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Volumn 11, Issue 3, 2016, Pages 399-414

Inactivation of GDP-fucose transporter gene (Slc35c1) in CHO cells by ZFNs, TALENs and CRISPR-Cas9 for production of fucose-free antibodies

Author keywords

Chinese hamster ovary (CHO) cells; Fluorescence activated cell sorting (FACS); Fucose free antibodies; GDP fucose transporter gene (Slc35c1); Genome editing technologies

Indexed keywords

CELLS; CYTOLOGY; CYTOTOXICITY; FLOW CYTOMETRY; GENES; MASS SPECTROMETRY;

EID: 84959236890     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201500331     Document Type: Article
Times cited : (60)

References (60)
  • 1
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcgamma receptor in complex with Fc
    • Radaev, S., Motyka, S., Fridman, W. H., Sautes-Fridman, C., Sun, P. D., The structure of a human type III Fcgamma receptor in complex with Fc. J. Biol. Chem. 2001, 276, 16469-16477.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 2
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • Sondermann, P., Huber, R., Oosthuizen, V., Jacob, U., The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 2000, 406, 267-273.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 3
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp, S., Mimura, Y., Jefferis, R., Huber, R., Sondermann, P., Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 2003, 325, 979-989.
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 4
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y. et al., Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 2002, 277, 26733-26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4
  • 5
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E. et al., The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 2003, 278, 3466-3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4
  • 6
    • 66149161776 scopus 로고    scopus 로고
    • In vitro and in vivo characterization of MDX-1401 for therapy of malignant lymphoma
    • Cardarelli, P. M., Moldovan-Loomis, M. C., Preston, B., Black, A. et al., In vitro and in vivo characterization of MDX-1401 for therapy of malignant lymphoma. Clin. Cancer Res. 2009, 15, 3376-3383.
    • (2009) Clin. Cancer Res. , vol.15 , pp. 3376-3383
    • Cardarelli, P.M.1    Moldovan-Loomis, M.C.2    Preston, B.3    Black, A.4
  • 7
    • 77953141926 scopus 로고    scopus 로고
    • Superior in vivo efficacy of afucosylated trastuzumab in the treatment of HER2-amplified breast cancer
    • Junttila, T. T., Parsons, K., Olsson, C., Lu, Y. et al., Superior in vivo efficacy of afucosylated trastuzumab in the treatment of HER2-amplified breast cancer. Cancer Res. 2010, 70, 4481-4489.
    • (2010) Cancer Res. , vol.70 , pp. 4481-4489
    • Junttila, T.T.1    Parsons, K.2    Olsson, C.3    Lu, Y.4
  • 8
    • 4644245701 scopus 로고    scopus 로고
    • Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 Is independent of FcgammaRIIIa functional polymorphism
    • Niwa, R., Hatanaka, S., Shoji-Hosaka, E., Sakurada, M. et al., Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 Is independent of FcgammaRIIIa functional polymorphism. Clin. Cancer Res. 2004, 10, 6248-6255.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6248-6255
    • Niwa, R.1    Hatanaka, S.2    Shoji-Hosaka, E.3    Sakurada, M.4
  • 9
    • 34247854443 scopus 로고    scopus 로고
    • A nonfucosylated anti-HER2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients
    • Suzuki, E., Niwa, R., Saji, S., Muta, M. et al., A nonfucosylated anti-HER2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients. Clin. Cancer Res. 2007, 13, 1875-1882.
    • (2007) Clin. Cancer Res. , vol.13 , pp. 1875-1882
    • Suzuki, E.1    Niwa, R.2    Saji, S.3    Muta, M.4
  • 10
  • 11
    • 0032486278 scopus 로고    scopus 로고
    • Molecular cloning and expression of GDP-D-mannose-4,6-dehydratase, a key enzyme for fucose metabolism defective in Lec13 cells
    • Ohyama, C., Smith, P. L., Angata, K., Fukuda, M. N. et al., Molecular cloning and expression of GDP-D-mannose-4, 6-dehydratase, a key enzyme for fucose metabolism defective in Lec13 cells. J. Biol. Chem. 1998, 273, 14582-14587.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14582-14587
    • Ohyama, C.1    Smith, P.L.2    Angata, K.3    Fukuda, M.N.4
  • 12
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • Becker, D. J., Lowe, J. B., Fucose: Biosynthesis and biological function in mammals. Glycobiology 2003, 13, 41R-53R..
    • (2003) Glycobiology , vol.13 , pp. 41R-53R
    • Becker, D.J.1    Lowe, J.B.2
  • 13
    • 4644245850 scopus 로고    scopus 로고
    • Establishment of FUT8 knockout Chinese hamster ovary cells: An ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity
    • Yamane-Ohnuki, N., Kinoshita, S., Inoue-Urakubo, M., Kusunoki, M. et al., Establishment of FUT8 knockout Chinese hamster ovary cells: An ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol. Bioeng. 2004, 87, 614-622.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 614-622
    • Yamane-Ohnuki, N.1    Kinoshita, S.2    Inoue-Urakubo, M.3    Kusunoki, M.4
  • 14
    • 77955390706 scopus 로고    scopus 로고
    • Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies
    • Malphettes, L., Freyvert, Y., Chang, J., Liu, P. Q. et al., Highly efficient deletion of FUT8 in CHO cell lines using zinc-finger nucleases yields cells that produce completely nonfucosylated antibodies. Biotechnol. Bioeng. 2010, 106, 774-783.
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 774-783
    • Malphettes, L.1    Freyvert, Y.2    Chang, J.3    Liu, P.Q.4
  • 15
    • 78149251654 scopus 로고    scopus 로고
    • Slc35c2 promotes Notch1 fucosylation and is required for optimal Notch signaling in mammalian cells
    • Lu, L., Hou, X., Shi, S., Korner, C., Stanley, P., Slc35c2 promotes Notch1 fucosylation and is required for optimal Notch signaling in mammalian cells. J. Biol. Chem. 2010, 285, 36245-36254.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36245-36254
    • Lu, L.1    Hou, X.2    Shi, S.3    Korner, C.4    Stanley, P.5
  • 16
    • 0035036072 scopus 로고    scopus 로고
    • Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency
    • Lubke, T., Marquardt, T., Etzioni, A., Hartmann, E. et al., Complementation cloning identifies CDG-IIc, a new type of congenital disorders of glycosylation, as a GDP-fucose transporter deficiency. Nat. Genet. 2001, 28, 73-76.
    • (2001) Nat. Genet. , vol.28 , pp. 73-76
    • Lubke, T.1    Marquardt, T.2    Etzioni, A.3    Hartmann, E.4
  • 17
    • 0035036832 scopus 로고    scopus 로고
    • The gene defective in leukocyte adhesion deficiency II encodes a putative GDP-fucose transporter
    • Luhn, K., Wild, M. K., Eckhardt, M., Gerardy-Schahn, R., Vestweber, D., The gene defective in leukocyte adhesion deficiency II encodes a putative GDP-fucose transporter. Nat. Genet. 2001, 28, 69-72.
    • (2001) Nat. Genet. , vol.28 , pp. 69-72
    • Luhn, K.1    Wild, M.K.2    Eckhardt, M.3    Gerardy-Schahn, R.4    Vestweber, D.5
  • 18
    • 44949155482 scopus 로고    scopus 로고
    • Heritable targeted gene disruption in zebrafish using designed zinc-finger nucleases
    • Doyon, Y., McCammon, J. M., Miller, J. C., Faraji, F. et al., Heritable targeted gene disruption in zebrafish using designed zinc-finger nucleases. Nat. Biotechnol. 2008, 26, 702-708.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 702-708
    • Doyon, Y.1    McCammon, J.M.2    Miller, J.C.3    Faraji, F.4
  • 19
    • 34447319080 scopus 로고    scopus 로고
    • An improved zinc-finger nuclease architecture for highly specific genome editing
    • Miller, J. C., Holmes, M. C., Wang, J., Guschin, D. Y. et al., An improved zinc-finger nuclease architecture for highly specific genome editing. Nat. Biotechnol. 2007, 25, 778-785.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 778-785
    • Miller, J.C.1    Holmes, M.C.2    Wang, J.3    Guschin, D.Y.4
  • 20
    • 18944373328 scopus 로고    scopus 로고
    • Highly efficient endogenous human gene correction using designed zinc-finger nucleases
    • Urnov, F. D., Miller, J. C., Lee, Y. L., Beausejour, C. M. et al., Highly efficient endogenous human gene correction using designed zinc-finger nucleases. Nature 2005, 435, 646-651.
    • (2005) Nature , vol.435 , pp. 646-651
    • Urnov, F.D.1    Miller, J.C.2    Lee, Y.L.3    Beausejour, C.M.4
  • 21
    • 78951479577 scopus 로고    scopus 로고
    • Targeting DNA double-strand breaks with TAL effector nucleases
    • Christian, M., Cermak, T., Doyle, E. L., Schmidt, C. et al., Targeting DNA double-strand breaks with TAL effector nucleases. Genetics 2010, 186, 757-761.
    • (2010) Genetics , vol.186 , pp. 757-761
    • Christian, M.1    Cermak, T.2    Doyle, E.L.3    Schmidt, C.4
  • 22
    • 79551685675 scopus 로고    scopus 로고
    • A TALE nuclease architecture for efficient genome editing
    • Miller, J. C., Tan, S., Qiao, G., Barlow, K. A. et al., A TALE nuclease architecture for efficient genome editing. Nat. Biotechnol. 2011, 29, 143-148.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 143-148
    • Miller, J.C.1    Tan, S.2    Qiao, G.3    Barlow, K.A.4
  • 23
    • 72149110399 scopus 로고    scopus 로고
    • Breaking the code of DNA binding specificity of TAL-type III effectors
    • Boch, J., Scholze, H., Schornack, S., Landgraf, A. et al., Breaking the code of DNA binding specificity of TAL-type III effectors. Science 2009, 326, 1509-1512.
    • (2009) Science , vol.326 , pp. 1509-1512
    • Boch, J.1    Scholze, H.2    Schornack, S.3    Landgraf, A.4
  • 24
    • 72149090954 scopus 로고    scopus 로고
    • A simple cipher governs DNA recognition by TAL effectors
    • Moscou, M. J., Bogdanove, A. J., A simple cipher governs DNA recognition by TAL effectors. Science 2009, 326, 1501.
    • (2009) Science , vol.326 , pp. 1501
    • Moscou, M.J.1    Bogdanove, A.J.2
  • 25
    • 84875157258 scopus 로고    scopus 로고
    • A library of TAL effector nucleases spanning the human genome
    • Kim, Y., Kweon, J., Kim, A., Chon, J. K. et al., A library of TAL effector nucleases spanning the human genome. Nat. Biotechnol. 2013, 31, 251-258.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 251-258
    • Kim, Y.1    Kweon, J.2    Kim, A.3    Chon, J.K.4
  • 26
    • 84873729095 scopus 로고    scopus 로고
    • Multiplex genome engineering using CRISPR/Cas systems
    • Cong, L., Ran, F. A., Cox, D., Lin, S. et al., Multiplex genome engineering using CRISPR/Cas systems. Science 2013, 339, 819-823.
    • (2013) Science , vol.339 , pp. 819-823
    • Cong, L.1    Ran, F.A.2    Cox, D.3    Lin, S.4
  • 27
    • 84865070369 scopus 로고    scopus 로고
    • A programmable dual-RNA-guided DNA endonuclease in adaptive bacterial immunity
    • Jinek, M., Chylinski, K., Fonfara, I., Hauer, M. et al., A programmable dual-RNA-guided DNA endonuclease in adaptive bacterial immunity. Science 2012, 337, 816-821.
    • (2012) Science , vol.337 , pp. 816-821
    • Jinek, M.1    Chylinski, K.2    Fonfara, I.3    Hauer, M.4
  • 28
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • Mali, P., Yang, L., Esvelt, K. M., Aach, J. et al., RNA-guided human genome engineering via Cas9. Science 2013, 339, 823-826.
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1    Yang, L.2    Esvelt, K.M.3    Aach, J.4
  • 29
    • 84855237715 scopus 로고    scopus 로고
    • Mariati , IRES-mediated Tricistronic vectors for enhancing generation of high monoclonal antibody expressing CHO cell lines
    • Ho, S. C., Bardor, M., Feng, H., Mariati et al., IRES-mediated Tricistronic vectors for enhancing generation of high monoclonal antibody expressing CHO cell lines. J. Biotechnol. 2012, 157, 130-139.
    • (2012) J. Biotechnol. , vol.157 , pp. 130-139
    • Ho, S.C.1    Bardor, M.2    Feng, H.3
  • 30
    • 84861376809 scopus 로고    scopus 로고
    • Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant
    • Zhang, P., Haryadi, R., Chan, K. F., Teo, G. et al., Identification of functional elements of the GDP-fucose transporter SLC35C1 using a novel Chinese hamster ovary mutant. Glycobiology 2012, 22, 897-911.
    • (2012) Glycobiology , vol.22 , pp. 897-911
    • Zhang, P.1    Haryadi, R.2    Chan, K.F.3    Teo, G.4
  • 31
    • 0024690540 scopus 로고
    • Genetic and structural characterization of the avirulence gene avrBs3 from Xanthomonas campestris pv. vesicatoria
    • Bonas, U., Stall, R. E., Staskawicz, B., Genetic and structural characterization of the avirulence gene avrBs3 from Xanthomonas campestris pv. vesicatoria. Mol. Gen. Genet. 1989, 218, 127-136.
    • (1989) Mol. Gen. Genet. , vol.218 , pp. 127-136
    • Bonas, U.1    Stall, R.E.2    Staskawicz, B.3
  • 32
    • 77953702888 scopus 로고    scopus 로고
    • 3rd, Directed evolution of an enhanced and highly efficient FokI cleavage domain for zinc finger nucleases
    • Guo, J., Gaj, T., Barbas, C. F., 3rd, Directed evolution of an enhanced and highly efficient FokI cleavage domain for zinc finger nucleases. J. Mol. Biol. 2010, 400, 96-107.
    • (2010) J. Mol. Biol. , vol.400 , pp. 96-107
    • Guo, J.1    Gaj, T.2    Barbas, C.F.3
  • 33
    • 78650912707 scopus 로고    scopus 로고
    • Enhancing zinc-finger-nuclease activity with improved obligate heterodimeric architectures
    • Doyon, Y., Vo, T. D., Mendel, M. C., Greenberg, S. G. et al., Enhancing zinc-finger-nuclease activity with improved obligate heterodimeric architectures. Nat. Methods 2011, 8, 74-79.
    • (2011) Nat. Methods , vol.8 , pp. 74-79
    • Doyon, Y.1    Vo, T.D.2    Mendel, M.C.3    Greenberg, S.G.4
  • 34
    • 84861170955 scopus 로고    scopus 로고
    • A transcription activator-like effector toolbox for genome engineering
    • Sanjana, N. E., Cong, L., Zhou, Y., Cunniff, M. M. et al., A transcription activator-like effector toolbox for genome engineering. Nat. Protoc. 2012, 7, 171-192.
    • (2012) Nat. Protoc. , vol.7 , pp. 171-192
    • Sanjana, N.E.1    Cong, L.2    Zhou, Y.3    Cunniff, M.M.4
  • 35
    • 79960064013 scopus 로고    scopus 로고
    • Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting
    • Cermak, T., Doyle, E. L., Christian, M., Wang, L. et al., Efficient design and assembly of custom TALEN and other TAL effector-based constructs for DNA targeting. Nucleic Acids Res. 2011, 39, e82.
    • (2011) Nucleic Acids Res. , vol.39
    • Cermak, T.1    Doyle, E.L.2    Christian, M.3    Wang, L.4
  • 36
    • 84864475122 scopus 로고    scopus 로고
    • TAL Effector-Nucleotide Targeter (TALE-NT) 2.0: Tools for TAL effector design and target prediction
    • Doyle, E. L., Booher, N. J., Standage, D. S., Voytas, D. F. et al., TAL Effector-Nucleotide Targeter (TALE-NT) 2.0: Tools for TAL effector design and target prediction. Nucleic Acids Res. 2012, 40, W117-W122.
    • (2012) Nucleic Acids Res. , vol.40 , pp. W117-W122
    • Doyle, E.L.1    Booher, N.J.2    Standage, D.S.3    Voytas, D.F.4
  • 37
    • 67650045497 scopus 로고    scopus 로고
    • Targeted genome editing in human cells with zinc finger nucleases constructed via modular assembly
    • Kim, H. J., Lee, H. J., Kim, H., Cho, S. W., Kim, J. S., Targeted genome editing in human cells with zinc finger nucleases constructed via modular assembly. Genome Res. 2009, 19, 1279-1288.
    • (2009) Genome Res. , vol.19 , pp. 1279-1288
    • Kim, H.J.1    Lee, H.J.2    Kim, H.3    Cho, S.W.4    Kim, J.S.5
  • 38
    • 77957754251 scopus 로고    scopus 로고
    • A rapid and general assay for monitoring endogenous gene modification
    • Guschin, D. Y., Waite, A. J., Katibah, G. E., Miller, J. C. et al., A rapid and general assay for monitoring endogenous gene modification. Methods Mol. Biol. 2010, 649, 247-256.
    • (2010) Methods Mol. Biol. , vol.649 , pp. 247-256
    • Guschin, D.Y.1    Waite, A.J.2    Katibah, G.E.3    Miller, J.C.4
  • 39
    • 77953025411 scopus 로고    scopus 로고
    • RCA-I-resistant CHO mutant cells have dysfunctional GnT I and expression of normal GnT I in these mutants enhances sialylation of recombinant erythropoietin
    • Goh, J. S., Zhang, P., Chan, K. F., Lee, M. M. et al., RCA-I-resistant CHO mutant cells have dysfunctional GnT I and expression of normal GnT I in these mutants enhances sialylation of recombinant erythropoietin. Metab. Eng. 2010, 12, 360-368.
    • (2010) Metab. Eng. , vol.12 , pp. 360-368
    • Goh, J.S.1    Zhang, P.2    Chan, K.F.3    Lee, M.M.4
  • 40
    • 54549083448 scopus 로고    scopus 로고
    • The Golgi CMP-sialic acid transporter: A new CHO mutant provides functional insights
    • Lim, S. F., Lee, M. M., Zhang, P., Song, Z., The Golgi CMP-sialic acid transporter: A new CHO mutant provides functional insights. Glycobiology 2008, 18, 851-860.
    • (2008) Glycobiology , vol.18 , pp. 851-860
    • Lim, S.F.1    Lee, M.M.2    Zhang, P.3    Song, Z.4
  • 41
    • 0028344521 scopus 로고
    • Mass spectrometry of carbohydrate-containing biopolymers
    • Dell, A., Reason, A. J., Khoo, K. H., Panico, M. et al., Mass spectrometry of carbohydrate-containing biopolymers. Methods Enzymol. 1994, 230, 108-132.
    • (1994) Methods Enzymol. , vol.230 , pp. 108-132
    • Dell, A.1    Reason, A.J.2    Khoo, K.H.3    Panico, M.4
  • 42
    • 77949325755 scopus 로고    scopus 로고
    • Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity
    • North, S. J., Huang, H. H., Sundaram, S., Jang-Lee, J. et al., Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity. J. Biol. Chem. 2010, 285, 5759-5775.
    • (2010) J. Biol. Chem. , vol.285 , pp. 5759-5775
    • North, S.J.1    Huang, H.H.2    Sundaram, S.3    Jang-Lee, J.4
  • 43
    • 79952924336 scopus 로고    scopus 로고
    • Erythropoietin produced in a human cell line (Dynepo) has significant differences in glycosylation compared with erythropoietins produced in CHO cell lines
    • Shahrokh, Z., Royle, L., Saldova, R., Bones, J. et al., Erythropoietin produced in a human cell line (Dynepo) has significant differences in glycosylation compared with erythropoietins produced in CHO cell lines. Mol. Pharm. 2011, 8, 286-296.
    • (2011) Mol. Pharm. , vol.8 , pp. 286-296
    • Shahrokh, Z.1    Royle, L.2    Saldova, R.3    Bones, J.4
  • 44
    • 0034602243 scopus 로고    scopus 로고
    • 3rd, Insights into the molecular recognition of the 5'-GNN-3' family of DNA sequences by zinc finger domains
    • Dreier, B., Segal, D. J., Barbas, C. F., 3rd, Insights into the molecular recognition of the 5'-GNN-3' family of DNA sequences by zinc finger domains. J. Mol. Biol. 2000, 303, 489-502.
    • (2000) J. Mol. Biol. , vol.303 , pp. 489-502
    • Dreier, B.1    Segal, D.J.2    Barbas, C.F.3
  • 45
    • 0037040240 scopus 로고    scopus 로고
    • Validated zinc finger protein designs for all 16 GNN DNA triplet targets
    • Liu, Q., Xia, Z., Zhong, X., Case, C. C., Validated zinc finger protein designs for all 16 GNN DNA triplet targets. J. Biol. Chem. 2002, 277, 3850-3856.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3850-3856
    • Liu, Q.1    Xia, Z.2    Zhong, X.3    Case, C.C.4
  • 46
    • 0032981699 scopus 로고    scopus 로고
    • 3rd, Toward controlling gene expression at will: Selection and design of zinc finger domains recognizing each of the 5'-GNN-3' DNA target sequences
    • Segal, D. J., Dreier, B., Beerli, R. R., Barbas, C. F., 3rd, Toward controlling gene expression at will: Selection and design of zinc finger domains recognizing each of the 5'-GNN-3' DNA target sequences. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 2758-2763.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2758-2763
    • Segal, D.J.1    Dreier, B.2    Beerli, R.R.3    Barbas, C.F.4
  • 47
    • 34547605763 scopus 로고    scopus 로고
    • Zinc Finger Targeter (ZiFiT): An engineered zinc finger/target site design tool
    • Sander, J. D., Zaback, P., Joung, J. K., Voytas, D. F., Dobbs, D., Zinc Finger Targeter (ZiFiT): An engineered zinc finger/target site design tool. Nucleic Acids Res. 2007, 35, W599-W605.
    • (2007) Nucleic Acids Res. , vol.35 , pp. W599-W605
    • Sander, J.D.1    Zaback, P.2    Joung, J.K.3    Voytas, D.F.4    Dobbs, D.5
  • 48
    • 84864856835 scopus 로고    scopus 로고
    • Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains
    • Cong, L., Zhou, R., Kuo, Y. C., Cunniff, M., Zhang, F., Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains. Nat. Commun. 2012, 3, 968.
    • (2012) Nat. Commun. , vol.3 , pp. 968
    • Cong, L.1    Zhou, R.2    Kuo, Y.C.3    Cunniff, M.4    Zhang, F.5
  • 49
    • 34447536869 scopus 로고    scopus 로고
    • Carbohydrate binding specificity of a fucose-specific lectin from Aspergillus oryzae: A novel probe for core fucose
    • Matsumura, K., Higashida, K., Ishida, H., Hata, Y. et al., Carbohydrate binding specificity of a fucose-specific lectin from Aspergillus oryzae: A novel probe for core fucose. J. Biol. Chem. 2007, 282, 15700-15708.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15700-15708
    • Matsumura, K.1    Higashida, K.2    Ishida, H.3    Hata, Y.4
  • 50
    • 84903545084 scopus 로고    scopus 로고
    • Genome-wide analysis reveals characteristics of off-target sites bound by the Cas9 endonuclease
    • Kuscu, C., Arslan, S., Singh, R., Thorpe, J., Adli, M., Genome-wide analysis reveals characteristics of off-target sites bound by the Cas9 endonuclease. Nat. Biotechnol. 2014, 32, 677-683.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 677-683
    • Kuscu, C.1    Arslan, S.2    Singh, R.3    Thorpe, J.4    Adli, M.5
  • 51
    • 84902095352 scopus 로고    scopus 로고
    • Genome-wide binding of the CRISPR endonuclease Cas9 in mammalian cells
    • Wu, X., Scott, D. A., Kriz, A. J., Chiu, A. C. et al., Genome-wide binding of the CRISPR endonuclease Cas9 in mammalian cells. Nat. Biotechnol. 2014, 32, 670-676.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 670-676
    • Wu, X.1    Scott, D.A.2    Kriz, A.J.3    Chiu, A.C.4
  • 52
    • 84923275611 scopus 로고    scopus 로고
    • Genome-wide detection of DNA double-stranded breaks induced by engineered nucleases
    • Frock, R. L., Hu, J., Meyers, R. M., Ho, Y. J. et al., Genome-wide detection of DNA double-stranded breaks induced by engineered nucleases. Nat. Biotechnol. 2015, 33, 179-186.
    • (2015) Nat. Biotechnol. , vol.33 , pp. 179-186
    • Frock, R.L.1    Hu, J.2    Meyers, R.M.3    Ho, Y.J.4
  • 53
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • Marino, K., Bones, J., Kattla, J. J., Rudd, P. M., A systematic approach to protein glycosylation analysis: A path through the maze. Nat. Chem. Biol. 2010, 6, 713-723.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 713-723
    • Marino, K.1    Bones, J.2    Kattla, J.J.3    Rudd, P.M.4
  • 54
    • 0023657264 scopus 로고
    • The GDP-fucose: N-acetylglucosaminide 3-alpha-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates
    • Howard, D. R., Fukuda, M., Fukuda, M. N., Stanley, P., The GDP-fucose: N-acetylglucosaminide 3-alpha-L-fucosyltransferases of LEC11 and LEC12 Chinese hamster ovary mutants exhibit novel specificities for glycolipid substrates. J. Biol. Chem. 1987, 262, 16830-16837.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16830-16837
    • Howard, D.R.1    Fukuda, M.2    Fukuda, M.N.3    Stanley, P.4
  • 55
    • 79961191745 scopus 로고    scopus 로고
    • The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line
    • Xu, X., Nagarajan, H., Lewis, N. E., Pan, S. et al., The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line. Nat. Biotechnol. 2011, 29, 735-741.
    • (2011) Nat. Biotechnol. , vol.29 , pp. 735-741
    • Xu, X.1    Nagarajan, H.2    Lewis, N.E.3    Pan, S.4
  • 56
    • 15744372996 scopus 로고    scopus 로고
    • O-fucosylation of notch occurs in the endoplasmic reticulum
    • Luo, Y., Haltiwanger, R. S., O-fucosylation of notch occurs in the endoplasmic reticulum. J. Biol. Chem. 2005, 280, 11289-11294.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11289-11294
    • Luo, Y.1    Haltiwanger, R.S.2
  • 57
    • 33646233634 scopus 로고    scopus 로고
    • Protein O-fucosyltransferase 2 add O-fucose to thrombospondin type 1 repeats
    • Luo, Y., Koles, K., Vorndam, W., Haltiwanger, R. S., Panin, V. M., Protein O-fucosyltransferase 2 add O-fucose to thrombospondin type 1 repeats. J. Biol. Chem. 2006, 281, 9393-9399.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9393-9399
    • Luo, Y.1    Koles, K.2    Vorndam, W.3    Haltiwanger, R.S.4    Panin, V.M.5
  • 58
    • 79953158012 scopus 로고    scopus 로고
    • The generation of zinc finger proteins by modular assembly
    • Bhakta, M. S., Segal, D. J., The generation of zinc finger proteins by modular assembly. Methods Mol. Biol. 2010, 649, 3-30.
    • (2010) Methods Mol. Biol. , vol.649 , pp. 3-30
    • Bhakta, M.S.1    Segal, D.J.2
  • 59
    • 84860747716 scopus 로고    scopus 로고
    • FLASH assembly of TALENs for high-throughput genome editing
    • Reyon, D., Tsai, S. Q., Khayter, C., Foden, J. A. et al., FLASH assembly of TALENs for high-throughput genome editing. Nat. Biotechnol. 2012, 30, 460-465.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 460-465
    • Reyon, D.1    Tsai, S.Q.2    Khayter, C.3    Foden, J.A.4
  • 60
    • 84872203111 scopus 로고    scopus 로고
    • A ligation-independent cloning technique for high-throughput assembly of transcription activator-like effector genes
    • Schmid-Burgk, J. L., Schmidt, T., Kaiser, V., Honing, K., Hornung, V., A ligation-independent cloning technique for high-throughput assembly of transcription activator-like effector genes. Nat. Biotechnol. 2013, 31, 76-81.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 76-81
    • Schmid-Burgk, J.L.1    Schmidt, T.2    Kaiser, V.3    Honing, K.4    Hornung, V.5


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