메뉴 건너뛰기




Volumn 4, Issue 200, 2011, Pages

Ric-8 proteins are molecular chaperones that direct nascent G protein α subunit membrane association

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; MESSENGER RNA; PROTEIN RIC 8A; PROTEIN RIC 8B; UNCLASSIFIED DRUG; GUANINE NUCLEOTIDE EXCHANGE FACTOR; RIC 8A PROTEIN, HUMAN; RIC 8B PROTEIN, HUMAN; RIC-8A PROTEIN, HUMAN; RIC-8B PROTEIN, HUMAN; RIC8 PROTEIN, MOUSE; RIC8B PROTEIN, MOUSE; STIMULATORY GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 81855183850     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002223     Document Type: Article
Times cited : (94)

References (66)
  • 2
    • 0037424298 scopus 로고    scopus 로고
    • Mammalian Ric-8A (synembryn) is a heterotrimeric Gα protein guanine nucleotide exchange factor
    • G. G. Tall, A. M. Krumins, A. G. Gilman, Mammalian Ric-8A (synembryn) is a heterotrimeric Gα protein guanine nucleotide exchange factor. J. Biol. Chem. 278, 8356-8362 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 8356-8362
    • Tall, G.G.1    Krumins, A.M.2    Gilman, A.G.3
  • 5
    • 0034533704 scopus 로고    scopus 로고
    • oα) in regulating a subset of centrosome movements during early embryogenesis in Caenorhabditis elegans
    • oα) in regulating a subset of centrosome movements during early embryogenesis in Caenorhabditis elegans. Genetics 156, 1649-1660 (2000).
    • (2000) Genetics , vol.156 , pp. 1649-1660
    • Miller, K.G.1    Rand, J.B.2
  • 6
    • 15544362770 scopus 로고    scopus 로고
    • Convergent, RIC-8-dependent Gαsignaling pathways in the Caenorhabditis elegans synaptic signaling network
    • N. K. Reynolds, M. A. Schade, K. G. Miller, Convergent, RIC-8-dependent Gαsignaling pathways in the Caenorhabditis elegans synaptic signaling network. Genetics 169, 651-670 (2005).
    • (2005) Genetics , vol.169 , pp. 651-670
    • Reynolds, N.K.1    Schade, M.A.2    Miller, K.G.3
  • 7
    • 5444260164 scopus 로고    scopus 로고
    • RIC-8 is required for GPR-1/2-dependent Gα function during asymmetric division of C. elegans embryos
    • K. Afshar, F. S. Willard, K. Colombo, C. A. Johnston, C. R. McCudden, D. P. Siderovski, P. Gönczy, RIC-8 is required for GPR-1/2-dependent Gα function during asymmetric division of C. elegans embryos. Cell 119, 219-230 (2004).
    • (2004) Cell , vol.119 , pp. 219-230
    • Afshar, K.1    Willard, F.S.2    Colombo, K.3    Johnston, C.A.4    McCudden, C.R.5    Siderovski, D.P.6    Gönczy, P.7
  • 8
    • 6944256893 scopus 로고    scopus 로고
    • Control of embryonic spindle positioning and Gα activity by C. elegans RIC-8
    • C. Couwenbergs, A. C. Spilker, M. Gotta, Control of embryonic spindle positioning and Gα activity by C. elegans RIC-8. Curr. Biol. 14, 1871-1876 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 1871-1876
    • Couwenbergs, C.1    Spilker, A.C.2    Gotta, M.3
  • 9
    • 5444259457 scopus 로고    scopus 로고
    • RGS-7 completes a receptor-independent heterotrimeric G protein cycle to asymmetrically regulate mitotic spindle positioning in C. elegans
    • H. A. Hess, J. C. Röper, S. W. Grill, M. R. Koelle, RGS-7 completes a receptor-independent heterotrimeric G protein cycle to asymmetrically regulate mitotic spindle positioning in C. elegans. Cell 119, 209-218 (2004).
    • (2004) Cell , vol.119 , pp. 209-218
    • Hess, H.A.1    Röper, J.C.2    Grill, S.W.3    Koelle, M.R.4
  • 10
    • 33644831591 scopus 로고    scopus 로고
    • Drosophila G-protein signalling: Intricate roles for Ric-8?
    • F. Matsuzaki, Drosophila G-protein signalling: Intricate roles for Ric-8? Nat. Cell Biol. 7, 1047-1049 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1047-1049
    • Matsuzaki, F.1
  • 11
    • 28044435388 scopus 로고    scopus 로고
    • Resistance to inhibitors of cholinesterase 8A catalyzes release of Gαi-GTP and nuclear mitotic apparatus protein (NuMA) from NuMA/LGN/Gαi-GDP complexes
    • G. G. Tall, A. G. Gilman, Resistance to inhibitors of cholinesterase 8A catalyzes release of Gαi-GTP and nuclear mitotic apparatus protein (NuMA) from NuMA/LGN/Gαi-GDP complexes. Proc. Natl. Acad. Sci. U.S.A. 102, 16584-16589 (2005).
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 16584-16589
    • Tall, G.G.1    Gilman, A.G.2
  • 12
    • 77954357112 scopus 로고    scopus 로고
    • Ric-8A and Giαrecruit LGN, NuMA, and dynein to the cell cortex to help orient the mitotic spindle
    • G. E. Woodard, N. N. Huang, H. Cho, T. Miki, G. G. Tall, J. H. Kehrl, Ric-8A and Giαrecruit LGN, NuMA, and dynein to the cell cortex to help orient the mitotic spindle. Mol. Cell. Biol. 30, 3519-3530 (2010).
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3519-3530
    • Woodard, G.E.1    Huang, N.N.2    Cho, H.3    Miki, T.4    Tall, G.G.5    Kehrl, J.H.6
  • 13
    • 45649083152 scopus 로고    scopus 로고
    • Ric-8B interacts with Gαolf and Gγ13 and co-localizes with Gαolf, Gβ1 and Gγ13 in the cilia of olfactory sensory neurons
    • D. S. Kerr, L. E. C. Von Dannecker, M. Davalos, J. S. Michaloski, B. Malnic, Ric-8B interacts with Gαolf and Gγ13 and co-localizes with Gαolf, Gβ1 and Gγ13 in the cilia of olfactory sensory neurons. Mol. Cell. Neurosci. 38, 341-348 (2008).
    • (2008) Mol. Cell. Neurosci. , vol.38 , pp. 341-348
    • Kerr, D.S.1    Von Dannecker, L.E.C.2    Davalos, M.3    Michaloski, J.S.4    Malnic, B.5
  • 14
    • 33645830270 scopus 로고    scopus 로고
    • Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells
    • A. Nishimura, M. Okamoto, Y. Sugawara, N. Mizuno, J. Yamauchi, H. Itoh, Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells. Genes Cells 11, 487-498 (2006).
    • (2006) Genes Cells , vol.11 , pp. 487-498
    • Nishimura, A.1    Okamoto, M.2    Sugawara, Y.3    Mizuno, N.4    Yamauchi, J.5    Itoh, H.6
  • 15
    • 17644404436 scopus 로고    scopus 로고
    • Ric-8B, an olfactory putative GTP exchange factor, amplifies signal transduction through the olfactory-specific G-protein Gαolf
    • L. E. C. Von Dannecker, A. F. Mercandante, B. Malnic, Ric-8B, an olfactory putative GTP exchange factor, amplifies signal transduction through the olfactory-specific G-protein Gαolf. J. Neurosci. 25, 3793-3800 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 3793-3800
    • Von Dannecker, L.E.C.1    Mercandante, A.F.2    Malnic, B.3
  • 17
    • 34447549293 scopus 로고    scopus 로고
    • Synergism of accessory factors in functional expression of mammalian odorant receptors
    • H. Zhuang, H. Matsunami, Synergism of accessory factors in functional expression of mammalian odorant receptors. J. Biol. Chem. 282, 15284-15293 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 15284-15293
    • Zhuang, H.1    Matsunami, H.2
  • 18
    • 27844524595 scopus 로고    scopus 로고
    • Drosophila Ric-8 regulates Gαi cortical localization to promote Gαi-dependent planar orientation of the mitotic spindle during asymmetric cell division
    • N. B. David, C. A. Martin, M. Segalen, F. Rosenfeld, F. Schweisguth, Y. Bellaïche, Drosophila Ric-8 regulates Gαi cortical localization to promote Gαi-dependent planar orientation of the mitotic spindle during asymmetric cell division. Nat. Cell Biol. 7, 1083-1090 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1083-1090
    • David, N.B.1    Martin, C.A.2    Segalen, M.3    Rosenfeld, F.4    Schweisguth, F.5    Bellaïche, Y.6
  • 19
    • 28844481199 scopus 로고    scopus 로고
    • Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins
    • B. Hampoelz, O. Hoeller, S. K. Bowman, D. Dunican, J. A. Knoblich, Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins. Nat. Cell Biol. 7, 1099-1105 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1099-1105
    • Hampoelz, B.1    Hoeller, O.2    Bowman, S.K.3    Dunican, D.4    Knoblich, J.A.5
  • 20
    • 28844482414 scopus 로고    scopus 로고
    • Ric-8 controls Drosophila neural progenitor asymmetric division by regulating heterotrimeric G proteins
    • H. Wang, K. H. Ng, H. Qian, D. P. Siderovski, W. Chia, F. Yu, Ric-8 controls Drosophila neural progenitor asymmetric division by regulating heterotrimeric G proteins. Nat. Cell Biol. 7, 1091-1098 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1091-1098
    • Wang, H.1    Ng, K.H.2    Qian, H.3    Siderovski, D.P.4    Chia, W.5    Yu, F.6
  • 21
    • 27544481187 scopus 로고    scopus 로고
    • Cortical localization of the Gα protein GPA-16 requires RIC-8 function during C. elegans asymmetric cell division
    • K. Afshar, F. S. Willard, K. Colombo, D. P. Siderovski, P. Gönczy, Cortical localization of the Gα protein GPA-16 requires RIC-8 function during C. elegans asymmetric cell division. Development 132, 4449-4459 (2005).
    • (2005) Development , vol.132 , pp. 4449-4459
    • Afshar, K.1    Willard, F.S.2    Colombo, K.3    Siderovski, D.P.4    Gönczy, P.5
  • 22
    • 77951215559 scopus 로고    scopus 로고
    • Ric-8B stabilizes the a subunit of stimulatory G protein by inhibiting its ubiquitination
    • Y. Nagai, A. Nishimura, K. Tago, N. Mizuno, H. Itoh, Ric-8B stabilizes the a subunit of stimulatory G protein by inhibiting its ubiquitination. J. Biol. Chem. 285, 11114-11120 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 11114-11120
    • Nagai, Y.1    Nishimura, A.2    Tago, K.3    Mizuno, N.4    Itoh, H.5
  • 24
    • 0030730821 scopus 로고    scopus 로고
    • Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms
    • G. W. Farr, E. C. Scharl, R. J. Schumacher, S. Sondek, A. L. Horwich, Chaperonin-mediated folding in the eukaryotic cytosol proceeds through rounds of release of native and nonnative forms. Cell 89, 927-937 (1997).
    • (1997) Cell , vol.89 , pp. 927-937
    • Farr, G.W.1    Scharl, E.C.2    Schumacher, R.J.3    Sondek, S.4    Horwich, A.L.5
  • 25
    • 33745989271 scopus 로고    scopus 로고
    • Role of the chaperonin CCT/TRiC complex in G protein βγ-dimer assembly
    • C. A. Wells, J. Dingus, J. D. Hildebrandt, Role of the chaperonin CCT/TRiC complex in G protein βγ-dimer assembly. J. Biol. Chem. 281, 20221-20232 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 20221-20232
    • Wells, C.A.1    Dingus, J.2    Hildebrandt, J.D.3
  • 26
    • 34250325496 scopus 로고    scopus 로고
    • Dopamine receptor-interacting protein 78 acts as a molecular chaperone for Gγ subunits before assembly with Gβ
    • D. J. Dupré, M. Robitaille, M. Richer, N. Ethier, A. M. Mamarbachi, T. E. Hébert, Dopamine receptor-interacting protein 78 acts as a molecular chaperone for Gγ subunits before assembly with Gβ. J. Biol. Chem. 282, 13703-13715 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 13703-13715
    • Dupré, D.J.1    Robitaille, M.2    Richer, M.3    Ethier, N.4    Mamarbachi, A.M.5    Hébert, T.E.6
  • 27
    • 33746816585 scopus 로고    scopus 로고
    • Mechanism of assembly of G protein βγ subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex
    • G. L. Lukov, C. M. Baker, P. J. Ludtke, T. Hu, M. D. Carter, R. A. Hackett, C. D. Thulin, B. M. Willardson, Mechanism of assembly of G protein βγ subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex. J. Biol. Chem. 281, 22261-22274 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 22261-22274
    • Lukov, G.L.1    Baker, C.M.2    Ludtke, P.J.3    Hu, T.4    Carter, M.D.5    Hackett, R.A.6    Thulin, C.D.7    Willardson, B.M.8
  • 28
    • 21244502200 scopus 로고    scopus 로고
    • Phosducin-like protein acts as a molecular chaperone for G protein βγ dimer assembly
    • G. L. Lukov, T. Hu, J. N. McLaughlin, H. E. Hamm, B. M. Willardson, Phosducin-like protein acts as a molecular chaperone for G protein βγ dimer assembly. EMBO J. 24, 1965-1975 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1965-1975
    • Lukov, G.L.1    Hu, T.2    McLaughlin, J.N.3    Hamm, H.E.4    Willardson, B.M.5
  • 29
    • 0030890789 scopus 로고    scopus 로고
    • Assembly and intracellular targeting of the βγ subunits of heterotrimeric G proteins
    • A. Rehm, H. L. Ploegh, Assembly and intracellular targeting of the βγ subunits of heterotrimeric G proteins. J. Cell Biol. 137, 305-317 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 305-317
    • Rehm, A.1    Ploegh, H.L.2
  • 30
    • 65249153536 scopus 로고    scopus 로고
    • The role of Gβγ subunits in the organization, assembly, and function of GPCR signaling complexes
    • D. J. Dupré, M. Robitaille, R. V. Rebois, T. E. Hébert, The role of Gβγ subunits in the organization, assembly, and function of GPCR signaling complexes. Annu. Rev. Pharmacol. Toxicol. 49, 31-56 (2009).
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 31-56
    • Dupré, D.J.1    Robitaille, M.2    Rebois, R.V.3    Hébert, T.E.4
  • 31
    • 35148868765 scopus 로고    scopus 로고
    • Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding
    • B. M. Willardson, A. C. Howlett, Function of phosducin-like proteins in G protein signaling and chaperone-assisted protein folding. Cell. Signal. 19, 2417-2427 (2007).
    • (2007) Cell. Signal. , vol.19 , pp. 2417-2427
    • Willardson, B.M.1    Howlett, A.C.2
  • 34
    • 0025012836 scopus 로고
    • G-protein α-subunit expression, myristoylation, and membrane association in COS cells
    • S. M. Mumby, R. O. Heukeroth, J. I. Gordon, A. G. Gilman, G-protein α-subunit expression, myristoylation, and membrane association in COS cells. Proc. Natl. Acad. Sci. U.S.A. 87, 728-732 (1990).
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 728-732
    • Mumby, S.M.1    Heukeroth, R.O.2    Gordon, J.I.3    Gilman, A.G.4
  • 38
    • 0343079334 scopus 로고
    • Stimulation of β-adrenergic receptors of S49 lymphoma cells redistributes the a subunit of the stimulatory G protein between cytosol and membranes
    • L. A. Ransnas, P. Svoboda, J. R. Jasper, P. A. Insel, Stimulation of β-adrenergic receptors of S49 lymphoma cells redistributes the a subunit of the stimulatory G protein between cytosol and membranes. Proc. Natl. Acad. Sci. U.S.A. 86, 7900-7903 (1989).
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7900-7903
    • Ransnas, L.A.1    Svoboda, P.2    Jasper, J.R.3    Insel, P.A.4
  • 39
    • 0036204952 scopus 로고    scopus 로고
    • Hormone-induced subcellular redistribution of trimeric G proteins
    • P. Svoboda, J. Novotny, Hormone-induced subcellular redistribution of trimeric G proteins. Cell. Mol. Life Sci. 59, 501-512 (2002).
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 501-512
    • Svoboda, P.1    Novotny, J.2
  • 42
    • 34548216374 scopus 로고    scopus 로고
    • Shuttling of G protein subunits between the plasma membrane and intracellular membranes
    • M. Chisari, D. K. Saini, V. Kalyanaraman, N. Gautam, Shuttling of G protein subunits between the plasma membrane and intracellular membranes. J. Biol. Chem. 282, 24092-24098 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 24092-24098
    • Chisari, M.1    Saini, D.K.2    Kalyanaraman, V.3    Gautam, N.4
  • 43
    • 78649713805 scopus 로고    scopus 로고
    • Nucleotide exchange factor RIC-8 is indispensable in mammalian early development
    • T. Tõnissoo, S. Lulla, R. Meier, M. Saare, K. Ruisu, M. Pooga, A. Karis, Nucleotide exchange factor RIC-8 is indispensable in mammalian early development. Dev. Dyn. 239, 3404-3415 (2010).
    • (2010) Dev. Dyn. , vol.239 , pp. 3404-3415
    • Tõnissoo, T.1    Lulla, S.2    Meier, R.3    Saare, M.4    Ruisu, K.5    Pooga, M.6    Karis, A.7
  • 46
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein α subunits
    • D. P. Siderovski, F. S. Willard, The GAPs, GEFs, and GDIs of heterotrimeric G-protein α subunits. Int. J. Biol. Sci. 1, 51-66 (2005).
    • (2005) Int. J. Biol. Sci. , vol.1 , pp. 51-66
    • Siderovski, D.P.1    Willard, F.S.2
  • 47
    • 3142766112 scopus 로고    scopus 로고
    • Visualization of G protein βγ dimers using bimolecular fluorescence complementation demonstrates roles for both β and γ in subcellular targeting
    • T. R. Hynes, L. Tang, S. M. Mervine, J. L. Sabo, E. A. Yost, P. N. Devreotes, C. H. Berlot, Visualization of G protein βγ dimers using bimolecular fluorescence complementation demonstrates roles for both β and γ in subcellular targeting. J. Biol. Chem. 279, 30279-30286 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 30279-30286
    • Hynes, T.R.1    Tang, L.2    Mervine, S.M.3    Sabo, J.L.4    Yost, E.A.5    Devreotes, P.N.6    Berlot, C.H.7
  • 48
    • 2142858516 scopus 로고
    • Antisera of designed specificity for subunits of guanine nucleotide-binding regulatory proteins
    • S. M. Mumby, R. A. Kahn, D. R. Manning, A. G. Gilman, Antisera of designed specificity for subunits of guanine nucleotide-binding regulatory proteins. Proc. Natl. Acad. Sci. U.S.A. 83, 265-269 (1986).
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 265-269
    • Mumby, S.M.1    Kahn, R.A.2    Manning, D.R.3    Gilman, A.G.4
  • 50
    • 0026785920 scopus 로고
    • Adenylyl cyclases
    • W. J. Tang, A. G. Gilman, Adenylyl cyclases. Cell 70, 869-872 (1992).
    • (1992) Cell , vol.70 , pp. 869-872
    • Tang, W.J.1    Gilman, A.G.2
  • 52
    • 33744544518 scopus 로고    scopus 로고
    • Targeted knockdown of G protein subunits selectively prevents receptor-mediated modulation of effectors and reveals complex changes in non-targeted signaling proteins
    • A. M. Krumins, A. G. Gilman, Targeted knockdown of G protein subunits selectively prevents receptor-mediated modulation of effectors and reveals complex changes in non-targeted signaling proteins. J. Biol. Chem. 281, 10250-10262 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 10250-10262
    • Krumins, A.M.1    Gilman, A.G.2
  • 54
    • 22344433739 scopus 로고    scopus 로고
    • Ric-8 enhances G protein βγ-dependent signaling in response to βγ-binding peptides in intact cells
    • S. Malik, M. Ghosh, T. M. Bonacci, G. G. Tall, A. V. Smrcka, Ric-8 enhances G protein βγ-dependent signaling in response to βγ-binding peptides in intact cells. Mol. Pharmacol. 68, 129-136 (2005).
    • (2005) Mol. Pharmacol. , vol.68 , pp. 129-136
    • Malik, S.1    Ghosh, M.2    Bonacci, T.M.3    Tall, G.G.4    Smrcka, A.V.5
  • 55
    • 0025878182 scopus 로고
    • Synthetic peptide antisera with determined specificity for G protein α or β subunits
    • S. M. Mumby, A. G. Gilman, Synthetic peptide antisera with determined specificity for G protein α or β subunits. Methods Enzymol. 195, 215-233 (1991).
    • (1991) Methods Enzymol. , vol.195 , pp. 215-233
    • Mumby, S.M.1    Gilman, A.G.2
  • 56
    • 0025724957 scopus 로고
    • q subfamily of guanine nucleotide-binding regulatory protein α subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones
    • q subfamily of guanine nucleotide-binding regulatory protein α subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones. J. Biol. Chem. 266, 20519-20524 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 20519-20524
    • Gutowski, S.1    Smrcka, A.2    Nowak, L.3    Wu, D.G.4    Simon, M.5    Sternweis, P.C.6
  • 57
    • 0025016132 scopus 로고
    • Purification of unique a subunits of GTP-binding regulatory proteins (G proteins) by affinity chromatography with immobilized βγ subunits
    • I. H. Pang, P. C. Sternweis, Purification of unique a subunits of GTP-binding regulatory proteins (G proteins) by affinity chromatography with immobilized βγ subunits. J. Biol. Chem. 265, 18707-18712 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 18707-18712
    • Pang, I.H.1    Sternweis, P.C.2
  • 60
    • 0032481104 scopus 로고    scopus 로고
    • The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes
    • Q. Liu, M. Z. Li, D. Leibham, D. Cortez, S. J. Elledge, The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes. Curr. Biol. 8, 1300-1309 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1300-1309
    • Liu, Q.1    Li, M.Z.2    Leibham, D.3    Cortez, D.4    Elledge, S.J.5
  • 61
    • 0033002084 scopus 로고    scopus 로고
    • Efficient and precise engineering of a 200 kb β-globin human/bacterial artificial chromosome in E. coli DH10B using an inducible homologous recombination system
    • K. Narayanan, R. Williamson, Y. Zhang, A. F. Stewart, P. A. Ioannou, Efficient and precise engineering of a 200 kb β-globin human/bacterial artificial chromosome in E. coli DH10B using an inducible homologous recombination system. Gene Ther. 6, 442-447 (1999).
    • (1999) Gene Ther. , vol.6 , pp. 442-447
    • Narayanan, K.1    Williamson, R.2    Zhang, Y.3    Stewart, A.F.4    Ioannou, P.A.5
  • 62
    • 0030842624 scopus 로고    scopus 로고
    • Homologous recombination based modification in Escherichia coli and germline transmission in transgenic mice of a bacterial artificial chromosome
    • X. W. Yang, P. Model, N. Heintz, Homologous recombination based modification in Escherichia coli and germline transmission in transgenic mice of a bacterial artificial chromosome. Nat. Biotechnol. 15, 859-865 (1997).
    • (1997) Nat. Biotechnol. , vol.15 , pp. 859-865
    • Yang, X.W.1    Model, P.2    Heintz, N.3
  • 63
    • 0031664853 scopus 로고    scopus 로고
    • A new logic for DNA engineering using recombination in Escherichia coli
    • Y. Zhang, F. Buchholz, J. P. P. Muyrers, A. F. Stewart, A new logic for DNA engineering using recombination in Escherichia coli. Nat. Genet. 20, 123-128 (1998).
    • (1998) Nat. Genet. , vol.20 , pp. 123-128
    • Zhang, Y.1    Buchholz, F.2    Muyrers, J.P.P.3    Stewart, A.F.4
  • 65
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • W. Schaffner, C. Weissmann, A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56, 502-514 (1973).
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.