shuman. "Structural insights to the metal specificity of an archaeal member of the LigD 3′-phosphoesterase DNA repair enzyme family". Nucleic Acids Research 40, nr 2 (28.09.2011): 828–36. http://dx.doi.org/10.1093/nar/gkr767.
Pełny tekst źródłaZhu, Hui, i Stewart Shuman. "Substrate Specificity and Structure-Function Analysis of the 3′-Phosphoesterase Component of the Bacterial NHEJ Protein, DNA Ligase D". Journal of Biological Chemistry 281, nr 20 (14.03.2006): 13873–81. http://dx.doi.org/10.1074/jbc.m600055200.
Pełny tekst źródłaDamen, Ester, Elmar Krieger, Jens E. Nielsen, Jelle Eygensteyn i Jeroen E. M. Van Leeuwen. "The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide". Biochemical Journal 398, nr 3 (29.08.2006): 399–409. http://dx.doi.org/10.1042/bj20060033.
Pełny tekst źródłaDutta, Kaushik, Aswin Natarajan, Pravin A. Nair, Stewart Shuman i Ranajeet Ghose. "Sequence-specific 1H, 13C and 15N assignments of the phosphoesterase (PE) domain of Pseudomonas aeruginosa DNA ligase D (LigD)". Biomolecular NMR Assignments 5, nr 2 (7.01.2011): 151–55. http://dx.doi.org/10.1007/s12104-010-9289-7.
Pełny tekst źródłaLi, Jinchao, Wenjie Liang, Yan Li i Weiqiang Qian. "APURINIC/APYRIMIDINIC ENDONUCLEASE2 and ZINC FINGER DNA 3′-PHOSPHOESTERASE Play Overlapping Roles in the Maintenance of Epigenome and Genome Stability". Plant Cell 30, nr 9 (22.08.2018): 1954–70. http://dx.doi.org/10.1105/tpc.18.00287.
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