{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,25]],"date-time":"2026-10-25T02:38:01Z","timestamp":1792895881398,"version":"4.5.0"},"reference-count":39,"publisher":"National Academy of Sciences","issue":"37","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2014,9,16]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Cystathionine \u03b2-synthase (CBS), the pivotal enzyme of the transsulfuration pathway, regulates flux through the pathway to yield compounds, such as cysteine, glutathione, taurine, and H\n                    <jats:sub>2<\/jats:sub>\n                    S, that control cellular redox status and signaling. Our crystal structure of an engineered human CBS construct bound to\n                    <jats:italic>S<\/jats:italic>\n                    -adenosylmethionine (AdoMet) reveals the unique binding site of the allosteric activator and the architecture of the human CBS enzyme in its activated conformation. Together with the basal conformation that we reported earlier, these structures unravel the molecular mechanism of human CBS activation by AdoMet. Current knowledge will allow for modeling of numerous pathogenic mutations causing inherited homocystinuria and for design of compounds modulating CBS activity.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1414545111","type":"journal-article","created":{"date-parts":[[2014,9,2]],"date-time":"2014-09-02T23:56:19Z","timestamp":1409702179000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":99,"title":["Structural insight into the molecular mechanism of allosteric activation of human cystathionine \u03b2-synthase by\n                    <i>S<\/i>\n                    -adenosylmethionine"],"prefix":"10.1073","volume":"111","author":[{"given":"June","family":"Ere\u00f1o-Orbea","sequence":"first","affiliation":[{"name":"Structural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Technology Park of Bizkaia, 48160 Derio, Spain; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomas","family":"Majtan","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, University of Colorado School of Medicine, Aurora, CO 80045"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Iker","family":"Oyenarte","sequence":"additional","affiliation":[{"name":"Structural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Technology Park of Bizkaia, 48160 Derio, Spain; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan P.","family":"Kraus","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, University of Colorado School of Medicine, Aurora, CO 80045"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis Alfonso","family":"Mart\u00ednez-Cruz","sequence":"additional","affiliation":[{"name":"Structural Biology Unit, Center for Cooperative Research in Biosciences (CIC bioGUNE), Technology Park of Bizkaia, 48160 Derio, Spain; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2014,9,2]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"29871","DOI":"10.1074\/jbc.R400005200","article-title":"Cystathionine beta-synthase: Structure, function, regulation, and location of homocystinuria-causing mutations","volume":"279","author":"Miles EW","year":"2004","unstructured":"EW Miles, JP Kraus, Cystathionine beta-synthase: Structure, function, regulation, and location of homocystinuria-causing mutations. J Biol Chem 279, 29871\u201329874 (2004).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_2_2","first-page":"2007","volume-title":"The Metabolic and Molecular Bases of Inherited Disease","author":"Mudd SH","year":"2001","unstructured":"SH Mudd, HL Levy, JP Kraus, Disorders of transsulfuration. The Metabolic and Molecular Bases of Inherited Disease, eds CR Scriver, et al. (McGraw-Hill, 8th Ed, New York), pp. 2007\u20132056 (2001).","edition":"8"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/S1570-9639(03)00044-X","article-title":"Reaction mechanism and regulation of cystathionine beta-synthase","volume":"1647","author":"Banerjee R","year":"2003","unstructured":"R Banerjee, R Evande, O Kabil, S Ojha, S Taoka, Reaction mechanism and regulation of cystathionine beta-synthase. Biochim Biophys Acta 1647, 30\u201335 (2003).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"34588","DOI":"10.1074\/jbc.M805928200","article-title":"Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone","volume":"283","author":"Majtan T","year":"2008","unstructured":"T Majtan, LR Singh, L Wang, WD Kruger, JP Kraus, Active cystathionine beta-synthase can be expressed in heme-free systems in the presence of metal-substituted porphyrins or a chemical chaperone. J Biol Chem 283, 34588\u201334595 (2008).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1002\/tcr.10005","article-title":"From cofactor to enzymes: The molecular evolution of pyridoxal-5\u2032-phosphate-dependent enzymes","volume":"1","author":"Christen P","year":"2001","unstructured":"P Christen, PK Mehta, From cofactor to enzymes: The molecular evolution of pyridoxal-5\u2032-phosphate-dependent enzymes. Chem Rec 1, 436\u2013447 (2001).","journal-title":"Chem Rec"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"3910","DOI":"10.1093\/emboj\/20.15.3910","article-title":"Structure of human cystathionine beta-synthase: A unique pyridoxal 5\u2032-phosphate-dependent heme protein","volume":"20","author":"Meier M","year":"2001","unstructured":"M Meier, M Janosik, V Kery, JP Kraus, P Burkhard, Structure of human cystathionine beta-synthase: A unique pyridoxal 5\u2032-phosphate-dependent heme protein. EMBO J 20, 3910\u20133916 (2001).","journal-title":"EMBO J"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/S0968-0004(96)30046-7","article-title":"The structure of a domain common to archaebacteria and the homocystinuria disease protein","volume":"22","author":"Bateman A","year":"1997","unstructured":"A Bateman, The structure of a domain common to archaebacteria and the homocystinuria disease protein. Trends Biochem Sci 22, 12\u201313 (1997).","journal-title":"Trends Biochem Sci"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1172\/JCI200420846","article-title":"Bateman domains and adenosine derivatives form a binding contract","volume":"113","author":"Kemp BE","year":"2004","unstructured":"BE Kemp, Bateman domains and adenosine derivatives form a binding contract. J Clin Invest 113, 182\u2013184 (2004).","journal-title":"J Clin Invest"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"C1369","DOI":"10.1152\/ajpcell.00282.2005","article-title":"CBS domains: Structure, function, and pathology in human proteins","volume":"289","author":"Ignoul S","year":"2005","unstructured":"S Ignoul, J Eggermont, CBS domains: Structure, function, and pathology in human proteins. Am J Physiol Cell Physiol 289, C1369\u2013C1378 (2005).","journal-title":"Am J Physiol Cell Physiol"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1038\/ng0598-91","article-title":"Correction of disease-causing CBS mutations in yeast","volume":"19","author":"Shan X","year":"1998","unstructured":"X Shan, WD Kruger, Correction of disease-causing CBS mutations in yeast. Nat Genet 19, 91\u201393 (1998).","journal-title":"Nat Genet"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.pep.2012.01.019","article-title":"Folding and activity of mutant cystathionine \u03b2-synthase depends on the position and nature of the purification tag: Characterization of the R266K CBS mutant","volume":"82","author":"Majtan T","year":"2012","unstructured":"T Majtan, JP Kraus, Folding and activity of mutant cystathionine \u03b2-synthase depends on the position and nature of the purification tag: Characterization of the R266K CBS mutant. Protein Expr Purif 82, 317\u2013324 (2012).","journal-title":"Protein Expr Purif"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1021\/cb200231c","article-title":"The CBS domain: A protein module with an emerging prominent role in regulation","volume":"6","author":"Baykov AA","year":"2011","unstructured":"AA Baykov, HK Tuominen, R Lahti, The CBS domain: A protein module with an emerging prominent role in regulation. ACS Chem Biol 6, 1156\u20131163 (2011).","journal-title":"ACS Chem Biol"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.abb.2013.10.008","article-title":"CBS domains: Ligand binding sites and conformational variability","volume":"540","author":"Ere\u00f1o-Orbea J","year":"2013","unstructured":"J Ere\u00f1o-Orbea, I Oyenarte, LA Mart\u00ednez-Cruz, CBS domains: Ligand binding sites and conformational variability. Arch Biochem Biophys 540, 70\u201381 (2013).","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/abbi.1998.0723","article-title":"Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: Structural and functional consequences","volume":"355","author":"Kery V","year":"1998","unstructured":"V Kery, L Poneleit, JP Kraus, Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: Structural and functional consequences. Arch Biochem Biophys 355, 222\u2013232 (1998).","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"10548","DOI":"10.1021\/bi001020g","article-title":"Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation","volume":"39","author":"Jhee KH","year":"2000","unstructured":"KH Jhee, P McPhie, EW Miles, Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation. Biochemistry 39, 10548\u201310556 (2000).","journal-title":"Biochemistry"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"10625","DOI":"10.1021\/bi010711p","article-title":"Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: Evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region","volume":"40","author":"Janos\u00edk M","year":"2001","unstructured":"M Janos\u00edk, V Kery, M Gaustadnes, KN Maclean, JP Kraus, Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: Evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Biochemistry 40, 10625\u201310633 (2001).","journal-title":"Biochemistry"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1002\/humu.10089","article-title":"High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations","volume":"19","author":"Maclean KN","year":"2002","unstructured":"KN Maclean, et al., High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations. Hum Mutat 19, 641\u2013655 (2002).","journal-title":"Hum Mutat"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"E3790","DOI":"10.1073\/pnas.1313683110","article-title":"Structural basis of regulation and oligomerization of human cystathionine \u03b2-synthase, the central enzyme of transsulfuration","volume":"110","author":"Ere\u00f1o-Orbea J","year":"2013","unstructured":"J Ere\u00f1o-Orbea, T Majtan, I Oyenarte, JP Kraus, LA Mart\u00ednez-Cruz, Structural basis of regulation and oligomerization of human cystathionine \u03b2-synthase, the central enzyme of transsulfuration. Proc Natl Acad Sci USA 110, E3790\u2013E3799 (2013).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1093\/hmg\/10.6.635","article-title":"Mutations in the regulatory domain of cystathionine beta synthase can functionally suppress patient-derived mutations in cis","volume":"10","author":"Shan X","year":"2001","unstructured":"X Shan, RL Dunbrack, SA Christopher, WD Kruger, Mutations in the regulatory domain of cystathionine beta synthase can functionally suppress patient-derived mutations in cis. Hum Mol Genet 10, 635\u2013643 (2001).","journal-title":"Hum Mol Genet"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"4110","DOI":"10.1021\/bi602617f","article-title":"A pathogenic linked mutation in the catalytic core of human cystathionine beta-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer","volume":"46","author":"Sen S","year":"2007","unstructured":"S Sen, R Banerjee, A pathogenic linked mutation in the catalytic core of human cystathionine beta-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer. Biochemistry 46, 4110\u20134116 (2007).","journal-title":"Biochemistry"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"10526","DOI":"10.1021\/bi101384m","article-title":"Cross-talk between the catalytic core and the regulatory domain in cystathionine \u03b2-synthase: study by differential covalent labeling and computational modeling","volume":"49","author":"Hn\u00edzda A","year":"2010","unstructured":"A Hn\u00edzda, et al., Cross-talk between the catalytic core and the regulatory domain in cystathionine \u03b2-synthase: study by differential covalent labeling and computational modeling. Biochemistry 49, 10526\u201310534 (2010).","journal-title":"Biochemistry"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"20958","DOI":"10.1073\/pnas.1011448107","article-title":"Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine beta-synthase","volume":"107","author":"Koutmos M","year":"2010","unstructured":"M Koutmos, O Kabil, JL Smith, R Banerjee, Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine beta-synthase. Proc Natl Acad Sci USA 107, 20958\u201320963 (2010).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1021\/bi300615c","article-title":"Comparative study of enzyme activity and heme reactivity in Drosophila melanogaster and Homo sapiens cystathionine \u03b2-synthases","volume":"52","author":"Su Y","year":"2013","unstructured":"Y Su, et al., Comparative study of enzyme activity and heme reactivity in Drosophila melanogaster and Homo sapiens cystathionine \u03b2-synthases. Biochemistry 52, 741\u2013751 (2013).","journal-title":"Biochemistry"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"e105290","DOI":"10.1371\/journal.pone.0105290","article-title":"Domain organization, catalysis and regulation of eukaryotic cystathionine beta-synthases","volume":"9","author":"Majtan T","year":"2014","unstructured":"T Majtan, et al., Domain organization, catalysis and regulation of eukaryotic cystathionine beta-synthases. PLoS ONE 9, e105290 (2014).","journal-title":"PLoS ONE"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"11832","DOI":"10.1021\/bi026248d","article-title":"Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase","volume":"41","author":"Evande R","year":"2002","unstructured":"R Evande, H Blom, GH Boers, R Banerjee, Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase. Biochemistry 41, 11832\u201311837 (2002).","journal-title":"Biochemistry"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"4755","DOI":"10.1021\/bi300435e","article-title":"Conformational properties of nine purified cystathionine \u03b2-synthase mutants","volume":"51","author":"Hn\u00edzda A","year":"2012","unstructured":"A Hn\u00edzda, et al., Conformational properties of nine purified cystathionine \u03b2-synthase mutants. Biochemistry 51, 4755\u20134763 (2012).","journal-title":"Biochemistry"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1042\/BJ20120731","article-title":"Human cystathionine \u03b2-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): Complex regulation of CBS activity and stability by SAM","volume":"449","author":"Pey AL","year":"2013","unstructured":"AL Pey, T Majtan, JM Sanchez-Ruiz, JP Kraus, Human cystathionine \u03b2-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): Complex regulation of CBS activity and stability by SAM. Biochem J 449, 109\u2013121 (2013).","journal-title":"Biochem J"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"10454","DOI":"10.1021\/bi026052d","article-title":"Human cystathionine beta-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","volume":"41","author":"Taoka S","year":"2002","unstructured":"S Taoka, et al., Human cystathionine beta-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 41, 10454\u201310461 (2002).","journal-title":"Biochemistry"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.abb.2004.08.037","article-title":"Redox regulation and reaction mechanism of human cystathionine-beta-synthase: A PLP-dependent hemesensor protein","volume":"433","author":"Banerjee R","year":"2005","unstructured":"R Banerjee, CG Zou, Redox regulation and reaction mechanism of human cystathionine-beta-synthase: A PLP-dependent hemesensor protein. Arch Biochem Biophys 433, 144\u2013156 (2005).","journal-title":"Arch Biochem Biophys"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1016\/S0021-9258(17)43702-1","article-title":"Biosynthesis and proteolytic activation of cystathionine beta-synthase in rat liver","volume":"259","author":"Skovby F","year":"1984","unstructured":"F Skovby, JP Kraus, LE Rosenberg, Biosynthesis and proteolytic activation of cystathionine beta-synthase in rat liver. J Biol Chem 259, 588\u2013593 (1984).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1107\/S1744309112037219","article-title":"Purification, crystallization and preliminary crystallographic analysis of human cystathionine \u03b2-synthase","volume":"68","author":"Oyenarte I","year":"2012","unstructured":"I Oyenarte, et al., Purification, crystallization and preliminary crystallographic analysis of human cystathionine \u03b2-synthase. Acta Crystallogr Sect F Struct Biol Cryst Commun 68, 1318\u20131322 (2012).","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1172\/JCI118791","article-title":"Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient","volume":"98","author":"Kluijtmans LA","year":"1996","unstructured":"LA Kluijtmans, et al., Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient. J Clin Invest 98, 285\u2013289 (1996).","journal-title":"J Clin Invest"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"15866","DOI":"10.1074\/jbc.M110.107722","article-title":"Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: Purification and characterization of eight CBS mutant enzymes","volume":"285","author":"Majtan T","year":"2010","unstructured":"T Majtan, L Liu, JF Carpenter, JP Kraus, Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: Purification and characterization of eight CBS mutant enzymes. J Biol Chem 285, 15866\u201315873 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/0076-6879(87)43068-1","article-title":"Cystathionine beta-synthase (human)","volume":"143","author":"Kraus JP","year":"1987","unstructured":"JP Kraus, Cystathionine beta-synthase (human). Methods Enzymol 143, 388\u2013394 (1987).","journal-title":"Methods Enzymol"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski Z","year":"1997","unstructured":"Z Otwinowski, W Minor, Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307\u2013326 (1997).","journal-title":"Methods Enzymol"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch W","year":"2010","unstructured":"W Kabsch, Xds. Acta Crystallogr D Biol Crystallogr 66, 125\u2013132 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ymeth.2011.07.005","article-title":"The Phenix software for automated determination of macromolecular structures","volume":"55","author":"Adams PD","year":"2011","unstructured":"PD Adams, et al., The Phenix software for automated determination of macromolecular structures. Methods 55, 94\u2013106 (2011).","journal-title":"Methods"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov GN","year":"2011","unstructured":"GN Murshudov, et al., REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355\u2013367 (2011).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley P","year":"2010","unstructured":"P Emsley, B Lohkamp, WG Scott, K Cowtan, Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1414545111","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T07:46:23Z","timestamp":1654587983000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1414545111"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,9,2]]},"references-count":39,"journal-issue":{"issue":"37","published-print":{"date-parts":[[2014,9,16]]}},"alternative-id":["10.1073\/pnas.1414545111"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1414545111","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,9,2]]},"assertion":[{"value":"2014-09-02","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}