메뉴 건너뛰기




Volumn 41, Issue 10, 2014, Pages 6887-6898

Characterization of camel nanobodies specific for superfolder GFP fusion proteins

Author keywords

Camel; Fusion protein; Nanobody; Phage display; sfGFP

Indexed keywords

EPITOPE; NANOBODY; ANTIGEN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; IMMUNOGLOBULIN G; PEPTIDE LIBRARY;

EID: 84919327096     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-014-3575-x     Document Type: Article
Times cited : (18)

References (45)
  • 1
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • PID: 13911999, COI: 1:CAS:528:DyaF38XksFSrt7k%3D
    • Shimomura O, Johnson FH, Saiga Y (1962) Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J Cell Comp Physiol 59:223–239
    • (1962) J Cell Comp Physiol , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 2
    • 0030780644 scopus 로고    scopus 로고
    • High-titer retroviral vectors containing the enhanced green fluorescent protein gene for efficient expression in hematopoietic cells
    • PID: 9345013, COI: 1:CAS:528:DyaK2sXntVSjtr8%3D
    • Limon A, Briones J, Puig T, Carmona M, Fornas O, Cancelas JA, Nadal M, Garcia J, Rueda F, Barquinero J (1997) High-titer retroviral vectors containing the enhanced green fluorescent protein gene for efficient expression in hematopoietic cells. Blood 90(9):3316–3321
    • (1997) Blood , vol.90 , Issue.9 , pp. 3316-3321
    • Limon, A.1    Briones, J.2    Puig, T.3    Carmona, M.4    Fornas, O.5    Cancelas, J.A.6    Nadal, M.7    Garcia, J.8    Rueda, F.9    Barquinero, J.10
  • 3
    • 0026578325 scopus 로고
    • Primary structure of the Aequorea victoria green-fluorescent protein
    • PID: 1347277, COI: 1:CAS:528:DyaK3sXitVOktLw%3D
    • Prasher DC, Eckenrode VK, Ward WW, Prendergast FG, Cormier MJ (1992) Primary structure of the Aequorea victoria green-fluorescent protein. Gene 111(2):229–233
    • (1992) Gene , vol.111 , Issue.2 , pp. 229-233
    • Prasher, D.C.1    Eckenrode, V.K.2    Ward, W.W.3    Prendergast, F.G.4    Cormier, M.J.5
  • 4
    • 48649096305 scopus 로고    scopus 로고
    • Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control
    • PID: 18545653
    • Fisher AC, DeLisa MP (2008) Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control. PLoS One 3(6):e2351–e2357
    • (2008) PLoS One , vol.3 , Issue.6 , pp. e2351-e2357
    • Fisher, A.C.1    DeLisa, M.P.2
  • 5
    • 0036051316 scopus 로고    scopus 로고
    • The dynamic microbe: green fluorescent protein brings bacteria to light
    • PID: 12207688, COI: 1:CAS:528:DC%2BD38XntFGktLw%3D
    • Southward CM, Surette MG (2002) The dynamic microbe: green fluorescent protein brings bacteria to light. Mol Microbiol 45(5):1191–1196
    • (2002) Mol Microbiol , vol.45 , Issue.5 , pp. 1191-1196
    • Southward, C.M.1    Surette, M.G.2
  • 6
    • 40849120279 scopus 로고    scopus 로고
    • Purification of recombinant enhanced green fluorescent protein expressed in Escherichia coli with new immobilized metal ion affinity magnetic absorbents
    • PID: 18313994, COI: 1:CAS:528:DC%2BD1cXjtlCisrc%3D
    • Chiang CL, Chen CY, Chang LW (2008) Purification of recombinant enhanced green fluorescent protein expressed in Escherichia coli with new immobilized metal ion affinity magnetic absorbents. J Chromatogr B Analyt Technol Biomed Life Sci 864(1–2):116–122
    • (2008) J Chromatogr B Analyt Technol Biomed Life Sci , vol.864 , Issue.1-2 , pp. 116-122
    • Chiang, C.L.1    Chen, C.Y.2    Chang, L.W.3
  • 7
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • PID: 9630892, COI: 1:CAS:528:DyaK28XhsFOjsrg%3D
    • Crameri A, Whitehorn E, Tate E, Stemmer W (1996) Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat Biotechnol 14:315–319
    • (1996) Nat Biotechnol , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.2    Tate, E.3    Stemmer, W.4
  • 8
    • 67349215735 scopus 로고    scopus 로고
    • Immunological behavior of enhanced green fluorescent protein (EGFP) as a minor histocompatibility antigen with a special reference to skin isograft and specific regulation of local graft-versus-host reaction (GvHR)
    • PID: 19428557, COI: 1:CAS:528:DC%2BD1MXltlequrc%3D
    • Pan XC, Deng YB, Sugawara Y, Makuuchi M, Okabe M, Ochiya T, Sugiura W, Kitazawa Y, Fuji N, Li XK, Miyamoto M, Kimura H (2009) Immunological behavior of enhanced green fluorescent protein (EGFP) as a minor histocompatibility antigen with a special reference to skin isograft and specific regulation of local graft-versus-host reaction (GvHR). Immunol Lett 123(2):103–113
    • (2009) Immunol Lett , vol.123 , Issue.2 , pp. 103-113
    • Pan, X.C.1    Deng, Y.B.2    Sugawara, Y.3    Makuuchi, M.4    Okabe, M.5    Ochiya, T.6    Sugiura, W.7    Kitazawa, Y.8    Fuji, N.9    Li, X.K.10    Miyamoto, M.11    Kimura, H.12
  • 9
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • PID: 16369541, COI: 1:CAS:528:DC%2BD28XisVGluw%3D%3D
    • Pedelacq JD, Cabantous S, Tran T, Terwilliger TC, Waldo GS (2006) Engineering and characterization of a superfolder green fluorescent protein. Nat Biotechnol 24(1):79–88
    • (2006) Nat Biotechnol , vol.24 , Issue.1 , pp. 79-88
    • Pedelacq, J.D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 10
    • 34548816178 scopus 로고    scopus 로고
    • The rough energy landscape of superfolder GFP is linked to the chromophore
    • PID: 17822714, COI: 1:CAS:528:DC%2BD2sXhtFSks7%2FO
    • Andrews BT, Schoenfish AR, Roy M, Waldo G, Jennings PA (2007) The rough energy landscape of superfolder GFP is linked to the chromophore. J Mol Biol 373(2):476–490
    • (2007) J Mol Biol , vol.373 , Issue.2 , pp. 476-490
    • Andrews, B.T.1    Schoenfish, A.R.2    Roy, M.3    Waldo, G.4    Jennings, P.A.5
  • 11
    • 39749193861 scopus 로고    scopus 로고
    • A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins
    • PID: 17951627, COI: 1:CAS:528:DC%2BD1cXitlylsbc%3D
    • Rothbauer U, Zolghadr K, Muyldermans S, Schepers A, Cardoso MC, Leonhardt H (2008) A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteins. Mol Cell Proteomics 7(2):282–289
    • (2008) Mol Cell Proteomics , vol.7 , Issue.2 , pp. 282-289
    • Rothbauer, U.1    Zolghadr, K.2    Muyldermans, S.3    Schepers, A.4    Cardoso, M.C.5    Leonhardt, H.6
  • 14
    • 84934444785 scopus 로고    scopus 로고
    • Introduction to heavy chain antibodies and derived Nanobodies
    • PID: 22886243, COI: 1:CAS:528:DC%2BC38XhsFChtrbL
    • Vincke C, Muyldermans S (2012) Introduction to heavy chain antibodies and derived Nanobodies. Methods Mol Biol 911:15–26
    • (2012) Methods Mol Biol , vol.911 , pp. 15-26
    • Vincke, C.1    Muyldermans, S.2
  • 15
    • 67650480902 scopus 로고    scopus 로고
    • Nanobodies-the new concept in antibody engineering
    • COI: 1:CAS:528:DC%2BD1MXot1KjsL0%3D
    • Deffar K, Shi H, Li L, Wang X, Zhu X (2009) Nanobodies-the new concept in antibody engineering. Afr J Biotechnol 8(12):2645–2652
    • (2009) Afr J Biotechnol , vol.8 , Issue.12 , pp. 2645-2652
    • Deffar, K.1    Shi, H.2    Li, L.3    Wang, X.4    Zhu, X.5
  • 16
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • PID: 16151406, COI: 1:CAS:528:DC%2BD2MXpvVyrtrc%3D
    • Holliger P, Hudson PJ (2005) Engineered antibody fragments and the rise of single domains. Nat Biotechnol 23(9):1126–1136
    • (2005) Nat Biotechnol , vol.23 , Issue.9 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 17
    • 0033103453 scopus 로고    scopus 로고
    • Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies
    • PID: 10398404, COI: 1:CAS:528:DyaK1MXisF2jtrs%3D
    • Muyldermans S, Lauwereys M (1999) Unique single-domain antigen binding fragments derived from naturally occurring camel heavy-chain antibodies. J Mol Recognit 12(2):131–140
    • (1999) J Mol Recognit , vol.12 , Issue.2 , pp. 131-140
    • Muyldermans, S.1    Lauwereys, M.2
  • 21
    • 84887568733 scopus 로고    scopus 로고
    • Construction of pRSET-sfGFP plasmid for fusion-protein expression, purification and detection
    • COI: 1:CAS:528:DC%2BC2cXos1OmsL4%3D
    • Al-Homsi L, Al-Assad JM, Kweider M, Al-Okla S, Abbady AQ (2012) Construction of pRSET-sfGFP plasmid for fusion-protein expression, purification and detection. Jordan J Biol Sci 5(4):279–288
    • (2012) Jordan J Biol Sci , vol.5 , Issue.4 , pp. 279-288
    • Al-Homsi, L.1    Al-Assad, J.M.2    Kweider, M.3    Al-Okla, S.4    Abbady, A.Q.5
  • 22
    • 84897547362 scopus 로고    scopus 로고
    • Prokaryotic overexpression of TEV–rhGH and characterization of its polyclonal antibody
    • PID: 24534464, COI: 1:CAS:528:DC%2BC2cXksF2jtro%3D
    • Murad H, Ali B, Makeya R, Abbady AQ (2014) Prokaryotic overexpression of TEV–rhGH and characterization of its polyclonal antibody. Gene 542(1):69–76
    • (2014) Gene , vol.542 , Issue.1 , pp. 69-76
    • Murad, H.1    Ali, B.2    Makeya, R.3    Abbady, A.Q.4
  • 23
    • 79957937913 scopus 로고    scopus 로고
    • Evaluation of a nanobody phage display library constructed from a Brucella-immunised camel
    • PID: 21592585, COI: 1:CAS:528:DC%2BC3MXntlGhtLg%3D
    • Abbady AQ, Al-Mariri A, Zarkawi M, Al-Assad A, Muyldermans S (2011) Evaluation of a nanobody phage display library constructed from a Brucella-immunised camel. Vet Immunol Immunopathol 142(1–2):49–56
    • (2011) Vet Immunol Immunopathol , vol.142 , Issue.1-2 , pp. 49-56
    • Abbady, A.Q.1    Al-Mariri, A.2    Zarkawi, M.3    Al-Assad, A.4    Muyldermans, S.5
  • 24
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • PID: 9323027, COI: 1:CAS:528:DyaK2sXlvVKrs7k%3D
    • Arbabi Ghahroudi M, Desmyter A, Wyns L, Hamers R, Muyldermans S (1997) Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Lett 414(3):521–526
    • (1997) FEBS Lett , vol.414 , Issue.3 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 25
    • 0034161488 scopus 로고    scopus 로고
    • Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire
    • PID: 10698934, COI: 1:CAS:528:DC%2BD3cXitVyrsrw%3D
    • Nguyen VK, Hamers R, Wyns L, Muyldermans S (2000) Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire. EMBO J 19(5):921–930
    • (2000) EMBO J , vol.19 , Issue.5 , pp. 921-930
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 26
    • 40049094697 scopus 로고    scopus 로고
    • Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains
    • PID: 18262543, COI: 1:CAS:528:DC%2BD1cXjtVWlu7g%3D
    • Saerens D, Conrath K, Govaert J, Muyldermans S (2008) Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains. J Mol Biol 377(2):478–488
    • (2008) J Mol Biol , vol.377 , Issue.2 , pp. 478-488
    • Saerens, D.1    Conrath, K.2    Govaert, J.3    Muyldermans, S.4
  • 28
    • 72949123016 scopus 로고    scopus 로고
    • Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris
    • PID: 19861136, COI: 1:CAS:528:DC%2BC3cXptlSi
    • Ryckaert S, Pardon E, Steyaert J, Callewaert N (2010) Isolation of antigen-binding camelid heavy chain antibody fragments (nanobodies) from an immune library displayed on the surface of Pichia pastoris. J Biotechnol 145(2):93–98
    • (2010) J Biotechnol , vol.145 , Issue.2 , pp. 93-98
    • Ryckaert, S.1    Pardon, E.2    Steyaert, J.3    Callewaert, N.4
  • 30
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • PID: 15580262, COI: 1:CAS:528:DC%2BD2MXhsFGntw%3D%3D
    • Cabantous S, Terwilliger TC, Waldo GS (2005) Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat Biotechnol 23(1):102–107
    • (2005) Nat Biotechnol , vol.23 , Issue.1 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 31
    • 33749005086 scopus 로고    scopus 로고
    • In vivo and in vitro protein solubility assays using split GFP
    • PID: 16990817, COI: 1:CAS:528:DC%2BD28XpvVCmtb8%3D
    • Cabantous S, Waldo G (2006) In vivo and in vitro protein solubility assays using split GFP. Nat Methods 3:845–854
    • (2006) Nat Methods , vol.3 , pp. 845-854
    • Cabantous, S.1    Waldo, G.2
  • 32
    • 77749328366 scopus 로고    scopus 로고
    • A novel method for high-level production of TEV protease by superfolder GFP tag
    • 591923
    • Wu X, Wu D, Lu Z, Chen W, Hu X, Ding Y (2009) A novel method for high-level production of TEV protease by superfolder GFP tag. J Biomed Biotechnol 591923:1–8
    • (2009) J Biomed Biotechnol , pp. 1-8
    • Wu, X.1    Wu, D.2    Lu, Z.3    Chen, W.4    Hu, X.5    Ding, Y.6
  • 34
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • PID: 17704915, COI: 1:CAS:528:DC%2BD2sXhtFGgs7bO
    • Harmsen MM, De Haard HJ (2007) Properties, production, and applications of camelid single-domain antibody fragments. Appl Microbiol Biotechnol 77(1):13–22
    • (2007) Appl Microbiol Biotechnol , vol.77 , Issue.1 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 36
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
    • PID: 11295555, COI: 1:CAS:528:DC%2BD3MXisF2nt7c%3D
    • Muyldermans S, Cambillau C, Wyns L (2001) Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. Trends Biochem Sci 26(4):230–235
    • (2001) Trends Biochem Sci , vol.26 , Issue.4 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 37
    • 35648995435 scopus 로고    scopus 로고
    • Mapping the epitopes of antibodies
    • PID: 18059626, COI: 1:CAS:528:DC%2BD2sXhtlKiurjN
    • Ladner RC (2007) Mapping the epitopes of antibodies. Biotechnol Genet Eng Rev 24:1–30
    • (2007) Biotechnol Genet Eng Rev , vol.24 , pp. 1-30
    • Ladner, R.C.1
  • 38
    • 33646540098 scopus 로고    scopus 로고
    • Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ni-nitrilotriacetic acid surfaces
    • PID: 16642995, COI: 1:CAS:528:DC%2BD28XjtFWjurw%3D
    • Khan F, He M, Taussig MJ (2006) Double-hexahistidine tag with high-affinity binding for protein immobilization, purification, and detection on ni-nitrilotriacetic acid surfaces. Anal Chem 78(9):3072–3079
    • (2006) Anal Chem , vol.78 , Issue.9 , pp. 3072-3079
    • Khan, F.1    He, M.2    Taussig, M.J.3
  • 39
    • 0029718894 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins with the 6xHis tag and Ni-NTA resin
    • PID: 8713899, COI: 1:CAS:528:DyaK28Xit1CktLw%3D
    • Crowe J, Masone BS, Ribbe J (1996) One-step purification of recombinant proteins with the 6xHis tag and Ni-NTA resin. Methods Mol Biol 58:491–510
    • (1996) Methods Mol Biol , vol.58 , pp. 491-510
    • Crowe, J.1    Masone, B.S.2    Ribbe, J.3
  • 40
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • PID: 16427311, COI: 1:CAS:528:DC%2BD28XltFCntLc%3D
    • Arnau J, Lauritzen C, Petersen GE, Pedersen J (2006) Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr Purif 48(1):1–13
    • (2006) Protein Expr Purif , vol.48 , Issue.1 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4
  • 41
    • 0344395582 scopus 로고    scopus 로고
    • Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfusion chromatography
    • PID: 14642809, COI: 1:CAS:528:DC%2BD3sXpt1ersr4%3D
    • Verheesen P, ten Haaft MR, Lindner N, Verrips CT, de Haard JJ (2003) Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfusion chromatography. Biochim Biophys Acta 1624(1–3):21–28
    • (2003) Biochim Biophys Acta , vol.1624 , Issue.1-3 , pp. 21-28
    • Verheesen, P.1    ten Haaft, M.R.2    Lindner, N.3    Verrips, C.T.4    de Haard, J.J.5
  • 42
    • 54849403487 scopus 로고    scopus 로고
    • Single-domain antibodies as building blocks for novel therapeutics
    • PID: 18691671, COI: 1:CAS:528:DC%2BD1cXhtlaqsLvE
    • Saerens D, Ghassabeh GH, Muyldermans S (2008) Single-domain antibodies as building blocks for novel therapeutics. Curr Opin Pharmacol 8(5):600–608
    • (2008) Curr Opin Pharmacol , vol.8 , Issue.5 , pp. 600-608
    • Saerens, D.1    Ghassabeh, G.H.2    Muyldermans, S.3
  • 43
    • 78649644404 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of the GFP:GFP-nanobody complex
    • PID: 20945358, COI: 1:CAS:528:DC%2BC3cXhsFCntbbO
    • Kubala MH, Kovtun O, Alexandrov K, Collins BM (2010) Structural and thermodynamic analysis of the GFP:GFP-nanobody complex. Protein Sci 19(12):2389–2398
    • (2010) Protein Sci , vol.19 , Issue.12 , pp. 2389-2398
    • Kubala, M.H.1    Kovtun, O.2    Alexandrov, K.3    Collins, B.M.4
  • 44
    • 84855425542 scopus 로고    scopus 로고
    • Fluorescent fusion protein knockout mediated by anti-GFP nanobody
    • COI: 1:CAS:528:DC%2BC3MXhs1eisbbI
    • Caussinus E, Kanca O, Affolter M (2012) Fluorescent fusion protein knockout mediated by anti-GFP nanobody. Nat Struct Mol Biol 19(1):117–121
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.1 , pp. 117-121
    • Caussinus, E.1    Kanca, O.2    Affolter, M.3
  • 45
    • 84861979783 scopus 로고    scopus 로고
    • A simple, versatile method for GFP-based super-resolution microscopy via nanobodies
    • PID: 22543348, COI: 1:CAS:528:DC%2BC38Xmt1Gksbs%3D
    • Ries J, Kaplan C, Platonova E, Eghlidi H, Ewers H (2012) A simple, versatile method for GFP-based super-resolution microscopy via nanobodies. Nat Methods 9(6):582–584
    • (2012) Nat Methods , vol.9 , Issue.6 , pp. 582-584
    • Ries, J.1    Kaplan, C.2    Platonova, E.3    Eghlidi, H.4    Ewers, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.