{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,18]],"date-time":"2026-03-18T19:42:31Z","timestamp":1773862951231,"version":"3.50.1"},"reference-count":43,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2003,11,1]],"date-time":"2003-11-01T00:00:00Z","timestamp":1067644800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2003,11]]},"DOI":"10.1016\/j.bbapap.2003.08.002","type":"journal-article","created":{"date-parts":[[2003,9,12]],"date-time":"2003-09-12T13:20:58Z","timestamp":1063372858000},"page":"52-63","source":"Crossref","is-referenced-by-count":37,"title":["A proposed mechanism for the thermal denaturation of a recombinant Bacillus halmapalus \u03b1-amylase\u2014the effect of calcium ions"],"prefix":"10.1016","volume":"1652","author":[{"given":"Anders D","family":"Nielsen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marc L","family":"Pusey","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Claus C","family":"Fuglsang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter","family":"Westh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2003.08.002_BIB1","doi-asserted-by":"crossref","first-page":"329","DOI":"10.3109\/10409238909082556","article-title":"Microbial amylolytic enzymes","volume":"24","author":"Vihinen","year":"1989","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB2","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1080\/10408399509527706","article-title":"Amylolytic enzymes and products derived from starch: a review","volume":"35","author":"Guzm\u00e1n-Maldonado","year":"1995","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB3","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/S0167-4838(00)00240-5","article-title":"Protein engineering of bacterial \u03b1-amylases","volume":"1543","author":"Nielsen","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB4","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1016\/S0958-1669(02)00328-2","article-title":"Industrial enzyme applications","volume":"13","author":"Kirk","year":"2002","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB5","first-page":"203","article-title":"Engineering the thermostability of Bacillus licheniformis alpha-amylase","volume":"57","author":"Declerck","year":"2002","journal-title":"Biologica"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB6","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1093\/oxfordjournals.jbchem.a135381","article-title":"Complete nucleotide sequence of a gene coding for heat- and pH-stable alpha-amylase of Bacillus licheniformis: comparison of the amino acid sequences of three bacterial liquefying alpha-amylases deduced from the DNA sequences","volume":"98","author":"Yuuki","year":"1985","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB7","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1006\/jmbi.1994.0106","article-title":"Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 \u00c5 resolution","volume":"246","author":"Machius","year":"1995","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB8","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/S1016-8478(23)13289-4","article-title":"Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 \u00c5 resolution","volume":"7","author":"Hwang","year":"1997","journal-title":"Mol. Cells"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB9","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1093\/oxfordjournals.jbchem.a002878","article-title":"Crystal structure of Bacillus stearothermaphilus alpha-amylase: possible factors determining the thermostability","volume":"129","author":"Suvd","year":"2001","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB10","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/S0969-2126(98)00032-X","article-title":"Activation of Bacillus licheniformis alpha-amylase through a disorder\u2013order transition of the substrate-binding site mediated by a calcium\u2013sodium\u2013calcium metal triad","volume":"6","author":"Machius","year":"1998","journal-title":"Structure"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB11","doi-asserted-by":"crossref","first-page":"2901","DOI":"10.1016\/S0021-9258(18)69691-7","article-title":"Metal content of amylases of various origins","volume":"234","author":"Vallee","year":"1959","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB12","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1042\/bj2630665","article-title":"Kinetic study of the irreversible thermal denaturation of Bacillus licheniformis alpha amylase","volume":"263","author":"Violet","year":"1989","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB13","doi-asserted-by":"crossref","first-page":"6244","DOI":"10.1021\/bi00478a019","article-title":"Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1 \u00c5\u2014some resolution of two enzymes from Aspergillus","volume":"29","author":"Boel","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB14","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1111\/j.1432-1033.1974.tb03257.x","article-title":"The allosteric activation of mammalian alpha-amylase by chloride","volume":"41","author":"Levitzki","year":"1974","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB15","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1006\/jmbi.2000.4025","article-title":"Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase","volume":"301","author":"Declerck","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB16","doi-asserted-by":"crossref","first-page":"9099","DOI":"10.1021\/bi0000317","article-title":"Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes","volume":"39","author":"Brzozowski","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB17","doi-asserted-by":"crossref","first-page":"3092","DOI":"10.1016\/S0021-9258(18)69039-8","article-title":"Why is one Bacillus alpha-amylase more resistant against irreversible thermoinactivation than another?","volume":"263","author":"Tomazic","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB18","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1016\/S0021-9258(18)69038-6","article-title":"Mechanisms of irreversible thermal inactivation of Bacillus alpha-amylases","volume":"263","author":"Tomazic","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB19","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1021\/bp980024y","article-title":"Model for inactivation of alpha-amylase in the presence of salts: theoretical and experimental studies","volume":"14","author":"Lecker","year":"1998","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB20","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1021\/bp960053d","article-title":"Theoretical and experimental studies of the effects of heat, EDTA, and enzyme concentration on the inactivation rate of alpha-amylase from Bacillus sp.","volume":"12","author":"Lecker","year":"1996","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB21","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1042\/bj20011436","article-title":"Calcium-binding parameter of Bacillus amyloliquefaciens alpha-amylase determined by inactivation kinetics","volume":"364","author":"Tanaka","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB22","doi-asserted-by":"crossref","first-page":"19392","DOI":"10.1016\/S0021-9258(19)47314-6","article-title":"The calcium requirement for stability and enzymatic activity of two isoforms of barley aleurone alpha-amylase","volume":"264","author":"Bush","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB23","doi-asserted-by":"crossref","first-page":"199","DOI":"10.5458\/jag.46.199","article-title":"Development of industrially important \u03b1-amylases","volume":"46","author":"Bisgaard-Frantzen","year":"1999","journal-title":"J. Appl. Glycosci."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB24","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1006\/abio.1997.2236","article-title":"A new ultrasensitive scanning calorimeter","volume":"250","author":"Plotnikov","year":"1997","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB25","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/S0006-3495(92)81899-4","article-title":"Theoretical analysis of Lumry\u2013Eyring models in differential scanning calorimetry","volume":"61","author":"Sanchez-Ruiz","year":"1992","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB26","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1002\/bem.2250050406","article-title":"Calorimetric measurements of the effect of 330-MHz radiofrequency radiation on human erythrocyte ghosts","volume":"5","author":"Shnyrov","year":"1984","journal-title":"Bioelectromagnetics"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB27","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0167-4838(01)00236-9","article-title":"Chemical modification of bacterial alpha-amylases: changes in tertiary structures and the effect of additional calcium","volume":"1548","author":"Khajeh","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB28","first-page":"158","article-title":"Spectroscopic and electrophoretic studies on structural stability of alpha amylase from Bacillus amyloliquefaciens","volume":"24","author":"Oh","year":"1991","journal-title":"Kor. Biochem. J."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB29","doi-asserted-by":"crossref","first-page":"12706","DOI":"10.1021\/bi00165a023","article-title":"Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation","volume":"31","author":"Lepock","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB30","doi-asserted-by":"crossref","first-page":"1648","DOI":"10.1021\/bi00405a039","article-title":"Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin","volume":"27","author":"Sanchez-Ruiz","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB31","doi-asserted-by":"crossref","first-page":"2061","DOI":"10.1021\/bi00222a009","article-title":"Kinetic study on the irreversible thermal denaturation of yeast phosphoglycerate kinase","volume":"30","author":"Galisteo","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB32","doi-asserted-by":"crossref","first-page":"4613","DOI":"10.1021\/bi982650+","article-title":"Thermodynamic stability of a cold-active alpha-amylase from the Antarctic bacterium Alteromonas haloplanctis","volume":"38","author":"Feller","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB33","doi-asserted-by":"crossref","first-page":"10723","DOI":"10.1021\/bi010808b","article-title":"Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation","volume":"40","author":"Fitter","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB34","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1021\/j150512a005","article-title":"Conformation changes of proteins","volume":"58","author":"Lumry","year":"1954","journal-title":"J. Phys. Chem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB35","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/978-1-4899-1727-0_6","article-title":"Differential scanning calorimetry of proteins","volume":"24","author":"Sanchez-Ruiz","year":"1995","journal-title":"Sub-cell. Biochem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB36","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1111\/j.1432-1033.1991.tb16230.x","article-title":"Differential scanning calorimetric study of carboxypeptidase B, procarboxypeptidase B and its globular activation domain","volume":"200","author":"Conejero-Lara","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB37","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1042\/bj20030220","article-title":"The effect of calcium ions on the irreversible denaturation of a recombinant Bacillus halmapalus \u03b1 amylase\u2014a calorimetric investigation","volume":"373","author":"Nielsen","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB38","doi-asserted-by":"crossref","first-page":"6927","DOI":"10.1021\/bi00481a024","article-title":"Study of strong to ultratight protein interactions using differential scanning calorimetry","volume":"29","author":"Brandts","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB39","doi-asserted-by":"crossref","first-page":"4063","DOI":"10.1021\/bi00387a048","article-title":"Differential scanning calorimetric study of the thermal unfolding of Taka-amylase A from Aspergillus oryzae","volume":"26","author":"Fukada","year":"1987","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2003.08.002_BIB40","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0014-5793(93)81400-T","article-title":"Thermal transitions in the purple membrane from Halobacterium halobium","volume":"324","author":"Shnyrov","year":"1993","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB41","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/0301-4622(94)00033-G","article-title":"Extended theoretical-analysis of irreversible protein thermal unfolding","volume":"52","author":"Milardi","year":"1994","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB42","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0003-2697(02)00655-3","article-title":"Isothermal titration calorimetric procedure to determine protein\u2013metal ion binding parameters in the presence of excess metal ion or chelator","volume":"314","author":"Nielsen","year":"2003","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbapap.2003.08.002_BIB43","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/S0301-4622(98)00149-5","article-title":"Folding under inequilibrium conditions as a possible reason for partial irreversibility of heat-denatured proteins: computer simulation study","volume":"73","author":"Potekhin","year":"1998","journal-title":"Biophys. Chem."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963903002693?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963903002693?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,1,10]],"date-time":"2024-01-10T18:47:07Z","timestamp":1704912427000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963903002693"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2003,11]]},"references-count":43,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2003,11]]}},"alternative-id":["S1570963903002693"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2003.08.002","relation":{},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2003,11]]}}}