메뉴 건너뛰기




Volumn 111, Issue 7, 2014, Pages 2728-2733

Structural basis for nuclear import of splicing factors by human Transportin 3

Author keywords

Host factor; Importin; SR protein; Transportin SR

Indexed keywords

ALTERNATIV SPLICING FACTOR; ARGININE; CARRIER PROTEIN; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 6; GUANOSINE TRIPHOSPHATASE; KARYOPHERIN BETA; NUCLEIC ACID BINDING PROTEIN; RNA; SERINE; SPLICING FACTOR 2; TRANSPORTIN 3; UNCLASSIFIED DRUG;

EID: 84894305729     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1320755111     Document Type: Article
Times cited : (109)

References (54)
  • 1
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart M (2007) Molecular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 8(3):195-208.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.3 , pp. 195-208
    • Stewart, M.1
  • 2
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Görlich D, Panté N, Kutay U, Aebi U, Bischoff FR (1996) Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J 15(20):5584-5594.
    • (1996) EMBO J , vol.15 , Issue.20 , pp. 5584-5594
    • Görlich, D.1    Panté, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 3
    • 0034913423 scopus 로고    scopus 로고
    • Importin-beta-like nuclear transport receptors
    • reviews 3008.1-3008.9
    • Strom AC, Weis K (2001) Importin-beta-like nuclear transport receptors. Genome Biol 2(6): Reviews 3008.1-3008.9.
    • (2001) Genome Biol , vol.2 , Issue.6
    • Strom, A.C.1    Weis, K.2
  • 4
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook A, Bono F, Jinek M, Conti E (2007) Structural biology of nucleocytoplasmic transport. Annu Rev Biochem 76:647-671.
    • (2007) Annu Rev Biochem , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 5
    • 77951299111 scopus 로고    scopus 로고
    • Nuclear export complexes in the frame
    • Cook AG, Conti E (2010) Nuclear export complexes in the frame. Curr Opin Struct Biol 20(2):247-252.
    • (2010) Curr Opin Struct Biol , vol.20 , Issue.2 , pp. 247-252
    • Cook, A.G.1    Conti, E.2
  • 6
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: Master regulators of gene expression
    • Long JC, Caceres JF (2009) The SR protein family of splicing factors: Master regulators of gene expression. Biochem J 417(1):15-27.
    • (2009) Biochem J , vol.417 , Issue.1 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 7
    • 0025827463 scopus 로고
    • Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators
    • Ge H, Zuo P, Manley JL (1991) Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators. Cell 66(2):373-382.
    • (1991) Cell , vol.66 , Issue.2 , pp. 373-382
    • Ge, H.1    Zuo, P.2    Manley, J.L.3
  • 8
    • 0025743575 scopus 로고
    • Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators
    • Krainer AR, Mayeda A, Kozak D, Binns G (1991) Functional expression of cloned human splicing factor SF2: Homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators. Cell 66(2):383-394.
    • (1991) Cell , vol.66 , Issue.2 , pp. 383-394
    • Krainer, A.R.1    Mayeda, A.2    Kozak, D.3    Binns, G.4
  • 9
    • 0025115231 scopus 로고
    • Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus
    • Fu XD, Maniatis T (1990) Factor required for mammalian spliceosome assembly is localized to discrete regions in the nucleus. Nature 343(6257):437-441.
    • (1990) Nature , vol.343 , Issue.6257 , pp. 437-441
    • Fu, X.D.1    Maniatis, T.2
  • 10
    • 0026716104 scopus 로고
    • SR proteins: A conserved family of premRNA splicing factors
    • Zahler AM, Lane WS, Stolk JA, Roth MB (1992) SR proteins: A conserved family of premRNA splicing factors. Genes Dev 6(5):837-847.
    • (1992) Genes Dev , vol.6 , Issue.5 , pp. 837-847
    • Zahler, A.M.1    Lane, W.S.2    Stolk, J.A.3    Roth, M.B.4
  • 11
  • 12
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui JF, Lane WS, Fu XD (1994) A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature 369(6482):678-682.
    • (1994) Nature , vol.369 , Issue.6482 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 13
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill K, et al. (1996) The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. EMBO J 15(2):265-275.
    • (1996) EMBO J , vol.15 , Issue.2 , pp. 265-275
    • Colwill, K.1
  • 14
    • 0032559642 scopus 로고    scopus 로고
    • SRPK2: A differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells
    • Wang HY, et al. (1998) SRPK2: A differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. J Cell Biol 140(4):737-750.
    • (1998) J Cell Biol , vol.140 , Issue.4 , pp. 737-750
    • Wang, H.Y.1
  • 15
    • 0242268460 scopus 로고    scopus 로고
    • Processive phosphorylation of alternative splicing factor/splicing factor 2
    • Aubol BE, et al. (2003) Processive phosphorylation of alternative splicing factor/splicing factor 2. Proc Natl Acad Sci USA 100(22):12601-12606.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.22 , pp. 12601-12606
    • Aubol, B.E.1
  • 16
    • 29244449634 scopus 로고    scopus 로고
    • Mass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty
    • Velazquez-Dones A, et al. (2005) Mass spectrometric and kinetic analysis of ASF/SF2 phosphorylation by SRPK1 and Clk/Sty. J Biol Chem 280(50):41761-41768.
    • (2005) J Biol Chem , vol.280 , Issue.50 , pp. 41761-41768
    • Velazquez-Dones, A.1
  • 17
    • 31944432341 scopus 로고    scopus 로고
    • Regulated cellular partitioning of SR protein-specific kinases in mammalian cells
    • Ding JH, et al. (2006) Regulated cellular partitioning of SR protein-specific kinases in mammalian cells. Mol Biol Cell 17(2):876-885.
    • (2006) Mol Biol Cell , vol.17 , Issue.2 , pp. 876-885
    • Ding, J.H.1
  • 18
    • 0028043718 scopus 로고
    • Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism
    • Mermoud JE, Cohen PT, Lamond AI (1994) Regulation of mammalian spliceosome assembly by a protein phosphorylation mechanism. EMBO J 13(23):5679-5688.
    • (1994) EMBO J , vol.13 , Issue.23 , pp. 5679-5688
    • Mermoud, J.E.1    Cohen, P.T.2    Lamond, A.I.3
  • 19
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao SH, Manley JL (1997) Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev 11(3):334-344.
    • (1997) Genes Dev , vol.11 , Issue.3 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 20
    • 0031468240 scopus 로고    scopus 로고
    • Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro
    • CaoW, Jamison SF, Garcia-BlancoMA (1997) Both phosphorylation and dephosphorylation of ASF/SF2 are required for pre-mRNA splicing in vitro. RNA 3(12):1456-1467.
    • (1997) RNA , vol.3 , Issue.12 , pp. 1456-1467
    • Cao, W.1    Jamison, S.F.2    Garcia-Blanco, M.A.3
  • 21
    • 0033553882 scopus 로고    scopus 로고
    • Transportin-SR, a nuclear import receptor for SR proteins
    • Kataoka N, Bachorik JL, Dreyfuss G (1999) Transportin-SR, a nuclear import receptor for SR proteins. J Cell Biol 145(6):1145-1152.
    • (1999) J Cell Biol , vol.145 , Issue.6 , pp. 1145-1152
    • Kataoka, N.1    Bachorik, J.L.2    Dreyfuss, G.3
  • 22
    • 0034677884 scopus 로고    scopus 로고
    • A human importin-beta family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins
    • Lai MC, Lin RI, Huang SY, Tsai CW, Tarn WY (2000) A human importin-beta family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins. J Biol Chem 275(11):7950-7957.
    • (2000) J Biol Chem , vol.275 , Issue.11 , pp. 7950-7957
    • Lai, M.C.1    Lin, R.I.2    Huang, S.Y.3    Tsai, C.W.4    Tarn, W.Y.5
  • 23
    • 0035964258 scopus 로고    scopus 로고
    • Transportin-SR2 mediates nuclear import of phosphorylated SR proteins
    • Lai MC, Lin RI, Tarn WY (2001) Transportin-SR2 mediates nuclear import of phosphorylated SR proteins. Proc Natl Acad Sci USA 98(18):10154-10159.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.18 , pp. 10154-10159
    • Lai, M.C.1    Lin, R.I.2    Tarn, W.Y.3
  • 24
    • 0032522343 scopus 로고    scopus 로고
    • Mtr10p functions as a nuclear import receptor for the mRNAbinding protein Npl3p
    • Senger B, et al. (1998) Mtr10p functions as a nuclear import receptor for the mRNAbinding protein Npl3p. EMBO J 17(8):2196-2207.
    • (1998) EMBO J , vol.17 , Issue.8 , pp. 2196-2207
    • Senger, B.1
  • 25
    • 0036329228 scopus 로고    scopus 로고
    • A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1
    • Allemand E, Dokudovskaya S, Bordonné R, Tazi J (2002) A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1. Mol Biol Cell 13(7):2436-2447.
    • (2002) Mol Biol Cell , vol.13 , Issue.7 , pp. 2436-2447
    • Allemand, E.1    Dokudovskaya, S.2    Bordonné, R.3    Tazi, J.4
  • 26
    • 79959831970 scopus 로고    scopus 로고
    • Transportin-SR is required for proper splicing of resistance genes and plant immunity
    • Xu S, et al. (2011) Transportin-SR is required for proper splicing of resistance genes and plant immunity. PLoS Genet 7(6):e1002159.
    • (2011) PLoS Genet , vol.7 , Issue.6
    • Xu, S.1
  • 27
    • 39349097864 scopus 로고    scopus 로고
    • Identification of host proteins required for HIV infection through a functional genomic screen
    • Brass AL, et al. (2008) Identification of host proteins required for HIV infection through a functional genomic screen. Science 319(5865):921-926.
    • (2008) Science , vol.319 , Issue.5865 , pp. 921-926
    • Brass, A.L.1
  • 28
    • 52949130695 scopus 로고    scopus 로고
    • Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication
    • König R, et al. (2008) Global analysis of host-pathogen interactions that regulate early-stage HIV-1 replication. Cell 135(1):49-60.
    • (2008) Cell , vol.135 , Issue.1 , pp. 49-60
    • König, R.1
  • 29
    • 49649105669 scopus 로고    scopus 로고
    • Transportin-SR2 imports HIV into the nucleus
    • Christ F, et al. (2008) Transportin-SR2 imports HIV into the nucleus. Curr Biol 18(16): 1192-1202.
    • (2008) Curr Biol , vol.18 , Issue.16 , pp. 1192-1202
    • Christ, F.1
  • 30
    • 82655186588 scopus 로고    scopus 로고
    • Inhibition of HIV-1 infection by TNPO3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus
    • De Iaco A, Luban J (2011) Inhibition of HIV-1 infection by TNPO3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus. Retrovirology 8:98.
    • (2011) Retrovirology , vol.8 , pp. 98
    • De Iaco, A.1    Luban, J.2
  • 31
    • 84873720427 scopus 로고    scopus 로고
    • TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm
    • De Iaco A, et al. (2013) TNPO3 protects HIV-1 replication from CPSF6-mediated capsid stabilization in the host cell cytoplasm. Retrovirology 10:20.
    • (2013) Retrovirology , vol.10 , pp. 20
    • De Iaco, A.1
  • 32
    • 72849130164 scopus 로고    scopus 로고
    • The requirement for cellular transportin 3 (TNPO3 or TRNSR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase
    • Krishnan L, et al. (2010) The requirement for cellular transportin 3 (TNPO3 or TRNSR2) during infection maps to human immunodeficiency virus type 1 capsid and not integrase. J Virol 84(1):397-406.
    • (2010) J Virol , vol.84 , Issue.1 , pp. 397-406
    • Krishnan, L.1
  • 33
    • 84861323711 scopus 로고    scopus 로고
    • TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core
    • Valle-Casuso JC, et al. (2012) TNPO3 is required for HIV-1 replication after nuclear import but prior to integration and binds the HIV-1 core. J Virol 86(10):5931-5936.
    • (2012) J Virol , vol.86 , Issue.10 , pp. 5931-5936
    • Valle-Casuso, J.C.1
  • 34
    • 77749342887 scopus 로고    scopus 로고
    • Flexible use of nuclear import pathways by HIV-1
    • Lee K, et al. (2010) Flexible use of nuclear import pathways by HIV-1. Cell Host Microbe 7(3):221-233.
    • (2010) Cell Host Microbe , vol.7 , Issue.3 , pp. 221-233
    • Lee, K.1
  • 35
    • 84866162552 scopus 로고    scopus 로고
    • CPSF6 defines a conserved capsid interface that modulates HIV-1 replication
    • Price AJ, et al. (2012) CPSF6 defines a conserved capsid interface that modulates HIV-1 replication. PLoS Pathog 8(8):e1002896.
    • (2012) PLoS Pathog , vol.8 , Issue.8
    • Price, A.J.1
  • 37
    • 74749084019 scopus 로고    scopus 로고
    • Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13
    • Bono F, Cook AG, Grünwald M, Ebert J, Conti E (2010) Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13. Mol Cell 37(2):211-222.
    • (2010) Mol Cell , vol.37 , Issue.2 , pp. 211-222
    • Bono, F.1    Cook, A.G.2    Grünwald, M.3    Ebert, J.4    Conti, E.5
  • 38
    • 78751629243 scopus 로고    scopus 로고
    • Structure of Importin13-Ubc9 complex: Nuclear import and release of a key regulator of sumoylation
    • Grünwald M, Bono F (2011) Structure of Importin13-Ubc9 complex: Nuclear import and release of a key regulator of sumoylation. EMBO J 30(2):427-438.
    • (2011) EMBO J , vol.30 , Issue.2 , pp. 427-438
    • Grünwald, M.1    Bono, F.2
  • 39
    • 84875467016 scopus 로고    scopus 로고
    • Structural basis for the nuclear export activity of Importin13
    • Grünwald M, Lazzaretti D, Bono F (2013) Structural basis for the nuclear export activity of Importin13. EMBO J 32(6):899-913.
    • (2013) EMBO J , vol.32 , Issue.6 , pp. 899-913
    • Grünwald, M.1    Lazzaretti, D.2    Bono, F.3
  • 40
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade MA, Bork P (1995) HEAT repeats in the Huntington's disease protein. Nat Genet 11(2):115-116.
    • (1995) Nat Genet , vol.11 , Issue.2 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 41
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani G, Petosa C, Weis K, Müller CW (1999) Structure of importin-beta bound to the IBB domain of importin-alpha. Nature 399(6733):221-229.
    • (1999) Nature , vol.399 , Issue.6733 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Müller, C.W.4
  • 42
    • 9744248734 scopus 로고    scopus 로고
    • Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex
    • Petosa C, et al. (2004) Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol Cell 16(5):761-775.
    • (2004) Mol Cell , vol.16 , Issue.5 , pp. 761-775
    • Petosa, C.1
  • 43
    • 84867247847 scopus 로고    scopus 로고
    • Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2)
    • Larue R, et al. (2012) Interaction of the HIV-1 intasome with transportin 3 protein (TNPO3 or TRN-SR2). J Biol Chem 287(41):34044-34058.
    • (2012) J Biol Chem , vol.287 , Issue.41 , pp. 34044-34058
    • Larue, R.1
  • 44
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherinbeta2-Ran x GppNHp
    • Chook YM, Blobel G (1999) Structure of the nuclear transport complex karyopherinbeta2-Ran x GppNHp. Nature 399(6733):230-237.
    • (1999) Nature , vol.399 , Issue.6733 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 45
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-Importin beta interaction at 2.3 A resolution
    • Vetter IR, Arndt A, Kutay U, Görlich D, Wittinghofer A (1999) Structural view of the Ran-Importin beta interaction at 2.3 A resolution. Cell 97(5):635-646.
    • (1999) Cell , vol.97 , Issue.5 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Görlich, D.4    Wittinghofer, A.5
  • 46
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A (2001) The guanine nucleotide-binding switch in three dimensions. Science 294(5545):1299-1304.
    • (2001) Science , vol.294 , Issue.5545 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 47
    • 0034146376 scopus 로고    scopus 로고
    • Functional coexpression of serine protein kinase SRPK1 and its substrate ASF/SF2 in Escherichia coli
    • Yue BG, Ajuh P, Akusjärvi G, Lamond AI, Kreivi JP (2000) Functional coexpression of serine protein kinase SRPK1 and its substrate ASF/SF2 in Escherichia coli. Nucleic Acids Res 28(5):E14.
    • (2000) Nucleic Acids Res , vol.28 , Issue.5
    • Yue, B.G.1    Ajuh, P.2    Akusjärvi, G.3    Lamond, A.I.4    Kreivi, J.P.5
  • 48
    • 84863255704 scopus 로고    scopus 로고
    • Evolution of SR protein and hnRNP splicing regulatory factors
    • Busch A, Hertel KJ (2012) Evolution of SR protein and hnRNP splicing regulatory factors. Wiley Interdiscip Rev RNA 3(1):1-12.
    • (2012) Wiley Interdiscip Rev RNA , vol.3 , Issue.1 , pp. 1-12
    • Busch, A.1    Hertel, K.J.2
  • 49
    • 80052336130 scopus 로고    scopus 로고
    • Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration
    • Zhou L, et al. (2011) Transportin 3 promotes a nuclear maturation step required for efficient HIV-1 integration. PLoS Pathog 7(8):e1002194.
    • (2011) PLoS Pathog , vol.7 , Issue.8
    • Zhou, L.1
  • 50
    • 84876687575 scopus 로고    scopus 로고
    • The ability of TNPO3-depleted cells to inhibit HIV-1 infection requires CPSF6
    • Fricke T, et al. (2013) The ability of TNPO3-depleted cells to inhibit HIV-1 infection requires CPSF6. Retrovirology 10:46.
    • (2013) Retrovirology , vol.10 , pp. 46
    • Fricke, T.1
  • 51
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , Issue.PART 4 , pp. 658-674
    • McCoy, A.J.1
  • 52
    • 40649092847 scopus 로고    scopus 로고
    • A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1
    • Ngo JC, et al. (2008) A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1. Mol Cell 29(5):563-576.
    • (2008) Mol Cell , vol.29 , Issue.5 , pp. 563-576
    • Ngo, J.C.1
  • 53
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 54
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 1 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.