{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T11:00:41Z","timestamp":1791889241478,"version":"4.3.4"},"reference-count":58,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,9,1]],"date-time":"2022-09-01T00:00:00Z","timestamp":1661990400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,5,11]],"date-time":"2022-05-11T00:00:00Z","timestamp":1652227200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biotechnology Reports"],"published-print":{"date-parts":[[2022,9]]},"DOI":"10.1016\/j.btre.2022.e00736","type":"journal-article","created":{"date-parts":[[2022,5,13]],"date-time":"2022-05-13T05:28:29Z","timestamp":1652419709000},"page":"e00736","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":6,"special_numbering":"C","title":["Production, purification, and characterization of recombinant rabies virus glycoprotein expressed in PichiaPink\u2122 yeast"],"prefix":"10.1016","volume":"35","author":[{"given":"Hana","family":"Askri","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ines","family":"Akrouti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samia","family":"Rourou","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hela","family":"Kall\u00e8l","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"8","key":"10.1016\/j.btre.2022.e00736_bib0001","doi-asserted-by":"crossref","first-page":"476","DOI":"10.3390\/pr7080476","article-title":"Recombinant proteins for industrial versus pharmaceutical purposes: a review of process and pricing","volume":"7","author":"Puetz","year":"2019","journal-title":"Processes"},{"key":"10.1016\/j.btre.2022.e00736_bib0002","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.sbi.2014.03.005","article-title":"Engineering cells to improve protein expression","volume":"26","author":"Xiao","year":"2014","journal-title":"Curr. Opin. Struct. Biol."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0003","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s00253-011-3654-z","article-title":"Protein secretion in Pichia pastoris and advances in protein production","volume":"93","author":"Damasceno","year":"2012","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0004","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1128\/iai.16.3.754-759.1977","article-title":"Rabies virus glycoprotein. II. Biological and serological characterization","volume":"16","author":"Cox","year":"1977","journal-title":"Infect. Immun."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0005","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1128\/jvi.23.2.286-293.1977","article-title":"Oligosaccharides of the glycoprotein of rabies virus","volume":"23","author":"Dietzschold","year":"1977","journal-title":"J. Virol."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0006","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/0042-6822(92)90465-2","article-title":"Rabies virus glycoprotein is a trimer","volume":"187","author":"Gaudin","year":"1992","journal-title":"Virology"},{"issue":"5","key":"10.1016\/j.btre.2022.e00736_bib0007","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1099\/0022-1317-80-5-1211","article-title":"Deduced structural model for animal rhabdovirus glycoproteins","volume":"80","author":"Walker","year":"1999","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.btre.2022.e00736_bib0008","doi-asserted-by":"crossref","unstructured":"Loza-Rubio, E. and E. Rojas-Anaya, Edible Rabies Vaccines. 2014, Springer Berlin Heidelberg. p. 153\u2013177.","DOI":"10.1007\/978-3-662-43836-7_9"},{"key":"10.1016\/j.btre.2022.e00736_bib0009","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.pep.2017.02.004","article-title":"An effective and simplified DO-stat control strategy for production of rabies glycoprotein in Pichia pastoris","volume":"132","author":"Picotto","year":"2017","journal-title":"Protein Expr. Purif."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0010","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1007\/s00705-016-3128-9","article-title":"Rabies vaccine development by expression of recombinant viral glycoprotein","volume":"162","author":"Astray","year":"2017","journal-title":"Arch. Virol."},{"issue":"3\u20134","key":"10.1016\/j.btre.2022.e00736_bib0011","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1007\/BF01309439","article-title":"Characterization of rabies glycoprotein expressed in yeast","volume":"128","author":"Klepfer","year":"1993","journal-title":"Arch. Virol."},{"issue":"10","key":"10.1016\/j.btre.2022.e00736_bib0012","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1128\/CVI.05258-11","article-title":"Expression and solubilization of insect cell-based rabies virus glycoprotein and assessment of its immunogenicity and protective efficacy in mice","volume":"18","author":"Ramya","year":"2011","journal-title":"Clin. Vaccine Immunol."},{"key":"10.1016\/j.btre.2022.e00736_bib0013","doi-asserted-by":"crossref","DOI":"10.1016\/j.pep.2019.105567","article-title":"Novel strategy for expression and characterization of rabies virus glycoprotein","volume":"168","author":"Zhao","year":"2020","journal-title":"Protein Expr. Purif."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0014","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1186\/s12934-017-0699-4","article-title":"The effect of hypoxia on the lipidome of recombinant Pichia pastoris","volume":"16","author":"Adelantado","year":"2017","journal-title":"Microb. Cell Factories"},{"key":"10.1016\/j.btre.2022.e00736_bib0015","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1186\/1475-2859-10-93","article-title":"Protein trafficking, ergosterol biosynthesis and membrane physics impact recombinant protein secretion in Pichia pastoris","volume":"10","author":"Baumann","year":"2011","journal-title":"Microb. Cell Factories"},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0016","doi-asserted-by":"crossref","first-page":"1380","DOI":"10.1021\/pr8007623","article-title":"The effect of temperature on the proteome of recombinant Pichia pastoris","volume":"8","author":"Dragosits","year":"2009","journal-title":"J. Proteome Res."},{"issue":"4","key":"10.1016\/j.btre.2022.e00736_bib0017","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1002\/biot.201300334","article-title":"In Pichia pastoris, growth rate regulates protein synthesis and secretion, mating and stress response","volume":"9","author":"Rebnegger","year":"2014","journal-title":"Biotechnol. J."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0018","doi-asserted-by":"crossref","first-page":"475","DOI":"10.1590\/S1517-83822014000200014","article-title":"Biomarkers to evaluate the effects of temperature and methanol on recombinant Pichia pastoris","volume":"45","author":"Zepeda","year":"2014","journal-title":"Braz. J. Microbiol."},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0019","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1111\/1751-7915.12350","article-title":"Molecular optimization of rabies virus glycoprotein expression in Pichia pastoris","volume":"9","author":"Ben Azoun","year":"2016","journal-title":"Microb. Biotechnol."},{"key":"10.1016\/j.btre.2022.e00736_bib0020","doi-asserted-by":"crossref","unstructured":"Cregg, J.M. and J.M. Cregg, Pichia protocols. 2nd ed. Methods in Molecular Biology. 2007, Totowa, N.J.: Humana Press. xi, 268 p.","DOI":"10.1007\/978-1-59745-456-8"},{"key":"10.1016\/j.btre.2022.e00736_bib0021","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1007\/978-1-4939-9024-5_3","article-title":"Pichia pastoris Promoters","volume":"1923","author":"Turkanoglu Ozcelik","year":"2019","journal-title":"Methods Mol. Biol."},{"issue":"7","key":"10.1016\/j.btre.2022.e00736_bib0022","doi-asserted-by":"crossref","first-page":"2925","DOI":"10.1007\/s00253-015-6470-z","article-title":"Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris","volume":"99","author":"Puxbaum","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"9","key":"10.1016\/j.btre.2022.e00736_bib0023","doi-asserted-by":"crossref","first-page":"2000","DOI":"10.1016\/j.freeradbiomed.2012.02.048","article-title":"Oxidative protein folding and unfolded protein response elicit differing redox regulation in endoplasmic reticulum and cytosol of yeast","volume":"52","author":"Delic","year":"2012","journal-title":"Free Radic. Biol. Med."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0024","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0378-1119(96)00675-0","article-title":"Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter","volume":"186","author":"Waterham","year":"1997","journal-title":"Gene"},{"key":"10.1016\/j.btre.2022.e00736_bib0025","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1475-2859-5-17","article-title":"Operational strategies, monitoring and control of heterologous protein production in the methylotrophic yeast Pichia pastoris under different promoters: a review","volume":"5","author":"Cos","year":"2006","journal-title":"Microb. Cell Factories"},{"key":"10.1016\/j.btre.2022.e00736_bib0026","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1186\/s12934-014-0163-7","article-title":"High-temperature cultivation of recombinant Pichia pastoris increases endoplasmic reticulum stress and decreases production of human interleukin-10","volume":"13","author":"Zhong","year":"2014","journal-title":"Microb. Cell Factories"},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0027","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1128\/jvi.67.3.1365-1372.1993","article-title":"Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion","volume":"67","author":"Gaudin","year":"1993","journal-title":"J. Virol."},{"issue":"9","key":"10.1016\/j.btre.2022.e00736_bib0028","doi-asserted-by":"crossref","first-page":"4853","DOI":"10.1128\/jvi.65.9.4853-4859.1991","article-title":"Reversible conformational changes and fusion activity of rabies virus glycoprotein","volume":"65","author":"Gaudin","year":"1991","journal-title":"J. Virol."},{"key":"10.1016\/j.btre.2022.e00736_bib0029","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1186\/1752-0509-4-141","article-title":"A multi-level study of recombinant Pichia pastoris in different oxygen conditions","volume":"4","author":"Baumann","year":"2010","journal-title":"BMC Syst. Biol."},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0030","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1002\/bit.10740","article-title":"A study of oxygen transfer in shake flasks using a non-invasive oxygen sensor","volume":"84","author":"Gupta","year":"2003","journal-title":"Biotechnol. Bioeng."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0031","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1080\/13550280590900427","article-title":"Rabies virus receptors","volume":"11","author":"Lafon","year":"2005","journal-title":"J. Neurovirol."},{"issue":"2\u20134","key":"10.1016\/j.btre.2022.e00736_bib0032","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.vetmic.2012.11.031","article-title":"Rabies virus glycoprotein is an important determinant for the induction of innate immune responses and the pathogenic mechanisms","volume":"162","author":"Zhang","year":"2013","journal-title":"Vet. Microbiol."},{"issue":"4","key":"10.1016\/j.btre.2022.e00736_bib0033","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.nbt.2012.11.010","article-title":"Regulation of Pichia pastoris promoters and its consequences for protein production","volume":"30","author":"Vogl","year":"2013","journal-title":"N. Biotechnol."},{"key":"10.1016\/j.btre.2022.e00736_bib0034","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.bej.2013.07.013","article-title":"Fed-batch operational strategies for recombinant Fab production with Pichia pastoris using the constitutive GAP promoter","volume":"79","author":"Garcia-Ortega","year":"2013","journal-title":"Biochem. Eng. J."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0035","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1186\/s12934-019-1240-8","article-title":"Specific growth rate governs AOX1 gene expression, affecting the production kinetics of Pichia pastoris (Komagataella phaffii) PAOX1-driven recombinant producer strains with different target gene dosage","volume":"18","author":"Garrigos-Martinez","year":"2019","journal-title":"Microb. Cell Factories"},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0036","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1002\/bit.21565","article-title":"Influence of specific growth rate on specific productivity and glycosylation of a recombinant avidin produced by a Pichia pastoris Mut+ strain","volume":"99","author":"Schenk","year":"2008","journal-title":"Biotechnol. Bioeng."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0037","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1186\/s12934-016-0542-3","article-title":"Hypoxia-elicited impairment of cell wall integrity, glycosylation precursor synthesis, and growth in scaled-up high-cell density fed-batch cultures of Saccharomyces cerevisiae","volume":"15","author":"Aon","year":"2016","journal-title":"Microb. Cell Factories"},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0038","first-page":"1353","article-title":"Inhibition of asparagine-linked glycosylation participates in hypoxia-induced down-regulation of cell-surface MICA expression","volume":"38","author":"Yamada","year":"2018","journal-title":"Anticancer Res."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0039","doi-asserted-by":"crossref","first-page":"20","DOI":"10.3164\/jcbn.11-015FR","article-title":"Hypoxic regulation of glycosylation via the N-acetylglucosamine cycle","volume":"48","author":"Shirato","year":"2011","journal-title":"J. Clin. Biochem. Nutr."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0040","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/0378-1119(87)90272-1","article-title":"Invertase gene (SUC2) of Saccharomyces cerevisiae as a dominant marker for transformation of Pichia pastoris","volume":"59","author":"Sreekrishna","year":"1987","journal-title":"Gene"},{"issue":"15","key":"10.1016\/j.btre.2022.e00736_bib0041","doi-asserted-by":"crossref","first-page":"4570","DOI":"10.1128\/AEM.00638-16","article-title":"Pichia pastoris exhibits high viability and a low maintenance energy requirement at near-zero specific growth rates","volume":"82","author":"Rebnegger","year":"2016","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.btre.2022.e00736_bib0042","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1186\/s12864-015-1393-8","article-title":"Pichia pastoris regulates its gene-specific response to different carbon sources at the transcriptional, rather than the translational, level","volume":"16","author":"Prielhofer","year":"2015","journal-title":"BMC Genom."},{"issue":"45","key":"10.1016\/j.btre.2022.e00736_bib0043","doi-asserted-by":"crossref","first-page":"E1089","DOI":"10.1073\/pnas.1101494108","article-title":"Survival of starving yeast is correlated with oxidative stress response and nonrespiratory mitochondrial function","volume":"108","author":"Petti","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0044","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1016\/j.bjm.2016.11.005","article-title":"Oxidative stress and antioxidant response in a thermotolerant yeast","volume":"48","author":"Mejia-Barajas","year":"2017","journal-title":"Braz. J. Microbiol."},{"key":"10.1016\/j.btre.2022.e00736_bib0045","doi-asserted-by":"crossref","DOI":"10.1155\/2012\/634674","article-title":"Kluyveromyces lactis: a suitable yeast model to study cellular defense mechanisms against hypoxia-induced oxidative stress","volume":"2012","author":"Gonzalez Siso","year":"2012","journal-title":"Oxid. Med. Cell Longev."},{"issue":"6","key":"10.1016\/j.btre.2022.e00736_bib0046","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1016\/j.ceb.2009.08.005","article-title":"Mitochondrial reactive oxygen species regulate hypoxic signaling","volume":"21","author":"Hamanaka","year":"2009","journal-title":"Curr. Opin. Cell Biol."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0047","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1099\/0022-1317-72-2-359","article-title":"Stable expression of rabies virus glycoprotein in Chinese hamster ovary cells","volume":"72","author":"Burger","year":"1991","journal-title":"J. Gen. Virol."},{"issue":"5","key":"10.1016\/j.btre.2022.e00736_bib0048","doi-asserted-by":"crossref","first-page":"3742","DOI":"10.1128\/jvi.71.5.3742-3750.1997","article-title":"Folding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperones","volume":"71","author":"Gaudin","year":"1997","journal-title":"J. Virol."},{"issue":"15","key":"10.1016\/j.btre.2022.e00736_bib0049","doi-asserted-by":"crossref","first-page":"10690","DOI":"10.1016\/S0021-9258(19)50073-4","article-title":"N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression","volume":"267","author":"Shakin-Eshleman","year":"1992","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0050","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1016\/0042-6822(91)90539-N","article-title":"Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein","volume":"185","author":"Whitt","year":"1991","journal-title":"Virology"},{"key":"10.1016\/j.btre.2022.e00736_bib0051","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.virusres.2013.10.015","article-title":"Efficient N-glycosylation at position 37, but not at position 146, in the street rabies virus glycoprotein reduces pathogenicity","volume":"179","author":"Yamada","year":"2014","journal-title":"Virus Res."},{"issue":"9","key":"10.1016\/j.btre.2022.e00736_bib0052","doi-asserted-by":"crossref","first-page":"5528","DOI":"10.1128\/jvi.69.9.5528-5534.1995","article-title":"Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): g is transported in a fusion-inactive state-like conformation","volume":"69","author":"Gaudin","year":"1995","journal-title":"J. Virol."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0053","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1111\/1751-7915.13499","article-title":"The secretome of Pichia pastoris in fed-batch cultivations is largely independent of the carbon source but changes quantitatively over cultivation time","volume":"13","author":"Burgard","year":"2020","journal-title":"Microb. Biotechnol."},{"issue":"1","key":"10.1016\/j.btre.2022.e00736_bib0054","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1007\/s00253-011-3118-5","article-title":"A proteomic analysis of the Pichia pastoris secretome in methanol-induced cultures","volume":"90","author":"Huang","year":"2011","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"6","key":"10.1016\/j.btre.2022.e00736_bib0055","doi-asserted-by":"crossref","first-page":"e3046","DOI":"10.1002\/btpr.3046","article-title":"Purification of rabies virus glycoprotein produced in Drosophila melanogaster S2 cells: an efficient immunoaffinity method","volume":"36","author":"Pilatti","year":"2020","journal-title":"Biotechnol. Prog."},{"issue":"40","key":"10.1016\/j.btre.2022.e00736_bib0056","doi-asserted-by":"crossref","first-page":"37655","DOI":"10.1074\/jbc.M201374200","article-title":"Rabies virus glycoprotein (RVG) is a trimeric ligand for the N-terminal cysteine-rich domain of the mammalian p75 neurotrophin receptor","volume":"277","author":"Langevin","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.btre.2022.e00736_bib0057","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1128\/JVI.72.2.1085-1091.1998","article-title":"Neuronal cell surface molecules mediate specific binding to rabies virus glycoprotein expressed by a recombinant baculovirus on the surfaces of lepidopteran cells","volume":"72","author":"Tuffereau","year":"1998","journal-title":"J. Virol."},{"issue":"3","key":"10.1016\/j.btre.2022.e00736_bib0058","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1128\/jvi.50.3.691-697.1984","article-title":"Characterization of saturable binding sites for rabies virus","volume":"50","author":"Wunner","year":"1984","journal-title":"J. Virol."}],"container-title":["Biotechnology Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2215017X22000352?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2215017X22000352?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,6]],"date-time":"2025-11-06T06:11:39Z","timestamp":1762409499000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2215017X22000352"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,9]]},"references-count":58,"alternative-id":["S2215017X22000352"],"URL":"https:\/\/doi.org\/10.1016\/j.btre.2022.e00736","relation":{},"ISSN":["2215-017X"],"issn-type":[{"value":"2215-017X","type":"print"}],"subject":[],"published":{"date-parts":[[2022,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Production, purification, and characterization of recombinant rabies virus glycoprotein expressed in PichiaPink\u2122 yeast","name":"articletitle","label":"Article Title"},{"value":"Biotechnology Reports","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.btre.2022.e00736","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"e00736"}}