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Volumn 80, Issue 2, 2014, Pages 723-729

pH-Dependent Activation of Streptomyces hygroscopicus Transglutaminase Mediated by Intein

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION PROCESS; ENZYMATIC PROPERTIES; MICROBIAL TRANSGLUTAMINASE; MOLECULAR DYNAMICS SIMULATIONS; PROTEIN-SPLICING; SECONDARY STRUCTURES; STREPTOMYCES HYGROSCOPICUS; TRANSGLUTAMINASES;

EID: 84892582866     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02820-13     Document Type: Article
Times cited : (9)

References (40)
  • 1
    • 0027421103 scopus 로고
    • Intramolecular chaperones and protein folding
    • Shinde U, Inouye M. 1993. Intramolecular chaperones and protein folding. Trends Biochem. Sci. 18:442-446. http://dx.doi.org/10.1016/0968-0004(93)90146-E.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 442-446
    • Shinde, U.1    Inouye, M.2
  • 2
    • 0034490227 scopus 로고    scopus 로고
    • Intramolecular chaperones: polypeptide extensions that modulate protein folding
    • Shinde U, Inouye M. 2000. Intramolecular chaperones: polypeptide extensions that modulate protein folding. Semin. Cell Dev. Biol. 11:35-44. http://dx.doi.org/10.1006/scdb.1999.0349.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 35-44
    • Shinde, U.1    Inouye, M.2
  • 3
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama K, Nio N, Kikuchi Y. 2004. Properties and applications of microbial transglutaminase. Appl. Microbiol. Biotechnol. 64:447-454. http://dx.doi.org/10.1007/s00253-003-1539-5.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 4
    • 79954897827 scopus 로고    scopus 로고
    • Processing and maturation of carboxypeptidase Y and alkaline phosphatase in Schizosaccharomyces pombe
    • Mukaiyama H, Iwaki T, Idiris A, Takegawa K. 2011. Processing and maturation of carboxypeptidase Y and alkaline phosphatase in Schizosaccharomyces pombe. Appl. Microbiol. Biotechnol. 90:203-213. http://dx.doi.org/10.1007/s00253-010-3031-3.
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , pp. 203-213
    • Mukaiyama, H.1    Iwaki, T.2    Idiris, A.3    Takegawa, K.4
  • 5
    • 84870359579 scopus 로고    scopus 로고
    • Regulation of the activities of the mammalian transglutaminase family of enzymes
    • Klöck C, Khosla C. 2012. Regulation of the activities of the mammalian transglutaminase family of enzymes. Protein Sci. 21:1781-1791. http://dx.doi.org/10.1002/pro.2162.
    • (2012) Protein Sci. , vol.21 , pp. 1781-1791
    • Klöck, C.1    Khosla, C.2
  • 6
    • 79851472440 scopus 로고    scopus 로고
    • Activity of maize transglutaminase overexpressed in Escherichia coli inclusion bodies: an alternative to protein refolding
    • Carvajal P, Gibert J, Campos N, Lopera O, Barbera E, Torne JM, Santos M. 2011. Activity of maize transglutaminase overexpressed in Escherichia coli inclusion bodies: an alternative to protein refolding. Biotechnol. Prog. 27:232-240. http://dx.doi.org/10.1002/btpr.538.
    • (2011) Biotechnol. Prog. , vol.27 , pp. 232-240
    • Carvajal, P.1    Gibert, J.2    Campos, N.3    Lopera, O.4    Barbera, E.5    Torne, J.M.6    Santos, M.7
  • 7
    • 77955559551 scopus 로고    scopus 로고
    • Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis
    • Yokoyama K, Utsumi H, Nakamura T, Ogaya D, Shimba N, Suzuki E, Taguchi S. 2010. Screening for improved activity of a transglutaminase from Streptomyces mobaraensis created by a novel rational mutagenesis and random mutagenesis. Appl. Microbiol. Biotechnol. 87:2087-2096. http://dx.doi.org/10.1007/s00253-010-2656-6.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 2087-2096
    • Yokoyama, K.1    Utsumi, H.2    Nakamura, T.3    Ogaya, D.4    Shimba, N.5    Suzuki, E.6    Taguchi, S.7
  • 9
    • 51249102955 scopus 로고    scopus 로고
    • Novel applications for microbial transglutaminase beyond food processing
    • Zhu Y, Tramper J. 2008. Novel applications for microbial transglutaminase beyond food processing. Trends Biotechnol. 26:559-565. http://dx.doi.org/10.1016/j.tibtech.2008.06.006.
    • (2008) Trends Biotechnol. , vol.26 , pp. 559-565
    • Zhu, Y.1    Tramper, J.2
  • 10
    • 0024801107 scopus 로고
    • Purification and characteristics of a novel transglutaminase derived from microorganisms
    • Ando H, Adachi M, Umeda K, Matsuura A, Nonaka M, Uchio R, Tanaka H, Motoki M. 1989. Purification and characteristics of a novel transglutaminase derived from microorganisms. Agric. Biol. Chem. 53: 2613-2617. http://dx.doi.org/10.1271/bbb1961.53.2613.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2613-2617
    • Ando, H.1    Adachi, M.2    Umeda, K.3    Matsuura, A.4    Nonaka, M.5    Uchio, R.6    Tanaka, H.7    Motoki, M.8
  • 11
    • 77749268141 scopus 로고    scopus 로고
    • Microbial transglutaminase production: understanding the mechanism
    • Zhang DX, Zhu Y, Chen J. 2010. Microbial transglutaminase production: understanding the mechanism. Biotechnol. Genet. Eng. Rev. 26:205-221.
    • (2010) Biotechnol. Genet. Eng. Rev. , vol.26 , pp. 205-221
    • Zhang, D.X.1    Zhu, Y.2    Chen, J.3
  • 12
    • 84876461880 scopus 로고    scopus 로고
    • Recent progress in intein research: from mechanism to directed evolution and applications
    • Volkmann G, Mootz H. 2013. Recent progress in intein research: from mechanism to directed evolution and applications. Cell. Mol. Life Sci. 70:1185-1206. http://dx.doi.org/10.1007/s00018-012-1120-4.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1185-1206
    • Volkmann, G.1    Mootz, H.2
  • 13
    • 18144439565 scopus 로고    scopus 로고
    • Protein trans-splicing and functional mini-inteins of a cyanobacterial dnaB intein
    • Wu H, Xu MQ, Liu XQ. 1998. Protein trans-splicing and functional mini-inteins of a cyanobacterial dnaB intein. Biochim. Biophys. Acta 1387: 422-432. http://dx.doi.org/10.1016/S0167-4838(98)00157-5.
    • (1998) Biochim. Biophys. Acta , vol.1387 , pp. 422-432
    • Wu, H.1    Xu, M.Q.2    Liu, X.Q.3
  • 14
    • 0033614484 scopus 로고    scopus 로고
    • Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: facile production of protein building blocks for protein ligation
    • Mathys S, Evans TC, Chute IC, Wu H, Chong S, Benner J, Liu XQ, Xu MQ. 1999. Characterization of a self-splicing mini-intein and its conversion into autocatalytic N- and C-terminal cleavage elements: facile production of protein building blocks for protein ligation. Gene 231:1-13. http://dx.doi.org/10.1016/S0378-1119(99)00103-1.
    • (1999) Gene , vol.231 , pp. 1-13
    • Mathys, S.1    Evans, T.C.2    Chute, I.C.3    Wu, H.4    Chong, S.5    Benner, J.6    Liu, X.Q.7    Xu, M.Q.8
  • 15
    • 84862906434 scopus 로고    scopus 로고
    • Production, purification, and characterization of the cecropin from Plutella xylostella, pxCECA1, using an intein-induced self-cleavable system in Escherichia coli
    • Wang H, Meng XL, Xu JP, Wang J, Ma CW. 2012. Production, purification, and characterization of the cecropin from Plutella xylostella, pxCECA1, using an intein-induced self-cleavable system in Escherichia coli. Appl. Microbiol. Biotechnol. 94:1031-1039. http://dx.doi.org/10.1007/s00253-011-3863-5.
    • (2012) Appl. Microbiol. Biotechnol. , vol.94 , pp. 1031-1039
    • Wang, H.1    Meng, X.L.2    Xu, J.P.3    Wang, J.4    Ma, C.W.5
  • 16
    • 80051871023 scopus 로고    scopus 로고
    • An improved particle bombardment for the generation of transgenic plants by direct immobilization of releasable Tn5 transposases onto gold particles
    • Wu J, Du H, Liao X, Zhao Y, Li L, Yang L. 2011. An improved particle bombardment for the generation of transgenic plants by direct immobilization of releasable Tn5 transposases onto gold particles. Plant Mol. Biol. 77:117-127. http://dx.doi.org/10.1007/s11103-011-9798-5.
    • (2011) Plant Mol. Biol. , vol.77 , pp. 117-127
    • Wu, J.1    Du, H.2    Liao, X.3    Zhao, Y.4    Li, L.5    Yang, L.6
  • 17
    • 77955030266 scopus 로고    scopus 로고
    • Intein-mediated cyclization of randomized peptides in the periplasm of Escherichia coli and their extracellular secretion
    • Deschuyteneer G, Garcia S, Michiels B, Baudoux B, Degand H, Morsomme P, Soumillion P. 2010. Intein-mediated cyclization of randomized peptides in the periplasm of Escherichia coli and their extracellular secretion. ACS Chem. Biol. 5:691-700. http://dx.doi.org/10.1021/cb100072u.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 691-700
    • Deschuyteneer, G.1    Garcia, S.2    Michiels, B.3    Baudoux, B.4    Degand, H.5    Morsomme, P.6    Soumillion, P.7
  • 18
    • 14844283810 scopus 로고    scopus 로고
    • Recombinant protein secretion in Escherichia coli
    • Mergulhão FJM, Summers DK, Monteiro GA. 2005. Recombinant protein secretion in Escherichia coli. Biotechnol. Adv. 23:177-202. http://dx.doi.org/10.1016/j.biotechadv.2004.11.003.
    • (2005) Biotechnol. Adv. , vol.23 , pp. 177-202
    • Mergulhão, F.J.M.1    Summers, D.K.2    Monteiro, G.A.3
  • 19
    • 67649625535 scopus 로고    scopus 로고
    • Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates.
    • Magnusdottir A, Johansson I, Dahlgren LG, Nordlund P, Berglund H. 2009 Enabling IMAC purification of low abundance recombinant proteins from E. coli lysates. Nat. Methods 6:477-478. http://dx.doi.org/10.1038/nmeth0709-477.
    • (2009) Nat. Methods , vol.6 , pp. 477-478
    • Magnusdottir, A.1    Johansson, I.2    Dahlgren, L.G.3    Nordlund, P.4    Berglund, H.5
  • 20
    • 2542459428 scopus 로고    scopus 로고
    • A modified osmotic shock for periplasmic release of a recombinant creatinase from Escherichia coli
    • Chen Y-C, Chen L-A, Chen S-J, Chang M-C, Chen T-L. 2004. A modified osmotic shock for periplasmic release of a recombinant creatinase from Escherichia coli. Biochem. Eng. J. 19:211-215. http://dx.doi.org/10.1016/j.bej.2004.03.001.
    • (2004) Biochem. Eng. J. , vol.19 , pp. 211-215
    • Chen, Y.-C.1    Chen, L.-A.2    Chen, S.-J.3    Chang, M.-C.4    Chen, T.-L.5
  • 21
    • 34447248556 scopus 로고    scopus 로고
    • Purification and characterization of transglutaminase from a newly isolated Streptomyces hygroscopicus
    • Cui L, Du GC, Zhang DX, Liu H, Chen J. 2007. Purification and characterization of transglutaminase from a newly isolated Streptomyces hygroscopicus. Food Chem. 105:612-618. http://dx.doi.org/10.1016/j.foodchem.2007.04.020.
    • (2007) Food Chem. , vol.105 , pp. 612-618
    • Cui, L.1    Du, G.C.2    Zhang, D.X.3    Liu, H.4    Chen, J.5
  • 22
    • 0000292314 scopus 로고
    • The relationship between Michaelis constants, maximum velocities and the equilibrium constant for an enzyme-catalyzed reaction
    • Alberty RA. 1953. The relationship between Michaelis constants, maximum velocities and the equilibrium constant for an enzyme-catalyzed reaction. J. Am. Chem. Soc. 75:1928-1932. http://dx.doi.org/10.1021/ja01104a045.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 1928-1932
    • Alberty, R.A.1
  • 23
    • 80054093224 scopus 로고    scopus 로고
    • The pro-region of Streptomyces hygroscopicus transglutaminase affects its secretion by Escherichia coli
    • Liu S, Zhang D, Wang M, Cui W, Chen K, Liu Y, Du G, Chen J, Zhou Z. 2011. The pro-region of Streptomyces hygroscopicus transglutaminase affects its secretion by Escherichia coli. FEMS Microbiol. Lett. 324:98-105. http://dx.doi.org/10.1111/j.1574-6968.2011.02387.x.
    • (2011) FEMS Microbiol. Lett. , vol.324 , pp. 98-105
    • Liu, S.1    Zhang, D.2    Wang, M.3    Cui, W.4    Chen, K.5    Liu, Y.6    Du, G.7    Chen, J.8    Zhou, Z.9
  • 24
    • 79953169882 scopus 로고    scopus 로고
    • Crystal structure and inhibition studies of transglutaminase from Streptomyces mobaraense.
    • Yang MT, Chang CH, Wang JM, Wu TK, Wang YK, Chang CY, Li TT. Crystal structure and inhibition studies of transglutaminase from Streptomyces mobaraense. J. Biol. Chem. 286:7301-7307. http://dx.doi.org/10.1074/jbc.M110.203315.
    • J. Biol. Chem. , vol.286 , pp. 7301-7307
    • Yang, M.T.1    Chang, C.H.2    Wang, J.M.3    Wu, T.K.4    Wang, Y.K.5    Chang, C.Y.6    Li, T.T.7
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291. http://dx.doi.org/10.1107/S0021889892009944.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 70350502592 scopus 로고    scopus 로고
    • Controllable protein cleavages through intein fragment complementation
    • Volkmann G, Sun WC, Liu XQ. 2009. Controllable protein cleavages through intein fragment complementation. Protein Sci. 18:2393-2402. http://dx.doi.org/10.1002/pro.249.
    • (2009) Protein Sci. , vol.18 , pp. 2393-2402
    • Volkmann, G.1    Sun, W.C.2    Liu, X.Q.3
  • 28
    • 0037165610 scopus 로고    scopus 로고
    • Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site
    • Shimba N, Shinohara M, Yokoyama K, Kashiwagi T, Ishikawa K, Ejima D, Suzuki E. 2002. Enhancement of transglutaminase activity by NMR identification of its flexible residues affecting the active site. FEBS Lett. 517:175-179. http://dx.doi.org/10.1016/S0014-5793(02)02616-9.
    • (2002) FEBS Lett. , vol.517 , pp. 175-179
    • Shimba, N.1    Shinohara, M.2    Yokoyama, K.3    Kashiwagi, T.4    Ishikawa, K.5    Ejima, D.6    Suzuki, E.7
  • 29
    • 29144455402 scopus 로고    scopus 로고
    • Heterologous leaky production of transglutaminase in Lactococcus lactis significantly enhances the growth performance of the host
    • Fu RY, Chen J, Li Y. 2005. Heterologous leaky production of transglutaminase in Lactococcus lactis significantly enhances the growth performance of the host. Appl. Environ. Microbiol. 71:8911-8919. http://dx.doi.org/10.1128/AEM.71.12.8911-8919.2005.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 8911-8919
    • Fu, R.Y.1    Chen, J.2    Li, Y.3
  • 30
    • 84155173326 scopus 로고    scopus 로고
    • The order of expression is a key factor in the production of active transglutaminase in Escherichia coli by co-expression with its propeptide.
    • Liu S, Zhang D, Wang M, Cui W, Chen K, Du G, Chen J, Zhou Z. 2011 The order of expression is a key factor in the production of active transglutaminase in Escherichia coli by co-expression with its propeptide. Microb. Cell Fact. 10:112. http://dx.doi.org/10.1186/1475-2859-10-112.
    • (2011) Microb. Cell Fact. , vol.10 , pp. 112
    • Liu, S.1    Zhang, D.2    Wang, M.3    Cui, W.4    Chen, K.5    Du, G.6    Chen, J.7    Zhou, Z.8
  • 31
    • 0037114005 scopus 로고    scopus 로고
    • Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense
    • Kashiwagi T, Yokoyama K, Ishikawa K, Ono K, Ejima D, Matsui H, Suzuki E. 2002. Crystal structure of microbial transglutaminase from Streptoverticillium mobaraense. J. Biol. Chem. 277:44252-44260. http://dx.doi.org/10.1074/jbc.M203933200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44252-44260
    • Kashiwagi, T.1    Yokoyama, K.2    Ishikawa, K.3    Ono, K.4    Ejima, D.5    Matsui, H.6    Suzuki, E.7
  • 32
    • 81855226607 scopus 로고    scopus 로고
    • A two-step refolding of acid-denatured microbial transglutaminase escaping from the aggregation- prone intermediate
    • Suzuki M, Yokoyama K-I, Lee Y-H, Goto Y. 2011. A two-step refolding of acid-denatured microbial transglutaminase escaping from the aggregation- prone intermediate. Biochemistry (Mosc.) 50:10390-10398. http://dx.doi.org/10.1021/bi2010619.
    • (2011) Biochemistry (Mosc.) , vol.50 , pp. 10390-10398
    • Suzuki, M.1    Yokoyama, K.-I.2    Lee, Y.-H.3    Goto, Y.4
  • 33
    • 84863916249 scopus 로고    scopus 로고
    • A back hydrogen exchange procedure via the acid-unfolded state for a large protein
    • Suzuki M, Sakurai K, Lee Y-H, Ikegami T, Yokoyama K, Goto Y. 2012. A back hydrogen exchange procedure via the acid-unfolded state for a large protein. Biochemistry (Mosc.) 51:5564-5570. http://dx.doi.org/10.1021/bi300495p.
    • (2012) Biochemistry (Mosc.) , vol.51 , pp. 5564-5570
    • Suzuki, M.1    Sakurai, K.2    Lee, Y.-H.3    Ikegami, T.4    Yokoyama, K.5    Goto, Y.6
  • 34
    • 0031973808 scopus 로고    scopus 로고
    • Genetic instability of the Streptomyces chromosome
    • Volff JN, Altenbuchner J. 1998. Genetic instability of the Streptomyces chromosome. Mol. Microbiol. 27:239-246. http://dx.doi.org/10.1046/j.1365-2958.1998.00652.x.
    • (1998) Mol. Microbiol. , vol.27 , pp. 239-246
    • Volff, J.N.1    Altenbuchner, J.2
  • 35
    • 0037229834 scopus 로고    scopus 로고
    • Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus
    • Kikuchi Y, Date M, Yokoyama K, Umezawa Y, Matsui H. 2003. Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus. Appl. Environ. Microbiol. 69:358-366. http://dx.doi.org/10.1128/AEM.69.1.358-366.2003.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 358-366
    • Kikuchi, Y.1    Date, M.2    Yokoyama, K.3    Umezawa, Y.4    Matsui, H.5
  • 36
    • 0038219967 scopus 로고    scopus 로고
    • Production of native-type Streptoverticillium mobaraense transglutaminase in Corynebacterium glutamicum
    • Date M, Yokoyama K, Umezawa Y, Matsui H, Kikuchi Y. 2003. Production of native-type Streptoverticillium mobaraense transglutaminase in Corynebacterium glutamicum. Appl. Environ. Microbiol. 69:3011-3014. http://dx.doi.org/10.1128/AEM.69.5.3011-3014.2003.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3011-3014
    • Date, M.1    Yokoyama, K.2    Umezawa, Y.3    Matsui, H.4    Kikuchi, Y.5
  • 37
    • 9244221174 scopus 로고    scopus 로고
    • The pro-peptide of Streptomyces mobaraensis transglutaminase functions in cis and in trans to mediate efficient secretion of active enzyme from methylotropic yeasts
    • Yurimoto H, Yamane M, Kikuchi Y, Matsui H, Kato N, Sakai Y. 2004. The pro-peptide of Streptomyces mobaraensis transglutaminase functions in cis and in trans to mediate efficient secretion of active enzyme from methylotropic yeasts. Biosci. Biotechnol. Biochem. 68:2058-2069. http://dx.doi.org/10.1271/bbb.68.2058.
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 2058-2069
    • Yurimoto, H.1    Yamane, M.2    Kikuchi, Y.3    Matsui, H.4    Kato, N.5    Sakai, Y.6
  • 38
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sørensen HP, Mortensen KK. 2005. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115:113- 128. http://dx.doi.org/10.1016/j.jbiotec.2004.08.004.
    • (2005) J. Biotechnol. , vol.115
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 39
    • 77949342622 scopus 로고    scopus 로고
    • A novel high-throughput screening method for microbial transglutaminases with high specificity toward Gln141 of human growth hormone
    • Zhao X, Shaw AC, Wang J, Chang C-C, Deng J, Su J. 2010. A novel high-throughput screening method for microbial transglutaminases with high specificity toward Gln141 of human growth hormone. J. Biomol. Screen. 15:206-212. http://dx.doi.org/10.1177/1087057109356206.
    • (2010) J. Biomol. Screen. , vol.15 , pp. 206-212
    • Zhao, X.1    Shaw, A.C.2    Wang, J.3    Chang, C.-C.4    Deng, J.5    Su, J.6
  • 40
    • 77958153489 scopus 로고    scopus 로고
    • Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery
    • Yu HH, Nakase I, Pujals S, Hirose H, Tanaka G, Katayama S, Imanishi M, Futaki S. 2010. Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery. Biochim. Biophys. Acta 1798:2249-2257. http://dx.doi.org/10.1016/j.bbamem.2010.02.003.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 2249-2257
    • Yu, H.H.1    Nakase, I.2    Pujals, S.3    Hirose, H.4    Tanaka, G.5    Katayama, S.6    Imanishi, M.7    Futaki, S.8


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