[1] Oliveberg M,Wolynes P G.The experimental survey of protein-folding energy landscape.Quarterly Reviews of Biophysics,2005,38(3):245-288.
[2] Krishna M M, Lin Y, Mayne L,et al. Intimate view of a kinetic protein folding intermediate: residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity.Journal of Molecular Biology,2003,334(3):501-513.
[3] Clark E D.Refolding of recombinant proteins.Current Opinion in Biotechnology,1998,9(2):157-163.
[4] Hudson D A, Gannon S A,Thorpe C.Oxidative protein folding:From thiol–disulfide exchange reactions to the redox poise of the endoplasmic reticulum. Free Radical Biology and Medicine,2015,3:171-182.
[5] Anfinsen C B,Redfield R R,Choate W L,et al.Studies on the gross structure,cross-linkages,and terminal sequences in ribonuclease.The Journal of Biological Chemistry,1954,207(1):201-210.
[6] Frerman F E,Duncombe G R. Studies on the subunits of Escherichia coli coenzyme A transferase:reconstitution of an active enzyme.Biochimica et Biophysica Acta,1979,580(2):289-297.
[7] Hagen A J,Hatton T A,Wang D I.Protein refolding in reversed micelles.Biotechnology and Bioengineering,1990,35(10):955-965.
[8] 耿信笃,冯文科,常建华,等.用制备型高效疏水色谱复性和预分离重组人干扰素-gamma.高技术通讯,1991,1(7):1-4. Geng X D,Feng W K,Chang J H,et al.Refolding and pre-separation of recombinant human interferon-gamma using preparative high performance liquid chromatography. High Technology Letters,1991,1(7):1-4.
[9] Werner M H,Clore G M,Gronenborn A M,et al.Refolding proteins by gel filtration chromatography.FEBS Letters,1994,345(2-3):125-130.
[10] Suttnar J,Dyr J E,Hamsikova E,et al.Procedure for refolding and purification of recombinant proteins from Escherichia coli inclusion bodies using a strong anion exchanger.Jouranl of Chromatography B,1994,656(1):123-126.
[11] Taguchi H,Makino Y,Yoshida M.Monomeric chaperonin-60 and its 50-kDa fragment posses the ability to interact with non-native proteins,to suppress aggregation,and to promote protein folding.The Journal of Biological Chemistry,1994,269(11):8529-8534.
[12] Phadtare S,Fisher M T,Yarbrough L R. Refolding and release of tubulins by a functional immobilized groEL column. Biochimica et Biophysica Acta,1994,1208(1):189-192.
[13] Forciniti D.Protein refolding using aqueous two-phase systems.Journal of Chromatography A,1994,668(1):95-100.
[14] Gorovits B M,Horowitz P M.High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure.Biochemistry,1998,37(17):6132-6135.
[15] Cho T H,Ahn S J,Lee E K.Refolding of protein inclusion bodies directly from E.coli homogenate using expanded bed adsorption chromatography.Bioseparation,2001,10(4-5):189-196.
[16] Chiku H,Matsui M,Murakami S,et al. Zeolites as new chromatographic carriers for proteins:easy recovery of proteins adsorbed on zeolites by polyethylene glycol.Analytical Biochemistry,2003,318(1):80-85.
[17] Chow M K, Amin A A, Fulton K F, et al. The REFOLD database: a tool for the optimization of protein expression and refolding.Nucleic Acids Research,2006,34(Database issue):D207-D212.
[18] Chen Z,Cui Y F,Leong Y A,et al.Efficient production of recombinant IL-21 proteins for pre-clinical studies by a two-step dilution refoldinong method.International Immunopharmacology,2013,16(3):376-381.
[19] Zhao D W,Liu Y D,Wang Y J,et al.Membrane combined with hydrophilic macromolecules enhances protein refolding at high concentration.Process Biochemisty.2014,49(7):1129-1134.
[20] Englander S W,Mayne L.The nature of protein folding pathways.Proceedings of the National Academy Sciences of the United States of America,2014,11(45):15873-15880.
[21] Yuan J,Zhou H F,Yang Y C,et al.Refolding and simultaneous purification of recombinant human proinsulin from inclusion bodies on protein-folding liquid-chromatography columns.Biomedical Chromatography,2014,doi:10.1002/bmc.3358.
[22] Rane A M,Jonnalagadda S,Li Z Y. On-column refolding of bone morphogenetic protein-2 using cation exchange resin.Protein Expression and Purification,2013,90(2):135-140.
[23] Sharapova O A,Yurkova M S,Laurinavichyute D K,et al.Efficient refolding of a hydrophobic protein with multiple S-S bonds by on-resin immobilized metal affinity chromatography.Journal of Chromatography A,2011,1218(31):5115-5119.
[24] Simpson R J.Purifying Proteins for Proteomics:A Laboratory Manual.New York:Cold Spring Harbor Laboratory Press,2004: 305,489-516.
[25] Antonio-Perez A,Ramon-Luing L A,Ortega-Lopez J.Chromatographic refolding of rhodanese and lysozyme assisted by the GroEL apical domain,DsbA and DsbC immobilized on cellulose.Journal of Chromatography A,2012,1248:122-129.
[26] Wang C Z,Geng X D.Refolding and purification of recombinant human granulocyte colony-stimulating factor using hydrophobic interaction chromatography at a large scale.Process Biochemistry,2012,47(12):2262-2266.
[27] Englander S W,Mayne L.The nature of protein folding pathways.Proceedings of the National Academy Sciences of the United States of America,2014,11(45):15873-15880.
[28] Chen Y C,Lin W Y,Wu K W,et al.Efficient lysozyme refolding at a high final concentration and a low dilution factor.Process Biochemistry,2012,47(12):1883-1888.
[29] Wang S S,Chang C K,Peng M J,et al.Effect of glutathione redox system on lysozyme refolding in size exclusion chromatography.Food and Bioproducts Processing,2006,84(1):18-27.
[30] Li M,Zhang G F,Su Z G.Dual gradient ion-exchange chromatography improved refolding yield of lysozyme.Journal of Chromatography A,2002,959(1-2):113-120.
[31] Li J J,Liu Y D,Wang F W,et al.Hydrophobic interaction chromatography correctly refolding proteins assisted by glycerol and urea gradients.Journal of Chromatography A,2004,1061(2):193-199.
[32] Dechavanne V,Barrillat N,Borlat F,et al. A high-throughput protein refolding screen in 96-well format combined with design of experiments to optimize the refolding conditions.Protein Expression and Purification,2011,75(2):192-203.
[33] Yamaguchi H,Miyazaki M. Refolding techniques for recovering biologically active recombinant proteins from inclusion bodies.Biomolecules.2014,4(1):235-251.
[34] Kuo M M,Nquyen P H,Jeon Y H,et al.MB109 as bioactive human bone morphogenetic protein-9 refolded and purified from E. coli inclusion bodies.Microbial Cell Factories.2014,13(1):29.
[35] Han G J,Dong X Y,Sun Y. Purification effect of artificial chaperone in the refolding of recombinant ribonuclease A from inclusion bodies.Biochemical Engineering Journal.2013,77:15-19.
[36] Kuboi R,Mawatari T,Yoshimoto M.Oxidative refolding of lysozyme assisted by negatively charged liposomes:relationship with lysozyme-mediated fusion of liposomes.Journal of Bioscience and Bioengineering.2000,90(1):14-19.
[37] Ishida H,Garcia-Herrero A,Vogel H J.The periplasmic domain of Escherichia coli outer membrane protein A can undergo a localized temperature dependent structural transition.Biochimiaca et Biophysica Acta.2014,1838(12):3014-3024.
[38] Xu J,Li J,Wu X,et al. Expression and refolding of bioactive α-bungarotoxin V31 in E. coli.Protein Expression and Purification.2015,doi:10.1016/j.pep.
[39] Niforou K,Cheimonidou C,Trougakos I P.Molecular chaperones and proteostasis regulation during redox imbalance.Redox Biology.2014,2:323-332.
[40] Tsumoto K,Ejima D,Kumagai I,et al.Practical considerations in refolding proteins from inclusion bodies.Protein Expression and Purification,2003,28(1):1-8.
[41] Chen Y,Leong S S.Adsorptive refolding of a highly disulfide-bonded inclusion body protein using anion-exchange chromatography.Journal of Chromatography A.2009,1216(24):4877-4886.
[42] 王静岩,朱胜庚,徐长法.生物化学.上册-3版.北京:高等教育出版社,2002:197-201. Wang J Y,Zhu S G,Xu C F.Biochemistry I.3rd ed.Beijing:Higher Education Press,2002:197-201.
[43] Denslow N D,Wingfield P T,Rose K. Overview of the characterization of recombinant proteins.Current Protocols in Protein Science,2001,doi:10.1002/0471140864.ps0701s00.
[44] Gull N,Mir M A,Khan J M,et al.Refolding of bovine serum albumin via artificial chaperone protocol using gemini surfactants.Journal of Colloid and Interface Science.2011,364(1):157-162.
[45] Chura-Chambi R M,Nakajima E,Carvalho R R,et al.Refolding of the recombinant protein Sm29,a step toward the production of the vaccine candidate against schistosomiasis.Journal of Biotechnology,2013,168(4):511-519.
[46] Linke T,Aspelund M T,Thompson C,et al. Development and scale-up of a commercial fed batch refolding process for an anti-CD22 two chain immunotoxin.Biotechnology Progress.2014,30(6):1380-1389.
[47] Ogura K,Kobashigawa Y,Saio T,et al.Practical applications of hydrostatic pressure to refold proteins from inclusion bodies for NMR structural studies.Protein Engineering,Design & Selection.2013,25(6):409-416.
[48] Barends T R,Foucar L,Botha S,et al. De novo protein crystal structure determination from X-ray free-electron laser data.Nature.2014,505(7482):244-247.
[49] Gallagher S R. One-dimensional electrophoresis using nondenaturing conditions.Current Protocols in Protein Science,2001,doi:10.1002/0471142727.mb1002bs47.
[50] Alsemgeest J,Old J M,Young L J.The macropod type 2 interferon gene shares important regulatory and functionally relevant regions with eutherian IFN-γ.Molecular Immunology,2015,63(2):297-304.
[51] Pizarro S A,Gunson J,Field M J,et al.High-yield expression of human vascular endothelial growth factor VEGF165 in Escherichia coli and purification for therapeutic applications.Protein Expression and Purification,2010,72(2):184-193.
[52] Coutard B,Danchin E G J,Oubelaid R,et al.Single pH buffer refolding screen for protein from inclusion bodies.Protein Expression and Purification.2012,82(2):352-359.
[53] Dechavanne V,Barrillat N,Borlat F,et al.A high-throughput protein refolding screen in 96-well format combined with design of experiments to optimiza the refolding conditions.Protein Expression and Purification.2011,75(2):192-203.
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