{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T20:12:05Z","timestamp":1790107925650,"version":"4.0.1"},"reference-count":61,"publisher":"Elsevier BV","issue":"9","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T00:00:00Z","timestamp":1784246400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100012914","name":"Vidyasirimedhi Institute of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100012914","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100017170","name":"Thailand Science Research and Innovation","doi-asserted-by":"publisher","award":["B23WIS-TSR010"],"award-info":[{"award-number":["B23WIS-TSR010"]}],"id":[{"id":"10.13039\/501100017170","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100017170","name":"Thailand Science Research and Innovation","doi-asserted-by":"publisher","award":["N42A660311"],"award-info":[{"award-number":["N42A660311"]}],"id":[{"id":"10.13039\/501100017170","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.jbc.2026.113351","type":"journal-article","created":{"date-parts":[[2026,7,21]],"date-time":"2026-07-21T06:21:01Z","timestamp":1784614861000},"page":"113351","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Structure-based functionality of a multi-domain periplasmic chitodextrinase from marine bacterium Vibrio cholerae"],"prefix":"10.1016","volume":"302","author":[{"given":"Kanokbhorn","family":"Khumnonkhro","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thitipat","family":"Chongrungreang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shohei","family":"Sakuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert Chales","family":"Robinson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4713-0246","authenticated-orcid":false,"given":"Tamo","family":"Fukamizo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5927-7192","authenticated-orcid":false,"given":"Wipa","family":"Suginta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113351_bib1","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1186\/s40643-022-00574-8","article-title":"Bioeconomic production of high-quality chitobiose from chitin food wastes using an in-house chitinase from Vibrio campbellii","volume":"9","author":"Thomas","year":"2022","journal-title":"Bioresour. Bioproc."},{"key":"10.1016\/j.jbc.2026.113351_bib2","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/0022-2836(78)90063-3","article-title":"The structure of \u03b1-chitin","volume":"120","author":"Minke","year":"1978","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.113351_bib3","doi-asserted-by":"crossref","first-page":"3423","DOI":"10.1002\/pola.20176","article-title":"Physicochemical characterization of \u03b1-chitin, \u03b2-chitin, and \u03b3-chitin separated from natural resources","volume":"42","author":"Jang","year":"2004","journal-title":"J. Polym. Sci. Polym. Chem."},{"key":"10.1016\/j.jbc.2026.113351_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1381-5148(00)00038-9","article-title":"A review of chitin and chitosan applications","volume":"46","author":"Ravi Kumar","year":"2000","journal-title":"React. Funct. Polym."},{"key":"10.1016\/j.jbc.2026.113351_bib5","series-title":"Advances In Microbial Ecology","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1007\/978-1-4684-7612-5_10","article-title":"The ecology of chitin degradation","author":"Gooday","year":"1990"},{"key":"10.1016\/j.jbc.2026.113351_bib6","doi-asserted-by":"crossref","first-page":"D571","DOI":"10.1093\/nar\/gkab1045","article-title":"The carbohydrate-active enzyme database: functions and literature","volume":"50","author":"Drula","year":"2022","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2026.113351_bib7","doi-asserted-by":"crossref","first-page":"5842","DOI":"10.1073\/pnas.97.11.5842","article-title":"Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-\u00c5 resolution","volume":"97","author":"van Aalten","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113351_bib8","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1042\/BJ20050090","article-title":"Molecular directionality in crystalline beta-chitin: hydrolysis by chitinases A and B from Serratia marcescens 2170","volume":"388","author":"Hult","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2026.113351_bib9","doi-asserted-by":"crossref","first-page":"3376","DOI":"10.1111\/j.1742-4658.2005.04753.x","article-title":"Enzymatic properties of wild-type and active site mutants of chitinase A from Vibrio carchariae, as revealed by HPLC-MS","volume":"272","author":"Suginta","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2026.113351_bib10","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1016\/S0969-2126(94)00119-7","article-title":"Crystal structure of a bacterial chitinase at 2.3 \u00c5 resolution","volume":"2","author":"Perrakis","year":"1994","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2026.113351_bib11","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1099\/13500872-142-7-1581","article-title":"Comparative studies of chitinases A and B from Serratia marcescens","volume":"142","author":"Brurberg","year":"1996","journal-title":"Microbiology (Reading)"},{"key":"10.1016\/j.jbc.2026.113351_bib12","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1042\/bj20030273","article-title":"Family 18 chitinase\u2013oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A","volume":"376","author":"Aronson","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.jbc.2026.113351_bib13","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/S0969-2126(01)00220-9","article-title":"Structures and mechanisms of glycosyl hydrolases","volume":"3","author":"Davies","year":"1995","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2026.113351_bib14","doi-asserted-by":"crossref","first-page":"8979","DOI":"10.1073\/pnas.151103798","article-title":"Structural insights into the catalytic mechanism of a family 18 exo-chitinase","volume":"98","author":"van Aalten","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113351_bib15","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1080\/10242420500518482","article-title":"Comparative studies of chitinases A, B and C from Serratia marcescens","volume":"24","author":"Horn","year":"2006","journal-title":"Biocatal. Biotransform."},{"key":"10.1016\/j.jbc.2026.113351_bib16","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/j.vetmic.2009.03.015","article-title":"Vibrios as causal agents of zoonoses","volume":"140","author":"Austin","year":"2010","journal-title":"Vet. Microbiol."},{"key":"10.1016\/j.jbc.2026.113351_bib17","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1073\/pnas.0307645100","article-title":"The chitinolytic cascade in vibrios is regulated by chitin oligosaccharides and a two-component chitin catabolic sensor\/kinase","volume":"101","author":"Li","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.113351_bib18","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1128\/AEM.01412-07","article-title":"Conservation of the chitin utilization pathway in the vibrionaceae","volume":"74","author":"Hunt","year":"2008","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jbc.2026.113351_bib19","doi-asserted-by":"crossref","first-page":"33414","DOI":"10.1074\/jbc.271.52.33414","article-title":"The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase","volume":"271","author":"Keyhani","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113351_bib20","doi-asserted-by":"crossref","first-page":"33425","DOI":"10.1074\/jbc.271.52.33425","article-title":"The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic \u03b2-N-acetylglucosaminidase","volume":"271","author":"Keyhani","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113351_bib21","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0055126","article-title":"Molecular uptake of chitooligosaccharides through chitoporin from the marine bacterium Vibrio harveyi","volume":"8","author":"Suginta","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.113351_bib22","doi-asserted-by":"crossref","first-page":"24276","DOI":"10.1016\/S0021-9258(18)54225-3","article-title":"Chitin utilization by marine bacteria. Degradation and catabolism of chitin oligosaccharides by Vibrio furnissii","volume":"266","author":"Bassler","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113351_bib23","doi-asserted-by":"crossref","first-page":"W320","DOI":"10.1093\/nar\/gku316","article-title":"Deciphering key features in protein structures with the new ENDscript server","volume":"42","author":"Robert","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.jbc.2026.113351_bib24","doi-asserted-by":"crossref","first-page":"2570","DOI":"10.1016\/j.febslet.2015.08.027","article-title":"A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins","volume":"589","author":"Kikhney","year":"2015","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2026.113351_bib25","doi-asserted-by":"crossref","first-page":"1545","DOI":"10.1107\/S1600576717011438","article-title":"BioXTAS RAW: improvements to a free open-source program for small-angle X-ray scattering data reduction and analysis","volume":"50","author":"Hopkins","year":"2017","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib26","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1107\/S1600576723011019","article-title":"BioXTAS RAW 2: new developments for a free open-source program for small-angle scattering data reduction and analysis","volume":"57","author":"Hopkins","year":"2024","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib27","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/nsb0497-269","article-title":"Improved R-factors for diffraction data analysis in macromolecular crystallography","volume":"4","author":"Diederichs","year":"1997","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113351_bib31","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1111\/tpj.12785","article-title":"Crystal structures and inhibitor binding properties of plant class V chitinases: the cycad enzyme exhibits unique structural and functional features","volume":"82","author":"Umemoto","year":"2015","journal-title":"Plant J."},{"key":"10.1016\/j.jbc.2026.113351_bib32","doi-asserted-by":"crossref","first-page":"6144","DOI":"10.1021\/jp909801x","article-title":"The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding","volume":"114","author":"Baban","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.jbc.2026.113351_bib33","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1016\/j.bbagen.2007.03.012","article-title":"Mutations of Trp275 and Trp397 altered the binding selectivity of Vibrio carchariae chitinase A","volume":"1770","author":"Suginta","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113351_bib34","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1111\/j.1742-4658.2005.05079.x","article-title":"Endo\/exo mechanism and processivity of family 18 chitinases produced by Serratia marcescens","volume":"273","author":"Horn","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2026.113351_bib35","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1107\/S0907444902021923","article-title":"De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin","volume":"59","author":"Papanikolau","year":"2003","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib36","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1046\/j.1432-1033.2003.03923.x","article-title":"Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase","volume":"271","author":"Synstad","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jbc.2026.113351_bib37","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.bbapap.2003.09.014","article-title":"Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin","volume":"1696","author":"Vaaje-Kolstad","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jbc.2026.113351_bib38","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.jsb.2008.03.008","article-title":"Crystal structures of Vibrio harveyi chitinase A complexed with chitooligosaccharides: implications for the catalytic mechanism","volume":"162","author":"Songsiriritthigul","year":"2008","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113351_bib39","doi-asserted-by":"crossref","first-page":"11038","DOI":"10.1074\/jbc.M113.454108","article-title":"Chitoporin from Vibrio harveyi, a channel with exceptional sugar specificity","volume":"288","author":"Suginta","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.113351_bib40","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1038\/s41467-017-02523-y","article-title":"Structural basis for chitin acquisition by marine Vibrio species","volume":"9","author":"Aunkham","year":"2018","journal-title":"Nat. Commun"},{"key":"10.1016\/j.jbc.2026.113351_bib41","doi-asserted-by":"crossref","first-page":"19184","DOI":"10.1074\/jbc.M115.660530","article-title":"Chitoporin from the marine bacterium Vibrio harveyi: probing the essential roles of Trp136 at the surface of the construction zone","volume":"290","author":"Chumjan","year":"2015","journal-title":"J. Biol.Chem."},{"key":"10.1016\/j.jbc.2026.113351_bib42","doi-asserted-by":"crossref","first-page":"296","DOI":"10.7164\/antibiotics.40.296","article-title":"A. Search for microbial insect growth regulators. II. Allosamidin, a novel insect chitinase inhibitor","volume":"40","author":"Sakuda","year":"1987","journal-title":"J. Antibiot. (Tokyo)"},{"key":"10.1016\/j.jbc.2026.113351_bib43","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113351_bib44","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1002\/pro.5560041120","article-title":"How to measure and predict the molar absorption coefficient of a protein","volume":"4","author":"Pace","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.jbc.2026.113351_bib29","series-title":"STARANISO Global Phasing Ltd","author":"Tickle","year":"2018"},{"key":"10.1016\/j.jbc.2026.113351_bib30","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1107\/S2059798324001487","article-title":"Advanced exploitation of unmerged reflection data during processing and refinement with autoPROC and BUSTER","volume":"80","author":"Vonrhein","year":"2024","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113351_bib45","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1107\/S0907444903008126","article-title":"A graphical user interface to the CCP4 program suite","volume":"59","author":"Potterton","year":"2003","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib46","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib47","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib48","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib49","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib50","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1107\/S0907444913000462","article-title":"Bulk-solvent and overall scaling revisited: faster calculations, improved results","volume":"69","author":"Afonine","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib51","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1107\/S0907444911047834","article-title":"Use of knowledge-based restraints in phenix.refine to improve macromolecular refinement at low resolution","volume":"68","author":"Headd","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib52","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113351_bib53","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1107\/S2059798322007987","article-title":"CCP4 Cloud for structure determination and project management in macromolecular crystallography","volume":"78","author":"Krissinel","year":"2022","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jbc.2026.113351_bib55","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1107\/S2059798317001061","article-title":"CheckMyMetal: a macromolecular metal-binding validation tool","volume":"73","author":"Zheng","year":"2017","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.jbc.2026.113351_bib56","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1107\/S1600576722001923","article-title":"Performance of the new biological small- and wide-angle X-ray scattering beamline 13A at the Taiwan Photon Source","volume":"55","author":"Shih","year":"2022","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib57","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1107\/S1600576720013412","article-title":"ATSAS 3.0: expanded functionality and new tools for small-angle scattering data analysis","volume":"54","author":"Manalastas-Cantos","year":"2021","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib58","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1107\/S205225251500202X","article-title":"Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering","volume":"2","author":"Tria","year":"2015","journal-title":"IUCrJ"},{"key":"10.1016\/j.jbc.2026.113351_bib59","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1107\/S0021889809000338","article-title":"DAMMIF, a program for rapid ab initio shape determination in small-angle scattering","volume":"42","author":"Franke","year":"2009","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib60","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1107\/S0021889803000268","article-title":"Uniqueness of ab initio shape determination in small-angle scattering","volume":"36","author":"Volkov","year":"2003","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jbc.2026.113351_bib61","doi-asserted-by":"crossref","first-page":"2448","DOI":"10.1021\/bi001537s","article-title":"Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis","volume":"40","author":"Fukamizo","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.jbc.2026.113351_bib62","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.1271\/bbb.62.1643","article-title":"HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme","volume":"62","author":"Koga","year":"1998","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"10.1016\/j.jbc.2026.113351_bib28","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826022234?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826022234?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T19:55:30Z","timestamp":1790106930000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826022234"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":61,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2026,9]]}},"alternative-id":["S0021925826022234"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113351","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structure-based functionality of a multi-domain periplasmic chitodextrinase from marine bacterium Vibrio cholerae","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113351","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113351"}}