{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T17:25:19Z","timestamp":1786987519495,"version":"build-2736575974"},"reference-count":53,"publisher":"American Association for the Advancement of Science (AAAS)","license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2021,6,4]],"date-time":"2021-06-04T00:00:00Z","timestamp":1622764800000},"content-version":"vor","delay-in-days":154,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["csbj.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Comput Struct Biotechnol J"],"published-print":{"date-parts":[[2021,1]]},"DOI":"10.1016\/j.csbj.2021.05.052","type":"journal-article","created":{"date-parts":[[2021,6,6]],"date-time":"2021-06-06T11:09:47Z","timestamp":1622977787000},"page":"3542-3555","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":11,"title":["Structural insight into the unique conformation of cystathionine \u03b2-synthase from\n                    <i>Toxoplasma gondii<\/i>"],"prefix":"10.34133","volume":"19","author":[{"given":"Carmen","family":"Fern\u00e1ndez-Rodr\u00edguez","sequence":"first","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iker","family":"Oyenarte","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolina","family":"Conter","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Gonz\u00e1lez-Recio","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reyes","family":"N\u00fa\u00f1ez-Franco","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudia","family":"Gil-Pitarch","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iban","family":"Quintana","sequence":"additional","affiliation":[{"name":"Physics of Surfaces and Materials Unit. TEKNIKER, Basque Research and Technology Alliance (BRTA), C\/I\u00f1aki Goenaga, 5, 20600 Eibar Gipuzkoa, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gonzalo","family":"Jim\u00e9nez-Os\u00e9s","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paola","family":"Dominici","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria Luz","family":"Martinez-Chantar","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alessandra","family":"Astegno","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis Alfonso","family":"Mart\u00ednez-Cruz","sequence":"additional","affiliation":[{"name":"Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park, Building 801A, 48160 Derio, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","published-online":{"date-parts":[[2021,6,18]]},"reference":[{"key":"e_1_3_4_2_2","article-title":"The one health approach to toxoplasmosis: epidemiology, control, and prevention strategies","author":"Aguirre A.A.","year":"2019","unstructured":"Aguirre A.A., Longcore T., Barbieri M., Dabritz H., Hill D., Klein P.N. et al: The one health approach to toxoplasmosis: epidemiology, control, and prevention strategies. EcoHealth 2019; .","journal-title":"EcoHealth"},{"key":"e_1_3_4_3_2","first-page":"1","article-title":"Toxoplasma gondii infection in immunocompromised patients: A systematic review and meta-analysis","volume":"8","author":"Wang Z.D.","year":"2017","unstructured":"Wang Z.D., Liu H.H., Ma Z.X., Ma H.Y., Li Z.Y., Bin Y.Z. et al: Toxoplasma gondii infection in immunocompromised patients: A systematic review and meta-analysis. Front Microbiol. 2017; 8: 1.","journal-title":"Front Microbiol."},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","DOI":"10.3389\/fpsyt.2019.01012","article-title":"Negative effects of latent toxoplasmosis on mental health","volume":"10","author":"Flegr J.","year":"2020","unstructured":"Flegr J. and Hor\u00e1\u010dek J.: Negative effects of latent toxoplasmosis on mental health. Front Psychiatry 2020; 10.","journal-title":"Front Psychiatry"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","unstructured":"Charvat RA Arrizabalaga G. Oxidative stress generated during monensin treatment contributes to altered Toxoplasma gondii mitochondrial function. Sci Rep. 2016;6(September 2015):1\u201317. Available from: http:\/\/dx.doi.org\/10.1038\/srep22997.","DOI":"10.1038\/srep22997"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1645\/GE-1608.1","article-title":"Inhibition of toxoplasma gondii and plasmodium falciparum infections in vitro by NSC3852, a redox active antiproliferative and tumor cell differentiation agent","volume":"95","author":"Strobl J.S.","year":"2009","unstructured":"Strobl J.S., Seibert C.W., Li Y., Nagarkatti R., Mitchell S.M., Rosypal A.C. et al: Inhibition of toxoplasma gondii and plasmodium falciparum infections in vitro by NSC3852, a redox active antiproliferative and tumor cell differentiation agent. J Parasitol 2009; 95: 215.","journal-title":"J Parasitol"},{"key":"e_1_3_4_7_2","article-title":"Oxidative stress control by apicomplexan parasites","author":"Bosch S.S.","year":"2015","unstructured":"Bosch S.S., Kronenberger T., Meissner K.A., Zimbres F.M., Stegehake D., Izui N.M. et al: Oxidative stress control by apicomplexan parasites. Biomed Res Int 2015; .","journal-title":"Biomed Res Int"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-020-71469-x","article-title":"Cystathionine beta synthase is involved in cysteine biosynthesis and H 2 S generation in Toxoplasma gondii","volume":"10","author":"Conter C.","year":"2020","unstructured":"Conter C., Fruncillo S., Fern\u00e1ndez-rodr\u00edguez C., Martinez-cruz L.A. and Astegno A.: Cystathionine beta synthase is involved in cysteine biosynthesis and H 2 S generation in Toxoplasma gondii. Sci Rep 2020; 10.","journal-title":"Sci Rep"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","unstructured":"Maresi E Janson G Fruncillo S Paiardini A Vallone R Dominici P et al. Functional Characterization and Structure-Guided Mutational Analysis of the Transsulfuration Enzyme Cystathionine \u03b3-Lyase from Toxoplasma gondii. Int J Mol Sci. 2018 Jul 20;19(7):2111. Available from: http:\/\/www.mdpi.com\/1422-0067\/19\/7\/2111.","DOI":"10.3390\/ijms19072111"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","unstructured":"Majtan T Pey AL Fern\u00e1ndez R Fern\u00e1ndez JA Mart\u00ednez-Cruz LA Kraus JP. Domain Organization Catalysis and Regulation of Eukaryotic Cystathionine Beta-Synthases. Uversky VN editor. PLoS One. 2014;9(8):e105290. Available from: https:\/\/dx.plos.org\/10.1371\/journal.pone.0105290.","DOI":"10.1371\/journal.pone.0105290"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","unstructured":"Devi S. Tarique K.F. Ali M.F. Abdul Rehman S.A. and Gourinath S.: Identification and characterization of Helicobacter pylori O-acetylserine-dependent cystathionine \u03b2-synthase a distinct member of the PLP-II family. Available from Mol Microbiol. 2019; 112: 718. https:\/\/onlinelibrary.wiley.com\/doi\/abs\/10.1111\/mmi.14315.","DOI":"10.1111\/mmi.14315"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","unstructured":"Devi S. Abdul Rehman S.A. Tarique K.F. and Gourinath S.: Structural characterization and functional analysis of cystathionine \u03b2-synthase: an enzyme involved in the reverse transsulfuration pathway of Bacillus anthracis. Available from FEBS J. 2017; 284: 3862. https:\/\/onlinelibrary.wiley.com\/doi\/abs\/10.1111\/febs.14273.","DOI":"10.1111\/febs.14273"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","unstructured":"Matoba Y. Yoshida T. Izuhara-Kihara H. Noda M. and Sugiyama M.: Crystallographic and mutational analyses of cystathionine \u03b2-synthase in the H 2 S-synthetic gene cluster in Lactobacillus plantarum. Available from Protein Sci. 2017; 26: 763. http:\/\/doi.wiley.com\/10.1002\/pro.3123.","DOI":"10.1002\/pro.3123"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","unstructured":"Vozdek R Hn\u00edzda A Krijt J Kostrouchov\u00e1 M Ko\u017eich V. Novel structural arrangement of nematode cystathionine \u03b2-synthases: characterization of Caenorhabditis elegans CBS-1. Biochem J. 2012;443(2):535\u201347.Available from: https:\/\/portlandpress.com\/biochemj\/article\/443\/2\/535\/46107\/Novel-structural-arrangement-of-nematode.","DOI":"10.1042\/BJ20111478"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","unstructured":"Jhee K.-H. McPhie P. and Miles E.W.: Yeast cystathionine \u03b2-synthase is a pyridoxal phosphate enzyme but unlike the human enzyme is not a heme protein. Available from J Biol Chem. 2000; 275: 11541. http:\/\/www.jbc.org\/lookup\/doi\/10.1074\/jbc.C000056200.","DOI":"10.1074\/jbc.C000056200"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","unstructured":"Bateman A.: The structure of a domain common to archaebacteria and the homocystinuria disease protein. Available from Trends Biochem Sci. 1997; 22: 12. https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0968000496300467.","DOI":"10.1016\/S0968-0004(96)30046-7"},{"key":"e_1_3_4_17_2","doi-asserted-by":"publisher","DOI":"10.1021\/cb200231c"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","unstructured":"Tu Y. Kreinbring C.A. Hill M. Liu C. Petsko G.A. McCune C.D. et al: Crystal Structures of Cystathionine \u03b2-Synthase from Saccharomyces cerevisiae : One Enzymatic Step at a Time. Available from Biochemistry 2018; 57: 3134. https:\/\/pubs.acs.org\/doi\/10.1021\/acs.biochem.8b00092.","DOI":"10.1021\/acs.biochem.8b00092"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","unstructured":"Koutmos M. Kabil O. Smith J.L. and Banerjee R.: Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine -synthase. Available from Proc Natl Acad Sci. 2010; 107: 20958. http:\/\/www.pnas.org\/cgi\/doi\/10.1073\/pnas.1011448107.","DOI":"10.1073\/pnas.1011448107"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","unstructured":"Gim\u00e9nez-Mascarell P. Majtan T. Oyenarte I. Ere\u00f1o-Orbea J. Majtan J. Klaudiny J. et al: Crystal structure of cystathionine \u03b2-synthase from honeybee Apis mellifera. Available from J Struct Biol. 2018; 202: 82. https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1047847717302319.","DOI":"10.1016\/j.jsb.2017.12.008"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","unstructured":"Taoka S Lepore BW Kabil \u00d6 Ojha S Ringe D Banerjee R. Human Cystathionine \u03b2-Synthase Is a Heme Sensor Protein. Evidence That the Redox Sensor Is Heme and Not the Vicinal Cysteines in the CXXC Motif Seen in the Crystal Structure of the Truncated Enzyme. Biochemistry. 2002 Aug;41(33):10454\u201361. Available from: https:\/\/pubs.acs.org\/doi\/10.1021\/bi026052d.","DOI":"10.1021\/bi026052d"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","unstructured":"Jano\u0161\u00edk M Oliveriusov\u00e1 J Jano\u0161\u00edkov\u00e1 B Sokolov\u00e1 J Kraus E Kraus JP et al. Impaired Heme Binding and Aggregation of Mutant Cystathionine \u03b2-Synthase Subunits in Homocystinuria. Am J Hum Genet.2001;68(6):1506-13.Available from: https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0002929707610623.","DOI":"10.1086\/320597"},{"key":"e_1_3_4_23_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja904468w"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","unstructured":"Meier M.: Structure of human cystathionine beta-synthase: a unique pyridoxal 5\u2019-phosphate-dependent heme protein. Available from EMBO J. 2001; 20: 3910. http:\/\/emboj.embopress.org\/cgi\/doi\/10.1093\/emboj\/20.15.3910.","DOI":"10.1093\/emboj\/20.15.3910"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","unstructured":"Ereno-Orbea J Majtan T Oyenarte I Kraus JP Martinez-Cruz LA. Structural basis of regulation and oligomerization of human cystathionine -synthase the central enzyme of transsulfuration. Proc Natl Acad Sci. 2013 Oct 1;110(40):E3790\u20139. Available from: http:\/\/www.pnas.org\/cgi\/doi\/10.1073\/pnas.1313683110.","DOI":"10.1073\/pnas.1313683110"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","unstructured":"McCorvie TJ Kopec J Hyung S-J Fitzpatrick F Feng X Termine D et al. Inter-domain Communication of Human Cystathionine \u03b2-Synthase. J Biol Chem. 2014 Dec 26;289(52):36018\u201330. Available from: http:\/\/www.jbc.org\/lookup\/doi\/10.1074\/jbc.M114.610782.","DOI":"10.1074\/jbc.M114.610782"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","unstructured":"Ere\u00f1o-Orbea J Majtan T Oyenarte I Kraus JP Mart\u00ednez-Cruz LA. Structural insight into the molecular mechanism of allosteric activation of human cystathionine \u03b2-synthase by S -adenosylmethionine. Proc Natl Acad Sci. 2014 Sep 16;111(37):E3845\u201352. Available from: http:\/\/www.pnas.org\/lookup\/doi\/10.1073\/pnas.1414545111.","DOI":"10.1073\/pnas.1414545111"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","unstructured":"Christen P Mehta PK. From cofactor to enzymes. The molecular evolution of pyridoxal-5?-phosphate-dependent enzymes. Chem Rec. 2001;1(6):436\u201347. Available from: http:\/\/doi.wiley.com\/10.1002\/tcr.10005.","DOI":"10.1002\/tcr.10005"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","unstructured":"Evande R. Blom H. Boers G.H.J. and Banerjee R.: Alleviation of Intrasteric Inhibition by the Pathogenic Activation Domain Mutation D444N in Human Cystathionine \u03b2-Synthase. Available from Biochemistry 2002; 41: 11832. https:\/\/pubs.acs.org\/doi\/10.1021\/bi026248d.","DOI":"10.1021\/bi026248d"},{"key":"e_1_3_4_30_2","doi-asserted-by":"publisher","DOI":"10.1107\/S2059798316018210"},{"key":"e_1_3_4_31_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1209855"},{"key":"e_1_3_4_32_2","doi-asserted-by":"publisher","DOI":"10.1002\/iub.1740"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","unstructured":"Saini V Chinta KC Reddy VP Glasgow JN Stein A Lamprecht DA et al. Hydrogen sulfide stimulates Mycobacterium tuberculosis respiration growth and pathogenesis. Nat Commun. 2020;11(1):1\u201317. Available from: http:\/\/dx.doi.org\/10.1038\/s41467-019-14132-y.","DOI":"10.1038\/s41467-019-14132-y"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","unstructured":"Astegno A. Capitani G. and Dominici P.: Functional roles of the hexamer organization of plant glutamate decarboxylase. Available from Biochim Biophys Acta - Proteins Proteomics. 2015; 1854: 1229. https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963915000126.","DOI":"10.1016\/j.bbapap.2015.01.001"},{"key":"e_1_3_4_35_2","article-title":"Characterization of C-S lyase from C. diphtheriae: A possible target for new antimicrobial drugs","volume":"701536","author":"Astegno A.","year":"2013","unstructured":"Astegno A., Giorgetti A., Allegrini A., Cellini B. and Dominici P.: Characterization of C-S lyase from C. diphtheriae: A possible target for new antimicrobial drugs. Biomed Res Int 2013; 701536.","journal-title":"Biomed Res Int"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1002\/prot.24707","article-title":"Role of active-site residues Tyr55 and Tyr114 in catalysis and substrate specificity of Corynebacterium diphtheriae C-S lyase","volume":"83","author":"Astegno A.","year":"2015","unstructured":"Astegno A., Allegrini A., Piccoli S., Giorgetti A. and Dominici P.: Role of active-site residues Tyr55 and Tyr114 in catalysis and substrate specificity of Corynebacterium diphtheriae C-S lyase. Proteins Struct Funct Bioinforma 2015; 83: 78.","journal-title":"Proteins Struct Funct Bioinforma"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","unstructured":"Oyenarte I. Majtan T. Ere\u00f1o J. Corral-Rodr\u00edguez M.A. Kraus J.P. and Mart\u00ednez-Cruz L.A.: Purification crystallization and preliminary crystallographic analysis of human cystathionine \u03b2-synthase. Available from Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012; 68: 1318. http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23143240.","DOI":"10.1107\/S1744309112037219"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"66","author":"Kabsch W.X.D.S.","year":"2010","unstructured":"Kabsch W.X.D.S.: Acta Crystallogr Sect D Biol Crystallogr 2010; 66: 125.","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"e_1_3_4_39_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444905036693"},{"key":"e_1_3_4_40_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444913000061"},{"key":"e_1_3_4_41_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444910045749"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","DOI":"10.1107\/S205327331909394X","article-title":"STARANISO : use of a WebGL-based 3D interactive graphical display to represent and visualise data quality metrics for anisotropic macromolecular diffraction data","volume":"75","author":"Tickle I.","year":"2019","unstructured":"Tickle I.: STARANISO : use of a WebGL-based 3D interactive graphical display to represent and visualise data quality metrics for anisotropic macromolecular diffraction data. Acta Crystallogr Sect A Found Adv 2019; 75: e162.","journal-title":"Acta Crystallogr Sect A Found Adv"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","unstructured":"Vonrhein C. Flensburg C. Keller P. Sharff A. Smart O. Paciorek W. et al: Data processing and analysis with the autoPROC toolbox. Available from Acta Crystallogr Sect D Biol Crystallogr. 2011; 67: 293. http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/4954368.","DOI":"10.1107\/S0907444911007773"},{"key":"e_1_3_4_44_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889807021206"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","unstructured":"Adams P.D. Afonine P.V. Bunk\u00f3czi G. Chen V.B. Echols N. Headd J.J. et al: The Phenix software for automated determination of macromolecular structures. Available from Methods 2011; 55: 94. https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046202311001319.","DOI":"10.1016\/j.ymeth.2011.07.005"},{"key":"e_1_3_4_46_2","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444912001308"},{"key":"e_1_3_4_47_2","doi-asserted-by":"crossref","unstructured":"Emsley P. Lohkamp B. Scott W.G. and Cowtan K.: Features and development of Coot. Available from Acta Crystallogr Sect D Biol Crystallogr. 2010; 66: 486. http:\/\/scripts.iucr.org\/cgi-bin\/paper?S0907444910007493.","DOI":"10.1107\/S0907444910007493"},{"key":"e_1_3_4_48_2","doi-asserted-by":"crossref","unstructured":"Bayly C.I. Cieplak P. Cornell W. and Kollman P.A.: A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. Available from J Phys Chem. 1993; 97: 10269. https:\/\/pubs.acs.org\/doi\/abs\/10.1021\/j100142a004.","DOI":"10.1021\/j100142a004"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","unstructured":"Maier J.A. Martinez C. Kasavajhala K. Wickstrom L. Hauser K.E. and Simmerling C.: ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB. Available from J Chem Theory Comput. 2015; 11: 3696. http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/26574453.","DOI":"10.1021\/acs.jctc.5b00255"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","unstructured":"Wang J. Wolf R.M. Caldwell J.W. Kollman P.A. and Case D.A.: Development and testing of a general amber force field. Available from J Comput Chem. 2004; 25: 1157. http:\/\/doi.wiley.com\/10.1002\/jcc.20035.","DOI":"10.1002\/jcc.20035"},{"key":"e_1_3_4_51_2","doi-asserted-by":"crossref","unstructured":"Jorgensen W.L. Chandrasekhar J. Madura J.D. Impey R.W. and Klein M.L.: Comparison of simple potential functions for simulating liquid water. Available from J Chem Phys. 1983; 79: 926. http:\/\/aip.scitation.org\/doi\/10.1063\/1.445869.","DOI":"10.1063\/1.445869"},{"key":"e_1_3_4_52_2","doi-asserted-by":"crossref","unstructured":"Miyamoto S. and Kollman P.A.: Settle: An analytical version of the SHAKE and RATTLE algorithm for rigid water models. Available from J Comput Chem. 1992; 13: 952. http:\/\/doi.wiley.com\/10.1002\/jcc.540130805.","DOI":"10.1002\/jcc.540130805"},{"key":"e_1_3_4_53_2","doi-asserted-by":"crossref","unstructured":"Darden T. York D. and Pedersen L.: Particle mesh Ewald: An N \u22c5log(N) method for Ewald sums in large systems. Available from J Chem Phys. 1993; 98: 10089. http:\/\/aip.scitation.org\/doi\/10.1063\/1.464397.","DOI":"10.1063\/1.464397"},{"key":"e_1_3_4_54_2","doi-asserted-by":"publisher","DOI":"10.1093\/bioinformatics\/btl461"}],"container-title":["Computational and Structural Biotechnology Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2001037021002403?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2001037021002403?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/spj.science.org\/doi\/pdf\/10.1016\/j.csbj.2021.05.052","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,5,17]],"date-time":"2026-05-17T12:47:26Z","timestamp":1779022046000},"score":1,"resource":{"primary":{"URL":"https:\/\/spj.science.org\/doi\/10.1016\/j.csbj.2021.05.052"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1]]},"references-count":53,"alternative-id":["10.1016\/j.csbj.2021.05.052"],"URL":"https:\/\/doi.org\/10.1016\/j.csbj.2021.05.052","relation":{},"ISSN":["2001-0370"],"issn-type":[{"value":"2001-0370","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural insight into the unique conformation of cystathionine \u03b2-synthase from Toxoplasma gondii","name":"articletitle","label":"Article Title"},{"value":"Computational and Structural Biotechnology Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.csbj.2021.05.052","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 The Authors. Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology.","name":"copyright","label":"Copyright"}]}}