{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T06:18:41Z","timestamp":1790057921486,"version":"4.0.1"},"reference-count":38,"publisher":"National Academy of Sciences","issue":"42","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,10,19]]},"abstract":"<jats:p>\n                    Trichloroethylene (TCE) is one of the most widespread environmental contaminants, which is metabolized to\n                    <jats:italic>N<\/jats:italic>\n                    -acetyl-\n                    <jats:italic>S<\/jats:italic>\n                    -1,2-dichlorovinyl-\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine (NA-DCVC) before being excreted in the urine. Alternatively, NA-DCVC can be deacetylated by aminoacylase 3 (AA3), an enzyme that is highly expressed in the kidney, liver, and brain. NA-DCVC deacetylation initiates the transformation into toxic products that ultimately causes acute renal failure. AA3 inhibition is therefore a target of interest to prevent TCE induced nephrotoxicity. Here we report the crystal structure of recombinant mouse AA3 (mAA3) in the presence of its acetate byproduct and two substrates:\n                    <jats:italic>N<\/jats:italic>\n                    <jats:sup>\n                      <jats:italic>\u03b1<\/jats:italic>\n                    <\/jats:sup>\n                    -acetyl-\n                    <jats:sc>l<\/jats:sc>\n                    -tyrosine and NA-DCVC. These structures, in conjunction with biochemical data, indicated that AA3 mediates substrate specificity through van der Waals interactions providing a dynamic interaction interface, which facilitates a diverse range of substrates.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1006687107","type":"journal-article","created":{"date-parts":[[2010,10,4]],"date-time":"2010-10-04T22:41:48Z","timestamp":1286232108000},"page":"17962-17967","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":12,"title":["Structures of aminoacylase 3 in complex with acetylated substrates"],"prefix":"10.1073","volume":"107","author":[{"given":"Jennifer M.","family":"Hsieh","sequence":"first","affiliation":[{"name":"Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095;"},{"name":"Departments of Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kirill","family":"Tsirulnikov","sequence":"additional","affiliation":[{"name":"Medicine\/Nephrology, David Geffen School of Medicine at University of California, Los Angeles, CA 90095; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R.","family":"Sawaya","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute, University of California\u2013Department of Energy Institute for Genomics and Proteomics, Los Angeles, CA 90095"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathaniel","family":"Magilnick","sequence":"additional","affiliation":[{"name":"Medicine\/Nephrology, David Geffen School of Medicine at University of California, Los Angeles, CA 90095; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Abuladze","sequence":"additional","affiliation":[{"name":"Medicine\/Nephrology, David Geffen School of Medicine at University of California, Los Angeles, CA 90095; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ira","family":"Kurtz","sequence":"additional","affiliation":[{"name":"Medicine\/Nephrology, David Geffen School of Medicine at University of California, Los Angeles, CA 90095; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeff","family":"Abramson","sequence":"additional","affiliation":[{"name":"Departments of Physiology and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Pushkin","sequence":"additional","affiliation":[{"name":"Medicine\/Nephrology, David Geffen School of Medicine at University of California, Los Angeles, CA 90095; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2010,10,4]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/S1054-3589(08)61042-X","article-title":"Aminoacylases","volume":"27","author":"Anders M","year":"1994","unstructured":"M Anders, W Dekant, Aminoacylases. Adv Pharmacol 27, 431\u2013448 (1994).","journal-title":"Adv Pharmacol"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"C848","DOI":"10.1152\/ajpcell.00192.2003","article-title":"Structural characterization, tissue distribution, and functional expression of murine aminoacylase III","volume":"286","author":"Pushkin A","year":"2004","unstructured":"A Pushkin, et al., Structural characterization, tissue distribution, and functional expression of murine aminoacylase III. Am J Physiol-Cell Ph 286, C848\u2013C856 (2004).","journal-title":"Am J Physiol-Cell Ph"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1021\/tx980018b","article-title":"Acylase I-catalyzed deacetylation of N-acetyl-l-cysteine and S-alkyl-N-acetyl-l-cysteines","volume":"11","author":"Uttamsingh V","year":"1998","unstructured":"V Uttamsingh, DA Keller, MW Anders, Acylase I-catalyzed deacetylation of N-acetyl-l-cysteine and S-alkyl-N-acetyl-l-cysteines. Chem Res Toxicol 11, 800\u2013809 (1998).","journal-title":"Chem Res Toxicol"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1021\/tx990090p","article-title":"Acylase-catalyzed deacetylation of haloalkene-derived mercapturates","volume":"12","author":"Uttamsingh V","year":"1999","unstructured":"V Uttamsingh, MW Anders, Acylase-catalyzed deacetylation of haloalkene-derived mercapturates. Chem Res Toxicolol 12, 937\u2013942 (1999).","journal-title":"Chem Res Toxicolol"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"5878","DOI":"10.1021\/bi052608w","article-title":"Characterization of human aspartoacylase: The brain enzyme responsible for Canavan disease","volume":"45","author":"Le Coq J","year":"2006","unstructured":"J Le Coq, HJ An, C Lebrilla, RE Viola, Characterization of human aspartoacylase: The brain enzyme responsible for Canavan disease. Biochemistry 45, 5878\u20135884 (2006).","journal-title":"Biochemistry"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1124\/dmd.106.012062","article-title":"Specificity of aminoacylase III mediated deacetylation of mercapturic acids","volume":"35","author":"Newman D","year":"2007","unstructured":"D Newman, et al., Specificity of aminoacylase III mediated deacetylation of mercapturic acids. Drug Metab Dispos 35, 43\u201350 (2007).","journal-title":"Drug Metab Dispos"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"44496","DOI":"10.1074\/jbc.M304233200","article-title":"Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1\/M20 family","volume":"278","author":"Lindner HA","year":"2003","unstructured":"HA Lindner, et al., Essential roles of zinc ligation and enzyme dimerization for catalysis in the aminoacylase-1\/M20 family. J Biol Chem 278, 44496\u201344504 (2003).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1073\/pnas.0607817104","article-title":"Structure of aspartoacylase, the brain enzyme impaired in Canavan disease","volume":"104","author":"Bitto E","year":"2007","unstructured":"E Bitto, CA Bingman, GE Wesenberg, JG McCoy, GN Phillips, Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. Proc Natl Acad Sci USA 104, 456\u2013461 (2007).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"3484","DOI":"10.1021\/bi702400x","article-title":"Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue","volume":"47","author":"Le Coq J","year":"2008","unstructured":"J Le Coq, et al., Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue. Biochemistry 47, 3484\u20133492 (2008).","journal-title":"Biochemistry"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/j.bbapap.2009.03.022","article-title":"Mouse aminoacylase 3: A metalloenzyme activated by cobalt and nickel","volume":"1794","author":"Tsirulnikov K","year":"2009","unstructured":"K Tsirulnikov, et al., Mouse aminoacylase 3: A metalloenzyme activated by cobalt and nickel. Biochim Biophys Acta 1794, 1049\u20131057 (2009).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1016\/S0278-6915(97)00084-7","article-title":"Public health implications of hazardous waste sites: Findings, assessment and research","volume":"34","author":"DeRosa CT","year":"1996","unstructured":"CT DeRosa, BL Johnson, M Fay, H Hansen, MM Mumtaz, Public health implications of hazardous waste sites: Findings, assessment and research. Food Chem Toxicol 34, 1131\u20131138 (1996).","journal-title":"Food Chem Toxicol"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s002040050461","article-title":"Biotransformation, excretion and nephrotoxicity of haloalkene-derived cysteine S-conjugates","volume":"72","author":"Birner G","year":"1997","unstructured":"G Birner, U Bernauer, M Werner, W Dekant, Biotransformation, excretion and nephrotoxicity of haloalkene-derived cysteine S-conjugates. Arch Toxicol 72, 1\u20138 (1997).","journal-title":"Arch Toxicol"},{"key":"e_1_3_4_13_2","first-page":"114","article-title":"Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: Cysteine conjugate \u03b2-lyase pathway","volume":"27","author":"Dekant W","year":"1994","unstructured":"W Dekant, S Vamvakas, M Anders, Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: Cysteine conjugate \u03b2-lyase pathway. Adv Pharmacol 27, 114\u2013162 (1994).","journal-title":"Adv Pharmacol"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"285","DOI":"10.3109\/01480548608998281","article-title":"Early biological indicators of S-(1,2-dichlorovinyl)-l-cysteine nephrotoxicity in the rabbit","volume":"9","author":"Silber PM","year":"1986","unstructured":"PM Silber, AJ Gandolfi, K Brendel, Early biological indicators of S-(1,2-dichlorovinyl)-l-cysteine nephrotoxicity in the rabbit. Drug Chem Toxicol 9, 285\u2013303 (1986).","journal-title":"Drug Chem Toxicol"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0041-008X(89)90270-6","article-title":"N-acetyl S-(1,2-dichlorovinyl)-l-cysteine produces a similar toxicity to S-(1,2-dichlorovinyl)-l-cysteine in rabbit renal slices\u2014differential transport and metabolism","volume":"101","author":"Wolfgang GHI","year":"1989","unstructured":"GHI Wolfgang, AJ Gandolfi, JL Stevens, K Brendel, N-acetyl S-(1,2-dichlorovinyl)-l-cysteine produces a similar toxicity to S-(1,2-dichlorovinyl)-l-cysteine in rabbit renal slices\u2014differential transport and metabolism. Toxicol Appl Pharmacol 101, 205\u2013219 (1989).","journal-title":"Toxicol Appl Pharmacol"},{"key":"e_1_3_4_16_2","first-page":"474","article-title":"Mechanism of the nephrogenic repair response\u2014studies on proliferation and vimentin expression after 35S-1,2-dichlorovinyl-l-cysteine nephrotoxicity in vivo and in cultured proximal tubule epithelial-cells","volume":"66","author":"Wallin A","year":"1992","unstructured":"A Wallin, GH Zhang, TW Jones, S Jaken, JL Stevens, Mechanism of the nephrogenic repair response\u2014studies on proliferation and vimentin expression after 35S-1,2-dichlorovinyl-l-cysteine nephrotoxicity in vivo and in cultured proximal tubule epithelial-cells. Lab Invest 66, 474\u2013484 (1992).","journal-title":"Lab Invest"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/1056-8719(93)90027-C","article-title":"An in-vitro model of renal proximal tubule cell regeneration","volume":"29","author":"Kays SE","year":"1993","unstructured":"SE Kays, CD Berdanier, AR Swagler, EA Lock, RG Schnellmann, An in-vitro model of renal proximal tubule cell regeneration. J Pharmacol Toxicol Methods 29, 211\u2013215 (1993).","journal-title":"J Pharmacol Toxicol Methods"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S1054-3589(08)61030-3","article-title":"Enzymology of cysteine S-conjugate beta-lyases","volume":"27","author":"Cooper A","year":"1994","unstructured":"A Cooper, Enzymology of cysteine S-conjugate beta-lyases. Adv Pharmacol 27, 71\u2013113 (1994).","journal-title":"Adv Pharmacol"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1080\/15287390500360133","article-title":"Metabolism and tissue distribution of orally administered trichloroethylene in male and female rats: Identification of glutathione- and cytochrome P-450-derived metabolites in liver, kidney, blood, and urine","volume":"69","author":"Lash LH","year":"2006","unstructured":"LH Lash, DA Putt, JC Parker, Metabolism and tissue distribution of orally administered trichloroethylene in male and female rats: Identification of glutathione- and cytochrome P-450-derived metabolites in liver, kidney, blood, and urine. J Toxicol Env Health A 69, 1285\u20131309 (2006).","journal-title":"J Toxicol Env Health A"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1146\/annurev.pharmtox.38.1.501","article-title":"Glutathione-dependent bioactivation of haloalkenes","volume":"38","author":"Anders MW","year":"1998","unstructured":"MW Anders, W Dekant, Glutathione-dependent bioactivation of haloalkenes. Annu Rev Pharmacol Toxicol 38, 501\u2013537 (1998).","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1289\/ehp.00108s2241","article-title":"Mode of action of liver tumor induction by trichloroethylene and its metabolites, trichloroacetate and dichroloacetate","volume":"108","author":"Bull RJ","year":"2000","unstructured":"RJ Bull, Mode of action of liver tumor induction by trichloroethylene and its metabolites, trichloroacetate and dichroloacetate. Environ Health Persp 108, 241\u2013259 (2000).","journal-title":"Environ Health Persp"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1289\/ehp.00108s2323","article-title":"Evaluating noncancer effects of trichloroethylene: dosimetry, mode of action, and risk assesment","volume":"108","author":"Barton HA","year":"2000","unstructured":"HA Barton, HJ Clewell, Evaluating noncancer effects of trichloroethylene: dosimetry, mode of action, and risk assesment. Environ Health Persp 108, 323\u2013334 (2000).","journal-title":"Environ Health Persp"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/0022-2836(92)90671-6","article-title":"Crystal-structure of the complex between carboxypeptidase A and the biproduct analog inhibitor l-benzylsuccinate at 2.0\u00a0\u00c5 resolution","volume":"223","author":"Mangani S","year":"1992","unstructured":"S Mangani, P Carloni, P Orioli, Crystal-structure of the complex between carboxypeptidase A and the biproduct analog inhibitor l-benzylsuccinate at 2.0\u00a0\u00c5 resolution. J Mol Biol 223, 573\u2013578 (1992).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: Model-building tools for molecular graphics","volume":"60","author":"Emsley P","year":"2004","unstructured":"P Emsley, K Cowtan, Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60, 2126\u20132132 (2004).","journal-title":"Acta Crystallogr D"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: A comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams PD","year":"2010","unstructured":"PD Adams, et al., PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr D"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1898","DOI":"10.1016\/j.febslet.2007.03.088","article-title":"Structural characterization of dimeric murine aminoacylase III","volume":"581","author":"Ryazantsev S","year":"2007","unstructured":"S Ryazantsev, et al., Structural characterization of dimeric murine aminoacylase III. FEBS Lett 581, 1898\u20131902 (2007).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"2780","DOI":"10.1093\/bioinformatics\/btn507","article-title":"Searching protein structure databases with DaliLite v.3","volume":"24","author":"Holm L","year":"2008","unstructured":"L Holm, S Kaariainen, P Rosenstrom, A Schenkel, Searching protein structure databases with DaliLite v.3. Bioinformatics 24, 2780\u20132781 (2008).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1021\/ar00158a003","article-title":"Carboxypeptidase A","volume":"22","author":"Christianson DW","year":"1989","unstructured":"DW Christianson, WN Lipscomb, Carboxypeptidase A. Accounts Chem Res 22, 62\u201369 (1989).","journal-title":"Accounts Chem Res"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"2070","DOI":"10.1021\/bi00735a008","article-title":"Binding of by-product analog benzylsuccinic acid by carboxypeptidase A","volume":"12","author":"Byers LD","year":"1973","unstructured":"LD Byers, R Wolfende, Binding of by-product analog benzylsuccinic acid by carboxypeptidase A. Biochemistry 12, 2070\u20132078 (1973).","journal-title":"Biochemistry"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1016\/S0090-9556(25)06807-2","article-title":"Bioactivation of tetrachloroethylene. Role of glutathione S-transferase-catalyzed conjugation versus cytochrome P-450-dependent phospholipid alkylation","volume":"15","author":"Dekant W","year":"1987","unstructured":"W Dekant, G Martens, S Vamvakas, M Metzler, D Henschler, Bioactivation of tetrachloroethylene. Role of glutathione S-transferase-catalyzed conjugation versus cytochrome P-450-dependent phospholipid alkylation. Drug Metab Dispos 15, 702\u2013709 (1987).","journal-title":"Drug Metab Dispos"},{"key":"e_1_3_4_31_2","first-page":"E38","article-title":"Impairment by aminoaxiacetate of ionic response to nutrients in pancreatic islets","volume":"245","author":"Lebrun P","year":"1983","unstructured":"P Lebrun, WJ Malaisse, A Herchuels, Impairment by aminoaxiacetate of ionic response to nutrients in pancreatic islets. Am J Physiol-Endoc M 245, E38\u2013E46 (1983).","journal-title":"Am J Physiol-Endoc M"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1177\/000348949009900113","article-title":"Evaluation of amino-oxyacetic acid as a palliative in tinnitus","volume":"99","author":"Guth PS","year":"1990","unstructured":"PS Guth, et al., Evaluation of amino-oxyacetic acid as a palliative in tinnitus. Ann Oto Rhinol Laryn 99, 74\u201379 (1990).","journal-title":"Ann Oto Rhinol Laryn"},{"key":"e_1_3_4_33_2","first-page":"13","article-title":"Experimentyal \u03b2-alaninuria induced by (aminooxy)acetate","volume":"53","author":"Kurozumi Y","year":"1999","unstructured":"Y Kurozumi, T Abe, W-B Yao, T Ubuka, Experimentyal \u03b2-alaninuria induced by (aminooxy)acetate. Acta Med Okayama 53, 13\u201318 (1999).","journal-title":"Acta Med Okayama"},{"key":"e_1_3_4_34_2","first-page":"804.1","article-title":"Reassessment of the mechanism by which aminoaxyacetate (AOA) inhibits gluconeogenesis (GNG) from lactate","volume":"21","author":"Subramanian RK","year":"2007","unstructured":"RK Subramanian, et al., Reassessment of the mechanism by which aminoaxyacetate (AOA) inhibits gluconeogenesis (GNG) from lactate. FASEB J 21, 804.1 (2007).","journal-title":"FASEB J"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.178.4063.871","article-title":"Fluorescamine\u2014reagent for assay of amino-acids, peptides, proteins, and primary amines in picomole range","volume":"178","author":"Udenfriend S","year":"1972","unstructured":"S Udenfriend, et al., Fluorescamine\u2014reagent for assay of amino-acids, peptides, proteins, and primary amines in picomole range. Science 178, 871\u2013872 (1972).","journal-title":"Science"},{"key":"e_1_3_4_36_2","first-page":"307","volume-title":"Method Enzymol","author":"Otwinowski Z","year":"1997","unstructured":"Z Otwinowski, W Minor, Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol, eds CW Carter, RM Sweet (Academic, San Diego) 276, 307\u2013326 (1997)."},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy AJ","year":"2007","unstructured":"AJ McCoy, et al., Phaser crystallographic software. J Appl Crystallogr 40, 658\u2013674 (2007).","journal-title":"J Appl Crystallogr"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: Programs for protein crystallography","volume":"50","year":"1994","unstructured":", The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50, 760\u2013763 (1994).","journal-title":"Acta Crystallogr D"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1006687107","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,2,26]],"date-time":"2025-02-26T01:24:11Z","timestamp":1740533051000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1006687107"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,10,4]]},"references-count":38,"journal-issue":{"issue":"42","published-print":{"date-parts":[[2010,10,19]]}},"alternative-id":["10.1073\/pnas.1006687107"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1006687107","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,10,4]]},"assertion":[{"value":"2010-10-04","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}