{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,19]],"date-time":"2025-10-19T17:48:13Z","timestamp":1760896093529},"reference-count":23,"publisher":"Springer Science and Business Media LLC","issue":"6","license":[{"start":{"date-parts":[[2007,9,6]],"date-time":"2007-09-06T00:00:00Z","timestamp":1189036800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2007,9,6]],"date-time":"2007-09-06T00:00:00Z","timestamp":1189036800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Fluoresc"],"published-print":{"date-parts":[[2007,11]]},"DOI":"10.1007\/s10895-007-0227-8","type":"journal-article","created":{"date-parts":[[2007,9,5]],"date-time":"2007-09-05T19:59:57Z","timestamp":1189022397000},"page":"599-605","update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Fluorescence Quenching and Time-resolved Fluorescence studies of \u03b1-Mannosidase from Aspergillus fischeri (NCIM 508)"],"prefix":"10.1007","volume":"17","author":[{"given":"K. S.","family":"Shashidhara","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sushama M.","family":"Gaikwad","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2007,9,6]]},"reference":[{"key":"227_CR1","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1093\/glycob\/4.2.113","volume":"4","author":"KW Moremen","year":"1994","unstructured":"Moremen KW, Trimble R, Herscovics A (1994) Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology 4:113\u2013125","journal-title":"Glycobiology"},{"key":"227_CR2","doi-asserted-by":"publisher","first-page":"28348","DOI":"10.1074\/jbc.271.20.11838","volume":"271","author":"Y-F Liao","year":"1996","unstructured":"Liao Y-F, Lai A, Moremen KW (1996) Cloning, expression, purification, and characterization of the human broad specificity lysosomal acid \u03b1-mannosidase. J Biol Chem 271:28348\u201328358","journal-title":"J Biol Chem"},{"key":"227_CR3","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1146\/annurev.bi.60.070191.001353","volume":"60","author":"EF Neufeld","year":"1991","unstructured":"Neufeld EF (1991) Lysosomal storage diseases. Annu Rev Biochem 60:257\u2013280","journal-title":"Annu Rev Biochem"},{"key":"227_CR4","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1042\/bj3160695","volume":"316","author":"B Henrissat","year":"1996","unstructured":"Henrissat B, Bairoch A (1996) Updating the sequence-based classification of glycosyl hydrolases. Biochem J 316:695\u2013696","journal-title":"Biochem J"},{"key":"227_CR5","first-page":"935","volume":"1","author":"PE Goss","year":"1995","unstructured":"Goss PE, Baker MA, Carver JP, Dennis JW (1995) Inhibitors of carbohydrate processing: a new class of anticancer agents. Clin Cancer Res 1:935\u2013944","journal-title":"Clin Cancer Res"},{"issue":"8","key":"227_CR6","doi-asserted-by":"publisher","first-page":"602","DOI":"10.1016\/0141-0229(95)00145-X","volume":"18","author":"SS Keskar","year":"1996","unstructured":"Keskar SS, Gaikwad SM, Khan MI (1996) Microbial \u03b1-mannosidases. Enzyme Microb Technol 18(8):602\u2013604","journal-title":"Enzyme Microb Technol"},{"key":"227_CR7","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1006\/bbrc.1998.8382","volume":"245","author":"EV Eneyskya","year":"1998","unstructured":"Eneyskya EV, Kulminskaya AA, Savel\u2019ev AN, Shabalin KA, Golubev AM, Neustroev KN (1998) \u03b1-Mannosidase from Trichoderma reesei participates in the postsecretory deglycosylation of glycoproteins. Biochem Biophys Res Commun 245:43\u201349","journal-title":"Biochem Biophys Res Commun"},{"key":"227_CR8","doi-asserted-by":"crossref","first-page":"14757","DOI":"10.1016\/S0021-9258(18)68102-5","volume":"263","author":"SJ Kelly","year":"1998","unstructured":"Kelly SJ, Herscovics A (1998) Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc. J Biol Chem 263:14757\u201314763","journal-title":"J Biol Chem"},{"key":"227_CR9","doi-asserted-by":"publisher","first-page":"533","DOI":"10.1093\/glycob\/9.6.533","volume":"9","author":"ABV Reyna","year":"1999","unstructured":"Reyna ABV, Noyola PP, Mendez CC, Romero EO, Carreon AF (1999) Purification and biochemical characterization of two soluble alpha-mannosidases from Candida albicans. Glycobiology 9:533\u2013537","journal-title":"Glycobiology"},{"key":"227_CR10","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1016\/S0168-1656(99)00222-9","volume":"77","author":"M Mares","year":"2000","unstructured":"Mares M, Callewaert N, Piens K, Claeyssens M, Martinet W, Dewalele S, Contreras H, Dewerte I, Penttila M, Contreras R (2000) Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-\u03b1-d-mannosidase. J Biotechnol 77:255\u2013263","journal-title":"J Biotechnol"},{"key":"227_CR11","doi-asserted-by":"publisher","first-page":"25289","DOI":"10.1074\/jbc.M302621200","volume":"278","author":"Y Tatara","year":"2003","unstructured":"Tatara Y, Lee BR, Yoshida T, Takahashi K, Ichshima E (2003) Identification of catalytic residues of Ca2+-independent 1,2-\u03b1-d-mannosidase from Aspergillus saitoi by site-directed mutagenesis. J Biol Chem 278:25289\u201325294","journal-title":"J Biol Chem"},{"key":"227_CR12","doi-asserted-by":"publisher","first-page":"609","DOI":"10.1016\/j.carres.2005.01.005","volume":"340","author":"VI Athanasopoulos","year":"2005","unstructured":"Athanasopoulos VI, Niranjan K, Rastall RA (2005) The production, purification and characterisation of two novel \u03b1-d-mannosidases from Aspergillus phoenicis. Carbohydr Res 340:609\u2013617","journal-title":"Carbohydr Res"},{"key":"227_CR13","doi-asserted-by":"publisher","first-page":"3254","DOI":"10.1021\/bi00793a015","volume":"10","author":"SS Lehrer","year":"1971","unstructured":"Lehrer SS (1971) Solute perturbation of protein fluorescence. The quenching of tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10:3254\u20133263","journal-title":"Biochemistry"},{"key":"227_CR14","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/S0076-6879(78)49012-3","volume":"49","author":"SS Lehrer","year":"1978","unstructured":"Lehrer SS, Leavis PC (1978) Solute quenching of protein fluorescence. Methods Enzymol 49:222\u2013236","journal-title":"Methods Enzymol"},{"key":"227_CR15","doi-asserted-by":"publisher","first-page":"4171","DOI":"10.1021\/bi00745a021","volume":"12","author":"EM Lakowicz","year":"1973","unstructured":"Lakowicz EM, Weber G (1973) Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12:4171\u20134179","journal-title":"Biochemistry"},{"key":"227_CR16","first-page":"144","volume":"1250","author":"SM Gaikwad","year":"1995","unstructured":"Gaikwad SM, Keskar SS, Khan MI (1995) Purification and characterization of \u03b1-mannosidase from Aspergillus sp. Biochem Biophys Acta 1250:144\u2013148","journal-title":"Biochem Biophys Acta"},{"key":"227_CR17","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1111\/j.1470-8744.1997.tb00421.x","volume":"25","author":"SM Gaikwad","year":"1997","unstructured":"Gaikwad SM, Khan MI, Keskar SS (1997) Chemical modification of \u03b1-mannosidase from Aspergillus sp. Biotechnol Appl Biochem 25:105\u2013108","journal-title":"Biotechnol Appl Biochem"},{"key":"227_CR18","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1007\/BF01080140","volume":"15","author":"SS Keskar","year":"1993","unstructured":"Keskar SS, Gaikwad SM, Khire JM, Khan MI (1993) Production and properties of \u03b1-mannosidase from Aspergillus sp. Biotechnol Lett 15:685\u2013690","journal-title":"Biotechnol Lett"},{"key":"227_CR19","doi-asserted-by":"publisher","first-page":"498","DOI":"10.1016\/S0076-6879(67)11060-4","volume":"11","author":"TF Spande","year":"1967","unstructured":"Spande TF, Witkop B (1967) Determination of the tryptophan content of proteins with N-bromosuccinimide. Methods Enzymol 11:498\u2013506","journal-title":"Methods Enzymol"},{"key":"227_CR20","doi-asserted-by":"crossref","first-page":"446","DOI":"10.1016\/0005-2795(78)90390-2","volume":"533","author":"E Pause","year":"1978","unstructured":"Pause E (1978) The chemical modification of tryptophan residues of \u03b1-mannosidase from Phaseolus vulgaris. Biochim Biophys Acta 533:446\u2013456","journal-title":"Biochim Biophys Acta"},{"key":"227_CR21","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1016\/S1011-1344(99)00079-2","volume":"50","author":"SS Komath","year":"1999","unstructured":"Komath SS, Swamy MJ (1999) Fluorescence quenching, time-resolved fluorescence and chemical modification studies on the tryptophan residues of snake gourd (Trichosanthes anguina) seed lectin. J Photochem Photobiol 50:108\u2013118","journal-title":"J Photochem Photobiol"},{"key":"227_CR22","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1042\/bj1160341","volume":"116","author":"FWJ Teale","year":"1970","unstructured":"Teale FWJ, Badley RA (1970) Depolarization of the intrinsic and extrinsic fluorescence of pepsinogen and pepsin. Biochem J 116:341\u2013348","journal-title":"Biochem J"},{"key":"227_CR23","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/j.jphotobiol.2005.03.003","volume":"80","author":"NA Sultan","year":"2005","unstructured":"Sultan NA, Swamy MJ (2005) Fluorescence quenching and time-resolved fluorescence studies on Trichosanthes dioica seed lectin. J Photochem Photobiol B Biol 80:93\u2013100","journal-title":"J Photochem Photobiol B Biol"}],"container-title":["Journal of Fluorescence"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10895-007-0227-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s10895-007-0227-8\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s10895-007-0227-8","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s10895-007-0227-8.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,2,17]],"date-time":"2024-02-17T19:28:28Z","timestamp":1708198108000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s10895-007-0227-8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,9,6]]},"references-count":23,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2007,11]]}},"alternative-id":["227"],"URL":"https:\/\/doi.org\/10.1007\/s10895-007-0227-8","relation":{},"ISSN":["1053-0509","1573-4994"],"issn-type":[{"value":"1053-0509","type":"print"},{"value":"1573-4994","type":"electronic"}],"subject":[],"published":{"date-parts":[[2007,9,6]]},"assertion":[{"value":"17 May 2007","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 July 2007","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"6 September 2007","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}]}}