{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T14:55:37Z","timestamp":1781103337056,"version":"3.54.1"},"reference-count":59,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2016,4,1]],"date-time":"2016-04-01T00:00:00Z","timestamp":1459468800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Plant Science"],"published-print":{"date-parts":[[2016,4]]},"DOI":"10.1016\/j.plantsci.2016.02.006","type":"journal-article","created":{"date-parts":[[2016,2,8]],"date-time":"2016-02-08T13:31:00Z","timestamp":1454938260000},"page":"135-142","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":34,"special_numbering":"C","title":["The Arabidopsis KS-type dehydrin recovers lactate dehydrogenase activity inhibited by copper with the contribution of His residues"],"prefix":"10.1016","volume":"245","author":[{"given":"Masakazu","family":"Hara","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shuhei","family":"Monna","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takae","family":"Murata","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taiyo","family":"Nakano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shono","family":"Amano","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markus","family":"Nachbar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hermann","family":"W\u00e4tzig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.plantsci.2016.02.006_bib0005","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1111\/j.1399-3054.1996.tb00546.x","article-title":"Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins","volume":"97","author":"Close","year":"1996","journal-title":"Physiol. Plant."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0010","doi-asserted-by":"crossref","first-page":"536","DOI":"10.2478\/s11658-006-0044-0","article-title":"Plant dehydrins: tissue location, structure and function","volume":"11","author":"Rorat","year":"2006","journal-title":"Cell Mol. Biol. Lett."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0015","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1104\/pp.108.120725","article-title":"The enigmatic LEA proteins and other hydrophilins","volume":"148","author":"Battaglia","year":"2008","journal-title":"Plant Physiol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0020","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1186\/1471-2164-9-118","article-title":"LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana","volume":"9","author":"Hundertmark","year":"2008","journal-title":"BMC Genomics"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0025","series-title":"Plant Desiccation Tolerance","first-page":"289","article-title":"Dehydrins: molecular biology, structure and function","author":"Eriksson","year":"2011"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0030","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.4161\/psb.6.10.17088","article-title":"Plant dehydrins and stress tolerance: versatile proteins for complex mechanisms","volume":"6","author":"Hanin","year":"2011","journal-title":"Plant Signal. Behav."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0035","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1105\/tpc.112.106062","article-title":"Multifarious roles of intrinsic disorder in proteins illustrate its broad impact on plant biology","volume":"25","author":"Sun","year":"2013","journal-title":"Plant Cell"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0040","doi-asserted-by":"crossref","first-page":"576","DOI":"10.3389\/fpls.2014.00576","article-title":"Disorder and function: a review of the dehydrin protein family","volume":"5","author":"Graether","year":"2014","journal-title":"Front. Plant Sci."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0045","doi-asserted-by":"crossref","first-page":"9587","DOI":"10.1021\/bi201205m","article-title":"Phosphorylation of Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 facilitates cation-induced conformational changes and actin assembly","volume":"50","author":"Rahman","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0050","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1007\/s12104-011-9297-2","article-title":"Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14","volume":"5","author":"Szalain\u00e9 \u00c1goston","year":"2011","journal-title":"Biomol. NMR Assign."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0055","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1007\/BF00019503","article-title":"Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants","volume":"26","author":"Godoy","year":"1994","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0060","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1105\/tpc.10.4.623","article-title":"Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat","volume":"10","author":"Danyluk","year":"1998","journal-title":"Plant Cell"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0065","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1034\/j.1399-3054.1999.106205.x","article-title":"Characterization of an 80-kDa dehydrin-like protein in barley responsive to cold acclimation","volume":"106","author":"Bravo","year":"1999","journal-title":"Physiol. Plant."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0070","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1023\/A:1006469128280","article-title":"Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana","volume":"45","author":"Nylander","year":"2001","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0075","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1007\/s00425-003-0986-7","article-title":"Enhancement of cold tolerance and inhibition of lipid peroxidation by Citrus dehydrin in transgenic tobacco","volume":"217","author":"Hara","year":"2001","journal-title":"Planta"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0080","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1023\/B:PLAN.0000040903.66496.a4","article-title":"Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis","volume":"54","author":"Puhakainen","year":"2004","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0085","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/j.1467-7652.2004.00082.x","article-title":"Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves","volume":"2","author":"Houde","year":"2004","journal-title":"Plant Biotechnol. J."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0090","doi-asserted-by":"crossref","first-page":"1164","DOI":"10.1016\/j.plantsci.2006.02.002","article-title":"Expression of a Solanum sogarandinum SK3-type dehydrin enhances cold tolerance in transgenic cucumber seedlings","volume":"170","author":"Yin","year":"2006","journal-title":"Plant Sci."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0095","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1007\/s10725-011-9580-3","article-title":"Overexpression of a maize dehydrin gene ZmDHN2b, in tobacco enhances tolerance to low temperature","volume":"65","author":"Xing","year":"2011","journal-title":"Plant Growth Regul."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0100","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1007\/s00425-011-1531-8","article-title":"Functional characterization of an acidic SK3 dehydrin isolated from an Opuntia streptacantha cDNA library","volume":"235","author":"Ochoa-Alfaro","year":"2012","journal-title":"Planta"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0105","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1023\/A:1020329401191","article-title":"Wheat LEA genes, PMA80 and PMA1959 enhance dehydration tolerance of transgenic rice (Oryza sativa L.)","volume":"10","author":"Cheng","year":"2002","journal-title":"Mol. Breed."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0110","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1111\/j.1744-7348.2004.tb00341.x","article-title":"Maize Rab17 overexpression in Arabidopsis plants promotes osmotic stress tolerance","volume":"144","author":"Figueras","year":"2004","journal-title":"Annal. Appl. Biol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0115","doi-asserted-by":"crossref","first-page":"2017","DOI":"10.1007\/s00299-007-0412-x","article-title":"Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in Arabidopsis thaliana","volume":"26","author":"Brini","year":"2007","journal-title":"Plant Cell Rep."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0120","doi-asserted-by":"crossref","first-page":"9225","DOI":"10.5897\/AJB10.1196","article-title":"Expression of a SK2-type dehydrin gene from Populus euphratica in a Populus tremula\u00d7Populus alba hybrid increased drought tolerance","volume":"10","author":"Wang","year":"2011","journal-title":"Afr. J. Biotechnol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0125","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1007\/s00425-011-1455-3","article-title":"MusaDHN-1 a novel multiple stress-inducible SK(3)-type dehydrin gene, contributes affirmatively to drought- and salt-stress tolerance in banana","volume":"234","author":"Shekhawat","year":"2011","journal-title":"Planta"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0130","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1007\/s12033-012-9606-8","article-title":"The K-segments of the wheat dehydrin DHN-5 are essential for the protection of lactate dehydrogenase and \u03b2-glucosidase activities in vitro","volume":"54","author":"Drira","year":"2013","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0135","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1104\/pp.109.136697","article-title":"The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes","volume":"150","author":"Koag","year":"2009","journal-title":"Plant Physiol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0140","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1104\/pp.108.118208","article-title":"Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins","volume":"147","author":"Kovacs","year":"2008","journal-title":"Plant Physiol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0145","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1105\/tpc.111.085183","article-title":"Tunable membrane binding of the intrinsically disordered dehydrin Lti30, a cold-induced plant stress protein","volume":"23","author":"Eriksson","year":"2011","journal-title":"Plant Cell"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0150","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.bbamem.2012.11.031","article-title":"Interactions of Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 with membranes at cold and ambient temperatures-surface morphology and single-molecule force measurements show phase separation, and reveal tertiary and quaternary associations","volume":"1828","author":"Rahman","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0155","doi-asserted-by":"crossref","first-page":"2243","DOI":"10.1529\/biophysj.106.084723","article-title":"Protein\u2013water and protein\u2013buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects","volume":"91","author":"Tompa","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0160","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1104\/pp.002550","article-title":"The calcium-binding activity of a vacuole-associated, dehydrin-like protein is regulated by phosphorylation","volume":"130","author":"Heyen","year":"2002","journal-title":"Plant Physiol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0165","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1111\/j.1365-3040.2005.01348.x","article-title":"Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins","volume":"28","author":"Alsheikh","year":"2005","journal-title":"Plant Cell Environ."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0170","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1111\/j.1365-3040.2009.01947.x","article-title":"DNA binding of citrus dehydrin promoted by zinc ion","volume":"32","author":"Hara","year":"2009","journal-title":"Plant Cell Environ."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0175","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1093\/pcp\/pcs040","article-title":"Characterization of a novel Y2K-type dehydrin VrDhn1 from Vigna radiata","volume":"53","author":"Lin","year":"2012","journal-title":"Plant Cell Physiol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0180","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1006\/prep.2000.1297","article-title":"Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography","volume":"20","author":"Svensson","year":"2000","journal-title":"Protein Exp. Purif."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0185","doi-asserted-by":"crossref","first-page":"25062","DOI":"10.1074\/jbc.M201896200","article-title":"A metal-binding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L","volume":"277","author":"Kr\u00fcger","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0190","doi-asserted-by":"crossref","first-page":"2695","DOI":"10.1093\/jxb\/eri262","article-title":"Metal binding by citrus dehydrin with histidine-rich domains","volume":"56","author":"Hara","year":"2005","journal-title":"J. Exp. Bot."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0195","first-page":"1351","article-title":"Plant responses to abiotic stresses: heavy metal-induced oxidative stress and protection by mycorrhization","volume":"53","author":"Sch\u00fctzend\u00fcbel","year":"2002","journal-title":"J. Exp. Bot."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0200","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1093\/jxb\/ert016","article-title":"A KS-type dehydrin and its related domains reduce Cu-promoted radical generation and the histidine residues contribute to the radical-reducing activities","volume":"64","author":"Hara","year":"2013","journal-title":"J. Exp. Bot."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0205","doi-asserted-by":"crossref","first-page":"2103","DOI":"10.1007\/s11738-011-0749-1","article-title":"Biochemical characterization of the Arabidopsis KS-type dehydrin protein, whose gene expression is constitutively abundant rather than stress dependent","volume":"33","author":"Hara","year":"2011","journal-title":"Acta Physiol. Plant."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0210","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1007\/BF02858564","article-title":"Biochemical, physiological and structure effects of excess copper in plants","volume":"57","author":"Fernandes","year":"1991","journal-title":"Bot. Rev."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0215","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s10534-004-5787-3","article-title":"Biosensors for heavy metals","volume":"18","author":"Verma","year":"2005","journal-title":"Biometals"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0220","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1007\/s00425-003-1171-8","article-title":"Expression of KS-type dehydrins is primarily regulated by factors related to organ type and leaf developmental stage during vegetative growth","volume":"218","author":"Rorat","year":"2004","journal-title":"Planta"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0225","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1093\/jb\/mvr082","article-title":"Cu2+ triggers reversible aggregation of a disordered His-rich dehydrin MpDhn12 from Musa paradisiaca","volume":"150","author":"Mu","year":"2011","journal-title":"J. Biochem."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0230","doi-asserted-by":"crossref","first-page":"9587","DOI":"10.1021\/bi201205m","article-title":"Phosphorylation of Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2 facilitates cation-induced conformational changes and actin assembly","volume":"50","author":"Rahman","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0235","doi-asserted-by":"crossref","first-page":"503","DOI":"10.4161\/psb.11085","article-title":"The multifunctionality of dehydrins: an overview","volume":"5","author":"Hara","year":"2010","journal-title":"Plant Signal. Behav."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0240","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1007\/s12033-007-9005-8","article-title":"BjDHNs confer heavy-metal tolerance in plants","volume":"38","author":"Xu","year":"2008","journal-title":"Mol. Biotechnol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0245","doi-asserted-by":"crossref","first-page":"755","DOI":"10.2478\/s11756-010-0090-y","article-title":"Role of plant dehydrins in antioxidation mechanisms","volume":"65","author":"Sun","year":"2010","journal-title":"Biologia"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0250","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0021-9673(02)02057-5","article-title":"Current and prospective applications of metal ion-protein binding","volume":"988","author":"Ueda","year":"2003","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0255","doi-asserted-by":"crossref","first-page":"702","DOI":"10.3389\/fpls.2015.00702","article-title":"Nuclear localization of the dehydrin OpsDHN1 is determined by histidine-rich motif","volume":"6","author":"Hern\u00e1ndez-S\u00e1nchez","year":"2015","journal-title":"Front. Plant Sci."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0260","doi-asserted-by":"crossref","first-page":"1968","DOI":"10.1073\/pnas.70.7.1968","article-title":"Structure-function relationships in lactate dehydrogenase","volume":"70","author":"Adams","year":"1973","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0265","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.bbrc.2008.05.052","article-title":"Heavy metal ions are potent inhibitors of protein folding","volume":"372","author":"Sharma","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0270","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1002\/elps.201300050","article-title":"Precise, fast and flexible determination of protein interactions by affinity capillary electrophoresis. Part 2: cations","volume":"34","author":"Redweik","year":"2013","journal-title":"Electrophoresis"},{"key":"10.1016\/j.plantsci.2016.02.006_bib0275","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1021\/ar9501535","article-title":"Amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif of proteins and peptides: metal binding, DNA cleavage, and other properties","volume":"30","author":"Harford","year":"1997","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0280","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1006\/jcis.1999.6193","article-title":"Microcalorimetric studies of the interactions of lysozyme with immobilized metal ions: effects of ion, pH value, and salt concentration","volume":"214","author":"Lin","year":"1999","journal-title":"J. Colloid Interface Sci."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0285","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1104\/pp.116.1.173","article-title":"Oxidative damage in pea plants exposed to water deficit or paraquat","volume":"116","author":"Iturbe-Ormaetxe","year":"1998","journal-title":"Plant Physiol."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0290","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1002\/pro.534","article-title":"Cryoprotective mechanism of a small intrinsically disordered dehydrin protein","volume":"20","author":"Hughes","year":"2011","journal-title":"Protein Sci."},{"key":"10.1016\/j.plantsci.2016.02.006_bib0295","doi-asserted-by":"crossref","first-page":"1376","DOI":"10.1104\/pp.113.226803","article-title":"The importance of size and disorder in the cryoprotective effects of dehydrins","volume":"163","author":"Hughes","year":"2013","journal-title":"Plant Physiol."}],"container-title":["Plant Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0168945216300188?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0168945216300188?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,29]],"date-time":"2025-09-29T23:32:04Z","timestamp":1759188724000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0168945216300188"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,4]]},"references-count":59,"alternative-id":["S0168945216300188"],"URL":"https:\/\/doi.org\/10.1016\/j.plantsci.2016.02.006","relation":{},"ISSN":["0168-9452"],"issn-type":[{"value":"0168-9452","type":"print"}],"subject":[],"published":{"date-parts":[[2016,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The Arabidopsis KS-type dehydrin recovers lactate dehydrogenase activity inhibited by copper with the contribution of His residues","name":"articletitle","label":"Article Title"},{"value":"Plant Science","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.plantsci.2016.02.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2016 Elsevier Ireland Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}