메뉴 건너뛰기




Volumn 46, Issue 1, 2010, Pages 23-31

Overcoming the solubility limit with solubility-enhancement tags: Successful applications in biomolecular NMR studies

Author keywords

NMR; Protein; Protein aggregation; Protein GB1; Protein stability enhancement; Solubility enhancement tag

Indexed keywords

CALMODULIN; GLUTATHIONE TRANSFERASE; INITIATION FACTOR 4E; INITIATION FACTOR 5; KI 67 ANTIGEN; MYELIN BASIC PROTEIN; PARKIN; PRION PROTEIN; PROTEIN E6; STAPHYLOCOCCUS PROTEIN A; TAX PROTEIN; THIOREDOXIN; VAV PROTEIN;

EID: 77649176543     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9371-6     Document Type: Review
Times cited : (75)

References (58)
  • 1
    • 0035823143 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies
    • DOI 10.1006/jmbi.2001.4914
    • H Bach Y Mazor S Shaky A Shoham-Lev Y Berdichevsky DL Gutnick I Benhar 2001 Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies J Mol Biol 312 79 93 10.1006/jmbi.2001.4914 (Pubitemid 32835677)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.1 , pp. 79-93
    • Bach, H.1    Mazor, Y.2    Shaky, S.3    Shoham-Lev, A.4    Berdichevsky, Y.5    Gutnick, D.L.6    Benhar, I.7
  • 2
    • 0031243139 scopus 로고    scopus 로고
    • The button test: A small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR
    • 10.1023/A:1018359305544
    • S Bagby KI Tong D Liu JR Alattia M Ikura 1997 The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR J Biomol NMR 10 279 282 10.1023/A:1018359305544
    • (1997) J Biomol NMR , vol.10 , pp. 279-282
    • Bagby, S.1    Tong, K.I.2    Liu, D.3    Alattia, J.R.4    Ikura, M.5
  • 4
    • 33744461058 scopus 로고    scopus 로고
    • Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin
    • DOI 10.1110/ps.051995006
    • YG Chang AX Song YG Gao YH Shi XJ Lin XT Cao DH Lin HY Hu 2006 Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin Protein Sci 15 1248 1259 10.1110/ps.051995006 (Pubitemid 43799998)
    • (2006) Protein Science , vol.15 , Issue.6 , pp. 1248-1259
    • Chang, Y.-G.1    Song, A.-X.2    Gao, Y.-G.3    Shi, Y.-H.4    Lin, X.-J.5    Cao, X.-T.6    Lin, D.-H.7    Hu, H.-Y.8
  • 5
    • 1842426648 scopus 로고    scopus 로고
    • An efficient system for small protein expression and refolding
    • DOI 10.1016/j.bbrc.2004.03.068, PII S0006291X04005601
    • Y Cheng DJ Patel 2004 An efficient system for small protein expression and refolding Biochem Biophys Res Commun 317 401 405 10.1016/j.bbrc.2004.03.068 (Pubitemid 38452497)
    • (2004) Biochemical and Biophysical Research Communications , vol.317 , Issue.2 , pp. 401-405
    • Cheng, Y.1    Patel, D.J.2
  • 7
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • DOI 10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.0.CO;2-I
    • GD Davis C Elisee DM Newham RG Harrison 1999 New fusion protein systems designed to give soluble expression in Escherichia coli Biotechnol Bioeng 65 382 388 10.1002/(SICI)1097-0290(19991120)65:4<382::AID-BIT2>3.0.CO;2-I (Pubitemid 29482993)
    • (1999) Biotechnology and Bioengineering , vol.65 , Issue.4 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Mewham, D.M.3    Harrison, R.G.4
  • 8
    • 84954358425 scopus 로고    scopus 로고
    • Mocr: A novel fusion tag for enhancing solubility that is compatible with structural biology applications
    • 10.1016/j.pep.2008.08.011
    • J DelProposto CY Majmudar JL Smith WC Brown 2009 Mocr: a novel fusion tag for enhancing solubility that is compatible with structural biology applications Protein Expr Purif 63 40 49 10.1016/j.pep.2008.08.011
    • (2009) Protein Expr Purif , vol.63 , pp. 40-49
    • Delproposto, J.1    Majmudar, C.Y.2    Smith, J.L.3    Brown, W.C.4
  • 10
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • DOI 10.1016/0378-1119(88)90004-2
    • C di Guan P Li PD Riggs H Inouye 1988 Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein Gene 67 21 30 10.1016/0378-1119(88)90004-2 (Pubitemid 18178777)
    • (1988) Gene , vol.67 , Issue.1 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 12
    • 34548050438 scopus 로고    scopus 로고
    • Biophysical and cell-based evidence for differential interactions between the death domains of CD95/Fas and FADD [3]
    • DOI 10.1038/sj.cdd.4402191, PII 4402191
    • BJ Ferguson D Esposito J Jovanovic A Sankar PC Driscoll H Mehmet 2007 Biophysical and cell-based evidence for differential interactions between the death domains of CD95/Fas and FADD Cell Death Differ 14 1717 1719 10.1038/sj.cdd.4402191 (Pubitemid 47278858)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.9 , pp. 1717-1719
    • Ferguson, B.J.1    Esposito, D.2    Jovanovic, J.3    Sankar, A.4    Driscoll, P.C.5    Mehmet, H.6
  • 13
    • 0032509329 scopus 로고    scopus 로고
    • High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage Lambda head protein D
    • DOI 10.1016/S0378-1119(98)00538-1, PII S0378111998005381
    • P Forrer R Jaussi 1998 High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D Gene 224 45 52 10.1016/S0378-1119(98)00538-1 (Pubitemid 29023539)
    • (1998) Gene , vol.224 , Issue.1-2 , pp. 45-52
    • Forrer, P.1    Jaussi, R.2
  • 15
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • DOI 10.1110/ps.22102
    • M Hammarström N Hellgren S van Den Berg H Berglund T Hard 2002 Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli Protein Sci 11 313 321 10.1110/ps.22102 (Pubitemid 34075794)
    • (2002) Protein Science , vol.11 , Issue.2 , pp. 313-321
    • Hammarstrom, M.1    Hellgren, N.2    Van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 18
    • 0141817846 scopus 로고    scopus 로고
    • NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain
    • DOI 10.1016/j.str.2003.08.009
    • S Hiller A Kohl F Fiorito T Herrmann G Wider J Tschopp MG Grutter K Wuthrich 2003 NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain Structure 11 1199 1205 10.1016/j.str.2003.08.009 (Pubitemid 37214882)
    • (2003) Structure , vol.11 , Issue.10 , pp. 1199-1205
    • Hiller, S.1    Kohl, A.2    Fiorito, F.3    Herrmann, T.4    Wider, G.5    Tschopp, J.6    Grutter, M.G.7    Wuthrich, K.8
  • 19
    • 63049099537 scopus 로고    scopus 로고
    • Prion protein library of recombinant constructs for structural biology
    • 10.1111/j.1742-4658.2009.06968.x
    • S Hornemann B Christen C von Schroetter DR Perez K Wüthrich 2009 Prion protein library of recombinant constructs for structural biology FEBS J 276 2359 2367 10.1111/j.1742-4658.2009.06968.x
    • (2009) FEBS J , vol.276 , pp. 2359-2367
    • Hornemann, S.1    Christen, B.2    Von Schroetter, C.3    Perez, D.R.4    Wüthrich, K.5
  • 20
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
    • DOI 10.1038/384638a0
    • B Huang M Eberstadt ET Olejniczak RP Meadows SW Fesik 1996 NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain Nature 384 638 641 10.1038/384638a0 1996Natur.384..638H (Pubitemid 27021516)
    • (1996) Nature , vol.384 , Issue.6610 , pp. 638-641
    • Huang, B.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Feslk, S.W.5
  • 21
    • 0030691041 scopus 로고    scopus 로고
    • Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
    • 10.1002/pro.5560061109
    • JR Huth CA Bewley BM Jackson AG Hinnebusch GM Clore AM Gronenborn 1997 Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR Protein Sci 6 2359 2364 10.1002/pro. 5560061109
    • (1997) Protein Sci , vol.6 , pp. 2359-2364
    • Huth, J.R.1    Bewley, C.A.2    Jackson, B.M.3    Hinnebusch, A.G.4    Clore, G.M.5    Gronenborn, A.M.6
  • 22
    • 1442306652 scopus 로고    scopus 로고
    • Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2α
    • DOI 10.1023/B:JNMR.0000015405.62261.cb
    • T Ito G Wagner 2004 Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2 alpha J Biomol NMR 28 357 367 10.1023/B:JNMR.0000015405.62261.cb (Pubitemid 38268166)
    • (2004) Journal of Biomolecular NMR , vol.28 , Issue.4 , pp. 357-367
    • Ito, T.1    Wagner, G.2
  • 23
    • 4444333127 scopus 로고    scopus 로고
    • Solution structure of human initiation factor eIF2α reveals homology to the elongation factor eEF1B
    • DOI 10.1016/j.str.2004.07.010, PII S0969212604002795
    • T Ito A Marintchev G Wagner 2004 Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B Structure 12 1693 1704 10.1016/j.str.2004.07.010 (Pubitemid 39200521)
    • (2004) Structure , vol.12 , Issue.9 , pp. 1693-1704
    • Ito, T.1    Marintchev, A.2    Wagner, G.3
  • 24
    • 33947716280 scopus 로고    scopus 로고
    • Identification of residues participating in the interaction between an intraluminal loop of inositol 1, 4, 5-trisphosphate receptor and a conserved N-terminal region of chromogranin B
    • J Kang S Kang SH Yoo S Park 2007 Identification of residues participating in the interaction between an intraluminal loop of inositol 1, 4, 5-trisphosphate receptor and a conserved N-terminal region of chromogranin B Biochim Biophys Acta 1774 502 509
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 502-509
    • Kang, J.1    Kang, S.2    Yoo, S.H.3    Park, S.4
  • 25
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • 10.1110/ps.8.8.1668
    • RB Kapust DS Waugh 1999 Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci 8 1668 1674 10.1110/ps.8.8.1668
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 26
    • 33846539316 scopus 로고    scopus 로고
    • Mutational analysis of protein solubility enhancement using short peptide tags
    • DOI 10.1002/bip.20596
    • A Kato K Maki T Ebina K Kuwajima K Soda Y Kuroda 2007 Mutational analysis of protein solubility enhancement using short peptide tags Biopolymers 85 12 18 10.1002/bip.20596 (Pubitemid 46154815)
    • (2007) Biopolymers , vol.85 , Issue.1 , pp. 12-18
    • Kato, A.1    Maki, K.2    Ebina, T.3    Kuwajima, K.4    Soda, K.5    Kuroda, Y.6
  • 27
    • 0038245262 scopus 로고    scopus 로고
    • Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
    • DOI 10.1042/BJ20030093
    • R Kern A Malki A Holmgren G Richarme 2003 Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase Biochem J 371 965 972 10.1042/BJ20030093 (Pubitemid 36578895)
    • (2003) Biochemical Journal , vol.371 , Issue.3 , pp. 965-972
    • Kern, R.1    Malki, A.2    Holmgren, A.3    Richarme, G.4
  • 28
    • 61549135769 scopus 로고    scopus 로고
    • Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method
    • 10.1007/s10858-008-9296-5
    • Y Kobashigawa H Kumeta K Ogura F Inagaki 2009 Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method J Biomol NMR 43 145 150 10.1007/s10858-008-9296-5
    • (2009) J Biomol NMR , vol.43 , pp. 145-150
    • Kobashigawa, Y.1    Kumeta, H.2    Ogura, K.3    Inagaki, F.4
  • 29
    • 0011962568 scopus 로고    scopus 로고
    • Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
    • 10.1016/S0076-6879(00)26063-1
    • ER LaVallie Z Lu EA Diblasio-Smith LA Collins-Racie JM McCoy 2000 Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli Methods Enzymol 326 322 340 10.1016/S0076-6879(00)26063-1
    • (2000) Methods Enzymol , vol.326 , pp. 322-340
    • Lavallie, E.R.1    Lu, Z.2    Diblasio-Smith, E.A.3    Collins-Racie, L.A.4    McCoy, J.M.5
  • 30
    • 0032201444 scopus 로고    scopus 로고
    • Microdrop screening: A rapid method to optimize solvent conditions for NMR spectroscopy of proteins
    • 10.1023/A:1008353000679
    • CA Lepre JM Moore 1998 Microdrop screening: a rapid method to optimize solvent conditions for NMR spectroscopy of proteins J Biomol NMR 12 493 499 10.1023/A:1008353000679
    • (1998) J Biomol NMR , vol.12 , pp. 493-499
    • Lepre, C.A.1    Moore, J.M.2
  • 31
    • 0037984597 scopus 로고    scopus 로고
    • Direct binding of the N-terminus of HTLV-1 tax oncoprotein to cyclin-dependent kinase 4 is a dominant path to stimulate the kinase activity
    • DOI 10.1021/bi034369n
    • J Li H Li MD Tsai 2003 Direct binding of the N-terminus of HTLV-1 tax oncoprotein to cyclin-dependent kinase 4 is a dominant path to stimulate the kinase activity Biochemistry 42 6921 6928 10.1021/bi034369n (Pubitemid 36666133)
    • (2003) Biochemistry , vol.42 , Issue.22 , pp. 6921-6928
    • Li, J.1    Li, H.2    Tsai, M.-D.3
  • 32
    • 0344255640 scopus 로고    scopus 로고
    • Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions
    • DOI 10.1016/j.jmb.2003.10.032
    • H Li IJ Byeon Y Ju MD Tsai 2004 Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions J Mol Biol 335 371 381 10.1016/j.jmb.2003.10.032 (Pubitemid 37494986)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.1 , pp. 371-381
    • Li, H.1    Byeon, I.-J.L.2    Ju, Y.3    Tsai, M.-D.4
  • 33
    • 60149089457 scopus 로고    scopus 로고
    • Determinants of stability for the E6 protein of papillomavirus type 16
    • 10.1016/j.jmb.2009.01.018
    • Y Liu JJ Cherry JV Dineen EJ Androphy JD Baleja 2009 Determinants of stability for the E6 protein of papillomavirus type 16 J Mol Biol 386 1123 1137 10.1016/j.jmb.2009.01.018
    • (2009) J Mol Biol , vol.386 , pp. 1123-1137
    • Liu, Y.1    Cherry, J.J.2    Dineen, J.V.3    Androphy, E.J.4    Baleja, J.D.5
  • 34
    • 54849432001 scopus 로고    scopus 로고
    • Evaluation of solvent accessibility epitopes for different dehydrogenase inhibitors
    • C Ludwig PJ Michiels A Lodi J Ride C Bunce UL Gunther 2008 Evaluation of solvent accessibility epitopes for different dehydrogenase inhibitors Chem Med Chem 3 1371 1376
    • (2008) Chem Med Chem , vol.3 , pp. 1371-1376
    • Ludwig, C.1    Michiels, P.J.2    Lodi, A.3    Ride, J.4    Bunce, C.5    Gunther, U.L.6
  • 35
    • 34547557341 scopus 로고    scopus 로고
    • Functional silencing of TATA-binding protein (TBP) by a covalent linkage of the N-terminal domain of TBP-associated factor
    • DOI 10.1074/jbc.M702988200
    • TK Mal S Takahata S Ki L Zheng T Kokubo M Ikura 2007 Functional silencing of TATA-binding protein (TBP) by a covalent linkage of the N-terminal domain of TBP-associated factor 1 J Biol Chem 282 22228 22238 10.1074/jbc.M702988200 (Pubitemid 47195744)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.30 , pp. 22228-22238
    • Mal, T.K.1    Takahata, S.2    Ki, S.3    Zheng, L.4    Kokubo, T.5    Ikura, M.6
  • 38
    • 0030131709 scopus 로고    scopus 로고
    • High-level expression and efficient recovery of ubiquitin fusion proteins from Escherichia coli
    • 10.1021/bp9600187
    • AL Pilon P Yost TE Chase GL Lohnas WE Bentley 1996 High-level expression and efficient recovery of ubiquitin fusion proteins from Escherichia coli Biotechnol Prog 12 331 337 10.1021/bp9600187
    • (1996) Biotechnol Prog , vol.12 , pp. 331-337
    • Pilon, A.L.1    Yost, P.2    Chase, T.E.3    Lohnas, G.L.4    Bentley, W.E.5
  • 39
    • 38149140938 scopus 로고    scopus 로고
    • Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection
    • 10.1074/jbc.M708155200
    • M Reibarkh Y Yamamoto CR Singh F del Rio A Fahmy B Lee RE Luna M Ii G Wagner K Asano 2008 Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection J Biol Chem 283 1094 1103 10.1074/jbc.M708155200
    • (2008) J Biol Chem , vol.283 , pp. 1094-1103
    • Reibarkh, M.1    Yamamoto, Y.2    Singh, C.R.3    Del Rio, F.4    Fahmy, A.5    Lee, B.6    Luna, R.E.7    Ii, M.8    Wagner, G.9    Asano, K.10
  • 40
    • 37049004798 scopus 로고    scopus 로고
    • A disease state mutation unfolds the parkin ubiquitin-like domain
    • DOI 10.1021/bi7016969
    • SS Safadi GS Shaw 2007 A disease state mutation unfolds the parkin ubiquitin-like domain Biochemistry 46 14162 14169 10.1021/bi7016969 (Pubitemid 350250310)
    • (2007) Biochemistry , vol.46 , Issue.49 , pp. 14162-14169
    • Safadi, S.S.1    Shaw, G.S.2
  • 41
    • 0028314030 scopus 로고
    • Enhanced in vitro refolding of insulin-like growth factor i using a solubilizing fusion partner
    • 10.1021/bi00180a013
    • E Samuelsson T Moks B Nilsson M Uhlen 1994 Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner Biochemistry 33 4207 4211 10.1021/bi00180a013
    • (1994) Biochemistry , vol.33 , pp. 4207-4211
    • Samuelsson, E.1    Moks, T.2    Nilsson, B.3    Uhlen, M.4
  • 42
    • 49649104057 scopus 로고    scopus 로고
    • NMR analysis of KChIP4a reveals structural basis for control of surface expression of Kv4 channel complexes
    • 10.1074/jbc.M800976200
    • J Schwenk G Zolles NG Kandias I Neubauer H Kalbacher M Covarrubias B Fakler D Bentrop 2008 NMR analysis of KChIP4a reveals structural basis for control of surface expression of Kv4 channel complexes J Biol Chem 283 18937 18946 10.1074/jbc.M800976200
    • (2008) J Biol Chem , vol.283 , pp. 18937-18946
    • Schwenk, J.1    Zolles, G.2    Kandias, N.G.3    Neubauer, I.4    Kalbacher, H.5    Covarrubias, M.6    Fakler, B.7    Bentrop, D.8
  • 44
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • DOI 10.1016/0378-1119(88)90005-4
    • DB Smith KS Johnson 1988 Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase Gene 67 31 40 10.1016/0378-1119(88)90005-4 (Pubitemid 18178778)
    • (1988) Gene , vol.67 , Issue.1 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 45
    • 22444447868 scopus 로고    scopus 로고
    • Letter to the Editor: Resonance assignments of the double-stranded RNA-binding of adenosine deaminase acting on RNA 2 (ADAR2) [5]
    • DOI 10.1007/s10858-004-6058-x
    • R Stefl L Skrisovska M Xu RB Emeson FH Allain 2005 Resonance assignments of the double-stranded RNA-binding domains of adenosine deaminase acting on RNA 2 (ADAR2) J Biomol NMR 31 71 72 10.1007/s10858-004-6058-x (Pubitemid 40796356)
    • (2005) Journal of Biomolecular NMR , vol.31 , Issue.1 , pp. 71-72
    • Stefl, R.1    Skrisovska, L.2    Xu, M.3    Emeson, R.B.4    Allain, F.H.-T.5
  • 46
    • 32044468729 scopus 로고    scopus 로고
    • Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs
    • DOI 10.1016/j.str.2005.11.013, PII S096921260600044X
    • R Stefl M Xu L Skrisovska RB Emeson FH Allain 2006 Structure and specific RNA binding of ADAR2 double-stranded RNA binding motifs Structure 14 345 355 10.1016/j.str.2005.11.013 (Pubitemid 43202023)
    • (2006) Structure , vol.14 , Issue.2 , pp. 345-355
    • Stefl, R.1    Xu, M.2    Skrisovska, L.3    Emeson, R.B.4    Allain, F.H.-T.5
  • 47
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: An in vivo role reversal for the thioredoxins
    • DOI 10.1093/emboj/17.19.5543
    • EJ Stewart F Aslund J Beckwith 1998 Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins EMBO J 17 5543 5550 10.1093/emboj/17.19.5543 (Pubitemid 28445966)
    • (1998) EMBO Journal , vol.17 , Issue.19 , pp. 5543-5550
    • Stewart, E.J.1    Aslund, F.2    Beckwith, J.3
  • 48
    • 0344223475 scopus 로고    scopus 로고
    • Functional glycan-free adhesion domain of human cell surface receptor CD58: Design, production and NMR studies
    • DOI 10.1093/emboj/18.11.2941
    • ZY Sun V Dötsch M Kim J Li EL Reinherz G Wagner 1999 Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies EMBO J 18 2941 2949 10.1093/emboj/18.11.2941 (Pubitemid 29255603)
    • (1999) EMBO Journal , vol.18 , Issue.11 , pp. 2941-2949
    • Sun, Z.-Y.J.1    Dotsch, V.2    Kim, M.3    Li, J.4    Reinherz, E.L.5    Wagner, G.6
  • 49
    • 0035967867 scopus 로고    scopus 로고
    • Mechanisms contributing to T cell receptor signaling and assembly revealed by the solution structure of an ectodomain fragment of the CD3εγ heterodimer
    • DOI 10.1016/S0092-8674(01)00395-6
    • ZJ Sun KS Kim G Wagner EL Reinherz 2001 Mechanisms contributing to T cell receptor signaling and assembly revealed by the solution structure of an ectodomain fragment of the CD3 epsilon gamma heterodimer Cell 105 913 923 10.1016/S0092-8674(01)00395-6 (Pubitemid 32635092)
    • (2001) Cell , vol.105 , Issue.7 , pp. 913-923
    • Sun, Z.-Y.J.1    Kim, K.S.2    Wagner, G.3    Reinherz, E.L.4
  • 50
    • 0037031551 scopus 로고    scopus 로고
    • 3 "inside-out" activation as regulated by its cytoplasmic face
    • DOI 10.1016/S0092-8674(02)00906-6
    • O Vinogradova A Velyvis A Velyviene B Hu T Haas E Plow J Qin 2002 A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face Cell 110 587 597 10.1016/S0092-8674(02)00906-6 (Pubitemid 35247839)
    • (2002) Cell , vol.110 , Issue.5 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5    Plow, E.F.6    Qin, J.7
  • 51
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • DOI 10.1016/j.tibtech.2005.03.012, PII S0167779905000843
    • DS Waugh 2005 Making the most of affinity tags Trends Biotechnol 23 316 320 10.1016/j.tibtech.2005.03.012 (Pubitemid 40726273)
    • (2005) Trends in Biotechnology , vol.23 , Issue.6 , pp. 316-320
    • Waugh, D.S.1
  • 52
    • 14744278850 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • 10.1038/nbt0591-443
    • DL Wilkinson RG Harrison 1991 Predicting the solubility of recombinant proteins in Escherichia coli Bio/technology (Nature Publishing Company) 9 443 448 10.1038/nbt0591-443
    • (1991) Bio/technology (Nature Publishing Company) , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 54
    • 0034987544 scopus 로고    scopus 로고
    • A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins
    • DOI 10.1023/A:1011258906244
    • P Zhou AA Lugovskoy G Wagner 2001 A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins J Biomol NMR 20 11 14 10.1023/A:1011258906244 (Pubitemid 32519649)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.1 , pp. 11-14
    • Zhou, P.1    Lugovskoy, A.A.2    Wagner, G.3
  • 55
    • 64349120856 scopus 로고    scopus 로고
    • Effects of full-length Borealin on the composition and protein-protein interaction activity of a binary chromosomal passenger complex
    • 10.1021/bi801298j
    • L Zhou J Li R George S Ruchaud HG Zhou JE Ladbury WC Earnshaw X Yuan 2009 Effects of full-length Borealin on the composition and protein-protein interaction activity of a binary chromosomal passenger complex Biochemistry 48 1156 1161 10.1021/bi801298j
    • (2009) Biochemistry , vol.48 , pp. 1156-1161
    • Zhou, L.1    Li, J.2    George, R.3    Ruchaud, S.4    Zhou, H.G.5    Ladbury, J.E.6    Earnshaw, W.C.7    Yuan, X.8
  • 56
    • 47249104180 scopus 로고    scopus 로고
    • Hyper-acidic protein fusion partners improve solubility and assist correct folding of recombinant proteins expressed in Escherichia coli
    • 10.1016/j.jbiotec.2008.05.007
    • Z Zou L Cao P Zhou Y Su Y Sun W Li 2008 Hyper-acidic protein fusion partners improve solubility and assist correct folding of recombinant proteins expressed in Escherichia coli J Biotechnol 135 333 339 10.1016/j.jbiotec.2008. 05.007
    • (2008) J Biotechnol , vol.135 , pp. 333-339
    • Zou, Z.1    Cao, L.2    Zhou, P.3    Su, Y.4    Sun, Y.5    Li, W.6
  • 57
    • 24944448735 scopus 로고    scopus 로고
    • Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies
    • DOI 10.1038/nbt1097
    • S Züger H Iwai 2005 Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies Nat Biotechnol 23 736 740 10.1038/nbt1097 (Pubitemid 41716365)
    • (2005) Nature Biotechnology , vol.23 , Issue.6 , pp. 736-740
    • Zuger, S.1    Iwai, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.