FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2010897185> ?p ?o ?g. }

• W2010897185 endingPage "1362" @default.
• W2010897185 startingPage "1358" @default.
• W2010897185 abstract "Proteins: Structure, Function, and BioinformaticsVolume 79, Issue 4 p. 1358-1362 Structure Notes Crystal structure of the pyrimidine 5′-nucleotidase SDT1 from Saccharomyces cerevisiae complexed with uridine 5′-monophosphate provides further insight into ligand binding Nuo Shi, Nuo Shi Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorYu-Jie Zhang, Yu-Jie Zhang Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorHong-Kai Chen, Hong-Kai Chen Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorYongxiang Gao, Yongxiang Gao Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorMaikun Teng, Corresponding Author Maikun Teng [email protected] Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Liwen Niu, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China===Search for more papers by this authorLiwen Niu, Corresponding Author Liwen Niu [email protected] Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Liwen Niu, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China===Search for more papers by this author Nuo Shi, Nuo Shi Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorYu-Jie Zhang, Yu-Jie Zhang Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorHong-Kai Chen, Hong-Kai Chen Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorYongxiang Gao, Yongxiang Gao Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaSearch for more papers by this authorMaikun Teng, Corresponding Author Maikun Teng [email protected] Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Liwen Niu, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China===Search for more papers by this authorLiwen Niu, Corresponding Author Liwen Niu [email protected] Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui 230026, ChinaHefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China. Liwen Niu, Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China===Search for more papers by this author First published: 13 December 2010 https://doi.org/10.1002/prot.22969Citations: 3Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat REFERENCES 1 Bianchi V,Pontis E,Reichard P. Interrelations between substrate cycles and de novo synthesis of pyrimidine deoxyribonucleoside triphosphates in 3T6 cells. Proc Natl Acad Sci U S A 1986; 83: 986–990. 2 Hunsucker SA,Mitchell BS,Spychala J. The 5′-nucleotidases as regulators of nucleotide and drug metabolism. Pharmacol Ther 2005; 107: 1–30. 3 Burroughs AM,Allen KN,Dunaway-Mariano D,Aravind L. Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes. J Mol Biol 2006; 361: 1003–1034. 4 Morais MC,Zhang G,Zhang W,Olsen DB,Dunaway-Mariano D,Allen KN. X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis. J Biol Chem 2004; 279: 9353–9361. 5 Wang W,Cho HS,Kim R,Jancarik J,Yokota H,Nguyen HH,Grigoriev IV,Wemmer DE,Kim SH. Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic “snapshots” of intermediate states. J Mol Biol 2002; 319: 421–431. 6 Uptain SM,Kane CM,Chamberlin MJ. Basic mechanisms of transcript elongation and its regulation. Annu Rev Biochem 1997; 66: 117–172. 7 Nakanishi T,Nakano A,Nomura K,Sekimizu K,Natori S. Purification, gene cloning, and gene disruption of the transcription elongation factor S-II in Saccharomyces cerevisiae. J Biol Chem 1992; 267: 13200–13204. 8 Nakanishi T,Sekimizu K. SDT1/SSM1, a multicopy suppressor of S-II null mutant, encodes a novel pyrimidine 5′-nucleotidase. J Biol Chem 2002; 277: 22103–22106. 9 Zimmermann H. 5′-Nucleotidase: molecular structure and functional aspects. Biochem J 1992; 285(Pt 2): 345–365. 10 Leslie AGW. Recent changes to the MOSFLM package for processing film and image plate data. Joint CCP4 1 ESF-EAMCB Newsletter on Protein Crystallography 1992; 26. 11 Evans PR. in Data Reduction Proceedings of CCP4 Study Weekend. on Data Collection and Processing, Warrington: Daresbury Laboratory; 1993. pp 114–122. 12 Otwinowski Z,Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr 1997; 276: 307–326. 13 Terwilliger TC,Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr Sect D 1999; 55(Pt 4): 849–861. 14 Terwilliger TC. Maximum-likelihood density modification. Acta Crystallogr Sect D 2000; 56(Pt 8): 965–972. 15 Murshudov GN,Vagin AA,Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr Sect D 1997; 53(Pt 3): 240–255. 16 The CCP4 suite: programs for protein crystallography. Acta Crystallogr Sect D 1994; 50(Pt 5): 760–763. 17 Emsley P,Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr Sect D 2004; 60(Pt 12Pt 1): 2126–2132. 18 Adams PD,Grosse-Kunstleve RW,Hung LW,Ioerger TR,McCoy AJ,Moriarty NW,Read RJ,Sacchettini JC,Sauter NK,Terwilliger TC. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr Sect D 2002; 58(Pt 11): 1948–1954. 19 Vagin A,Teplyakov A. MOLREP: an Automated Program for Molecular Replacement. J Appl Crystallogr 1997; 30: 1022–1025. 20 Davis IW,Leaver-Fay A,Chen VB,Block JN,Kapral GJ,Wang X,Murray LW,Arendall WB,III,Snoeyink J,Richardson JS,Richardson DC. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 2007; 35: W375–383. 21 Laskowski RA,Macarthur MW,Moss DS,Thornton JM. Procheck—a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993; 26: 283–291. 22 Wang W,Kim R,Jancarik J,Yokota H,Kim SH. Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 A resolution. Structure 2001; 9: 65–71. 23 Bitto E,Bingman CA,Wesenberg GE,McCoy JG,Phillips GN,Jr. Structure of pyrimidine 5′-nucleotidase type 1. Insight into mechanism of action and inhibition during lead poisoning. J Biol Chem 2006; 281: 20521–20529. 24 Wallden K,Ruzzenente B,Rinaldo-Matthis A,Bianchi V,Nordlund P. Structural basis for substrate specificity of the human mitochondrial deoxyribonucleotidase. Structure 2005; 13: 1081–1088. Citing Literature Volume79, Issue4April 2011Pages 1358-1362 ReferencesRelatedInformation" @default.
• W2010897185 created "2016-06-24" @default.
• W2010897185 creator A5000105157 @default.
• W2010897185 creator A5000420493 @default.
• W2010897185 creator A5001228727 @default.
• W2010897185 creator A5031910729 @default.
• W2010897185 creator A5044083934 @default.
• W2010897185 creator A5058555426 @default.
• W2010897185 date "2011-01-25" @default.
• W2010897185 modified "2023-10-16" @default.
• W2010897185 title "Crystal structure of the pyrimidine 5′-nucleotidase SDT1 from Saccharomyces cerevisiae complexed with uridine 5′-monophosphate provides further insight into ligand binding" @default.
• W2010897185 cites W1539796472 @default.
• W2010897185 cites W1577770943 @default.
• W2010897185 cites W1792542720 @default.
• W2010897185 cites W1965277349 @default.
• W2010897185 cites W1982959450 @default.
• W2010897185 cites W1986191025 @default.
• W2010897185 cites W1993000713 @default.
• W2010897185 cites W2038840577 @default.
• W2010897185 cites W2041729391 @default.
• W2010897185 cites W2057121401 @default.
• W2010897185 cites W2060955755 @default.
• W2010897185 cites W2097493124 @default.
• W2010897185 cites W2109184569 @default.
• W2010897185 cites W2122339645 @default.
• W2010897185 cites W2127149222 @default.
• W2010897185 cites W2143694829 @default.
• W2010897185 cites W2144081223 @default.
• W2010897185 cites W2149132502 @default.
• W2010897185 cites W2154802584 @default.
• W2010897185 cites W2165289894 @default.
• W2010897185 cites W2172049330 @default.
• W2010897185 doi "https://doi.org/10.1002/prot.22969" @default.
• W2010897185 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21268116" @default.
• W2010897185 hasPublicationYear "2011" @default.
• W2010897185 type Work @default.
• W2010897185 sameAs 2010897185 @default.
• W2010897185 citedByCount "4" @default.
• W2010897185 countsByYear W20108971852012 @default.
• W2010897185 countsByYear W20108971852013 @default.
• W2010897185 countsByYear W20108971852015 @default.
• W2010897185 countsByYear W20108971852018 @default.
• W2010897185 crossrefType "journal-article" @default.
• W2010897185 hasAuthorship W2010897185A5000105157 @default.
• W2010897185 hasAuthorship W2010897185A5000420493 @default.
• W2010897185 hasAuthorship W2010897185A5001228727 @default.
• W2010897185 hasAuthorship W2010897185A5031910729 @default.
• W2010897185 hasAuthorship W2010897185A5044083934 @default.
• W2010897185 hasAuthorship W2010897185A5058555426 @default.
• W2010897185 hasBestOaLocation W20108971851 @default.
• W2010897185 hasConcept C104317684 @default.
• W2010897185 hasConcept C116569031 @default.
• W2010897185 hasConcept C170493617 @default.
• W2010897185 hasConcept C181199279 @default.
• W2010897185 hasConcept C185592680 @default.
• W2010897185 hasConcept C18880352 @default.
• W2010897185 hasConcept C2777576037 @default.
• W2010897185 hasConcept C2779222958 @default.
• W2010897185 hasConcept C2779321679 @default.
• W2010897185 hasConcept C2781259782 @default.
• W2010897185 hasConcept C55493867 @default.
• W2010897185 hasConcept C67705224 @default.
• W2010897185 hasConcept C71240020 @default.
• W2010897185 hasConcept C8010536 @default.
• W2010897185 hasConceptScore W2010897185C104317684 @default.
• W2010897185 hasConceptScore W2010897185C116569031 @default.
• W2010897185 hasConceptScore W2010897185C170493617 @default.
• W2010897185 hasConceptScore W2010897185C181199279 @default.
• W2010897185 hasConceptScore W2010897185C185592680 @default.
• W2010897185 hasConceptScore W2010897185C18880352 @default.
• W2010897185 hasConceptScore W2010897185C2777576037 @default.
• W2010897185 hasConceptScore W2010897185C2779222958 @default.
• W2010897185 hasConceptScore W2010897185C2779321679 @default.
• W2010897185 hasConceptScore W2010897185C2781259782 @default.
• W2010897185 hasConceptScore W2010897185C55493867 @default.
• W2010897185 hasConceptScore W2010897185C67705224 @default.
• W2010897185 hasConceptScore W2010897185C71240020 @default.
• W2010897185 hasConceptScore W2010897185C8010536 @default.
• W2010897185 hasIssue "4" @default.
• W2010897185 hasLocation W20108971851 @default.
• W2010897185 hasLocation W20108971852 @default.
• W2010897185 hasOpenAccess W2010897185 @default.
• W2010897185 hasPrimaryLocation W20108971851 @default.
• W2010897185 hasRelatedWork W1803328452 @default.
• W2010897185 hasRelatedWork W1973338661 @default.
• W2010897185 hasRelatedWork W1976250883 @default.
• W2010897185 hasRelatedWork W1981001845 @default.
• W2010897185 hasRelatedWork W2035323472 @default.
• W2010897185 hasRelatedWork W2071221403 @default.
• W2010897185 hasRelatedWork W2078787622 @default.
• W2010897185 hasRelatedWork W2105657546 @default.
• W2010897185 hasRelatedWork W2442861330 @default.
• W2010897185 hasRelatedWork W4243925219 @default.
• W2010897185 hasVolume "79" @default.
• W2010897185 isParatext "false" @default.
• W2010897185 isRetracted "false" @default.
• W2010897185 magId "2010897185" @default.
• W2010897185 workType "article" @default.