{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,9,11]],"date-time":"2024-09-11T04:35:56Z","timestamp":1726029356485},"publisher-location":"New York, NY","reference-count":22,"publisher":"Springer New York","isbn-type":[{"type":"print","value":"9781493994953"},{"type":"electronic","value":"9781493994960"}],"license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2019]]},"DOI":"10.1007\/978-1-4939-9496-0_15","type":"book-chapter","created":{"date-parts":[[2019,5,23]],"date-time":"2019-05-23T02:31:50Z","timestamp":1558578710000},"page":"233-266","update-policy":"http:\/\/dx.doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Cloning, Expression, and Purification of Recombinant Neisseria gonorrhoeae Proteins"],"prefix":"10.1007","author":[{"given":"Mar\u00eda Victoria","family":"Humbert","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2019,5,23]]},"reference":[{"key":"15_CR1","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/S0076-6879(09)63016-0","volume-title":"Methods in enzymology","author":"A Malhotra","year":"2009","unstructured":"Malhotra A (2009) Chapter 16: Tagging for protein expression. In: Burgess RR, Deutscher MP (eds) Methods in enzymology, vol 463. Academic Press, San Diego, CA, pp 239\u2013258. \n                  https:\/\/doi.org\/10.1016\/S0076-6879(09)63016-0"},{"key":"15_CR2","doi-asserted-by":"publisher","first-page":"6.1.1","DOI":"10.1002\/0471140864.ps0601s80","volume":"80","author":"PT Wingfield","year":"2015","unstructured":"Wingfield PT (2015) Overview of the purification of recombinant proteins. Curr Protoc Protein Sci 80:6.1.1\u20136.135. \n                  https:\/\/doi.org\/10.1002\/0471140864.ps0601s80","journal-title":"Curr Protoc Protein Sci"},{"issue":"4","key":"15_CR3","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1016\/j.copbio.2006.06.003","volume":"17","author":"D Esposito","year":"2006","unstructured":"Esposito D, Chatterjee DK (2006) Enhancement of soluble protein expression through the use of fusion tags. Curr Opin Biotechnol 17(4):353\u2013358. \n                  https:\/\/doi.org\/10.1016\/j.copbio.2006.06.003","journal-title":"Curr Opin Biotechnol"},{"issue":"5","key":"15_CR4","doi-asserted-by":"publisher","first-page":"620","DOI":"10.1002\/biot.201100155","volume":"7","author":"CL Young","year":"2012","unstructured":"Young CL, Britton ZT, Robinson AS (2012) Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications. Biotechnol J 7(5):620\u2013634. \n                  https:\/\/doi.org\/10.1002\/biot.201100155","journal-title":"Biotechnol J"},{"issue":"6","key":"15_CR5","doi-asserted-by":"publisher","first-page":"316","DOI":"10.1016\/j.tibtech.2005.03.012","volume":"23","author":"DS Waugh","year":"2005","unstructured":"Waugh DS (2005) Making the most of affinity tags. Trends Biotechnol 23(6):316\u2013320. \n                  https:\/\/doi.org\/10.1016\/j.tibtech.2005.03.012","journal-title":"Trends Biotechnol"},{"key":"15_CR6","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1385\/0-89603-485-2:257","volume":"13","author":"RC Mierendorf","year":"1998","unstructured":"Mierendorf RC, Morris BB, Hammer B et al (1998) Expression and purification of recombinant proteins using the pET system. Methods Mol Med 13:257\u2013292. \n                  https:\/\/doi.org\/10.1385\/0-89603-485-2:257","journal-title":"Methods Mol Med"},{"issue":"1","key":"15_CR7","doi-asserted-by":"publisher","first-page":"65","DOI":"10.1016\/j.ymeth.2011.08.010","volume":"55","author":"R Vincentelli","year":"2011","unstructured":"Vincentelli R, Cimino A, Geerlof A et al (2011) High-throughput protein expression screening and purification in Escherichia coli. Methods 55(1):65\u201372. \n                  https:\/\/doi.org\/10.1016\/j.ymeth.2011.08.010","journal-title":"Methods"},{"issue":"4","key":"15_CR8","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/1046-5928(92)90001-D","volume":"3","author":"J Porath","year":"1992","unstructured":"Porath J (1992) Immobilized metal ion affinity chromatography. Protein Expr Purif 3(4):263\u2013281. \n                  https:\/\/doi.org\/10.1016\/1046-5928(92)90001-D","journal-title":"Protein Expr Purif"},{"key":"15_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/bs.mie.2014.11.003","volume-title":"Methods in enzymology","author":"A Spriestersbach","year":"2015","unstructured":"Spriestersbach A, Kubicek J, Sch\u00e4fer F et al (2015) Chapter 1: Purification of His-tagged proteins. In: Lorsch JR (ed) Methods in enzymology, vol 559. Academic Press, San Diego, CA, pp 1\u201315. \n                  https:\/\/doi.org\/10.1016\/bs.mie.2014.11.003"},{"key":"15_CR10","doi-asserted-by":"publisher","first-page":"321","DOI":"10.1016\/B978-0-12-418687-3.00027-6","volume":"529","author":"JC Lessard","year":"2013","unstructured":"Lessard JC (2013) Transformation of E. coli via electroporation. Methods Enzymol 529:321\u2013327. \n                  https:\/\/doi.org\/10.1016\/B978-0-12-418687-3.00027-6","journal-title":"Methods Enzymol"},{"issue":"5","key":"15_CR11","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/0167-7799(88)90065-0","volume":"6","author":"JF Kane","year":"1988","unstructured":"Kane JF, Hartley DL (1988) Formation of recombinant protein inclusion bodies in Escherichia coli. Trends Biotechnol 6(5):95\u2013101. \n                  https:\/\/doi.org\/10.1016\/0167-7799(88)90065-0","journal-title":"Trends Biotechnol"},{"issue":"12","key":"15_CR12","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0052482","volume":"7","author":"DJ Leibly","year":"2012","unstructured":"Leibly DJ, Nguyen TN, Kao LT et al (2012) Stabilizing additives added during cell lysis aid in the solubilization of recombinant proteins. PLoS One 7(12):e52482. \n                  https:\/\/doi.org\/10.1371\/journal.pone.0052482","journal-title":"PLoS One"},{"key":"15_CR13","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1038\/nbt0388-291","volume":"6","author":"CH Schein","year":"1988","unstructured":"Schein CH, Noteborn MHM (1988) Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Biotechnology 6:291. \n                  https:\/\/doi.org\/10.1038\/nbt0388-291","journal-title":"Biotechnology"},{"issue":"1","key":"15_CR14","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1186\/1475-2859-4-1","volume":"4","author":"HP Sorensen","year":"2005","unstructured":"Sorensen HP, Mortensen KK (2005) Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 4(1):1. \n                  https:\/\/doi.org\/10.1186\/1475-2859-4-1","journal-title":"Microb Cell Fact"},{"issue":"1","key":"15_CR15","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pep.2005.03.028","volume":"42","author":"M Ishibashi","year":"2005","unstructured":"Ishibashi M, Tsumoto K, Tokunaga M et al (2005) Is arginine a protein-denaturant? Protein Expr Purif 42(1):1\u20136. \n                  https:\/\/doi.org\/10.1016\/j.pep.2005.03.028","journal-title":"Protein Expr Purif"},{"issue":"2","key":"15_CR16","doi-asserted-by":"publisher","first-page":"202","DOI":"10.1016\/S0958-1669(00)00200-7","volume":"12","author":"EDB Clark","year":"2001","unstructured":"Clark EDB (2001) Protein refolding for industrial processes. Curr Opin Biotechnol 12(2):202\u2013207. \n                  https:\/\/doi.org\/10.1016\/S0958-1669(00)00200-7","journal-title":"Curr Opin Biotechnol"},{"key":"15_CR17","first-page":"61","volume":"56","author":"A Mukhopadhyay","year":"1997","unstructured":"Mukhopadhyay A (1997) Inclusion bodies and purification of proteins in biologically active forms. Adv Biochem Eng Biotechnol 56:61\u2013109","journal-title":"Adv Biochem Eng Biotechnol"},{"issue":"1","key":"15_CR18","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1096\/fasebj.10.1.8566547","volume":"10","author":"R Rudolph","year":"1996","unstructured":"Rudolph R, Lilie H (1996) In vitro folding of inclusion body proteins. FASEB J 10(1):49\u201356","journal-title":"FASEB J"},{"key":"15_CR19","doi-asserted-by":"publisher","first-page":"264","DOI":"10.1016\/0076-6879(90)82022-T","volume":"182","author":"FA Marston","year":"1990","unstructured":"Marston FA, Hartley DL (1990) Solubilization of protein aggregates. Methods Enzymol 182:264\u2013276","journal-title":"Methods Enzymol"},{"issue":"1","key":"15_CR20","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.pep.2005.12.002","volume":"48","author":"J Arnau","year":"2006","unstructured":"Arnau J, Lauritzen C, Petersen GE et al (2006) Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr Purif 48(1):1\u201313. \n                  https:\/\/doi.org\/10.1016\/j.pep.2005.12.002","journal-title":"Protein Expr Purif"},{"issue":"2","key":"15_CR21","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1016\/j.pep.2011.08.005","volume":"80","author":"DS Waugh","year":"2011","unstructured":"Waugh DS (2011) An overview of enzymatic reagents for the removal of affinity tags. Protein Expr Purif 80(2):283\u2013293. \n                  https:\/\/doi.org\/10.1016\/j.pep.2011.08.005","journal-title":"Protein Expr Purif"},{"issue":"2","key":"15_CR22","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1016\/0003-2697(89)90602-7","volume":"182","author":"SC Gill","year":"1989","unstructured":"Gill SC, von Hippel PH (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 182(2):319\u2013326. \n                  https:\/\/doi.org\/10.1016\/0003-2697(89)90602-7","journal-title":"Anal Biochem"}],"container-title":["Methods in Molecular Biology","Neisseria gonorrhoeae"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/978-1-4939-9496-0_15","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,5,23]],"date-time":"2019-05-23T02:36:52Z","timestamp":1558579012000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/978-1-4939-9496-0_15"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019]]},"ISBN":["9781493994953","9781493994960"],"references-count":22,"URL":"https:\/\/doi.org\/10.1007\/978-1-4939-9496-0_15","relation":{},"ISSN":["1064-3745","1940-6029"],"issn-type":[{"type":"print","value":"1064-3745"},{"type":"electronic","value":"1940-6029"}],"subject":[],"published":{"date-parts":[[2019]]},"assertion":[{"value":"23 May 2019","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}