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Volumn 11, Issue 4, 2004, Pages 330-337

The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 4G; MESSENGER RNA; NUCLEIC ACID; PROTEIN; RIBOSOME RNA; UNCLASSIFIED DRUG; UP FRAMESHIFT PROTEIN 2; UP FRAMESHIFT PROTEIN 3;

EID: 1842473091     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb741     Document Type: Article
Times cited : (157)

References (49)
  • 1
    • 0036677083 scopus 로고    scopus 로고
    • mRNA surveillance: The perfect persist
    • Wagner, E. & Lykke-Andersen, J. mRNA surveillance: the perfect persist. J. Cell Sci. 115, 3033-3038 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 3033-3038
    • Wagner, E.1    Lykke-Andersen, J.2
  • 2
    • 0034704201 scopus 로고    scopus 로고
    • Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon
    • Lykke-Andersen, J., Shu, M.D. & Steitz, J.A. Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell 103, 1121-1131 (2000).
    • (2000) Cell , vol.103 , pp. 1121-1131
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 3
    • 0034460323 scopus 로고    scopus 로고
    • Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes
    • Mendell, J.T., Medghalchi, S.M., Lake, R.G., Noensie, E.N. & Dietz, H.C. Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes. Mol. Cell. Biol. 20, 8944-8957 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8944-8957
    • Mendell, J.T.1    Medghalchi, S.M.2    Lake, R.G.3    Noensie, E.N.4    Dietz, H.C.5
  • 4
    • 0034751160 scopus 로고    scopus 로고
    • Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4)
    • Serin, G., Gersappe, A., Black, J.D., Aronoff, R. & Maquat, L.E. Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4). Mol. Cell. Biol. 21, 209-223 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 209-223
    • Serin, G.1    Gersappe, A.2    Black, J.D.3    Aronoff, R.4    Maquat, L.E.5
  • 6
    • 0037766047 scopus 로고    scopus 로고
    • A novel mode of RBD-protein recognition in the Y14-Mago complex
    • Fribourg, S., Gatfield, D., Izaurralde, E. & Conti, E. A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat. Struct. Biol. 10, 433-439 (2003).
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 433-439
    • Fribourg, S.1    Gatfield, D.2    Izaurralde, E.3    Conti, E.4
  • 7
    • 0042025014 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in Drosophila: At the intersection of the yeast and mammalian pathways
    • Gatfield, D., Unterholzner, L., Ciccarelli, F.D., Bork, P. & Izaurralde, E. Nonsense-mediated mRNA decay in Drosophila: at the intersection of the yeast and mammalian pathways. EMBO J. 22, 3960-3970 (2003).
    • (2003) EMBO J. , vol.22 , pp. 3960-3970
    • Gatfield, D.1    Unterholzner, L.2    Ciccarelli, F.D.3    Bork, P.4    Izaurralde, E.5
  • 8
    • 0035933889 scopus 로고    scopus 로고
    • Cloning of a novel phosphatidylinositol kinase-related kinase: Characterization of the human SMG-1 RNA surveillance protein
    • Denning, G., Jamieson, L., Maquat, L.E., Thompson, E.A. & Fields, A.P. Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein. J. Biol. Chem. 276, 22709-22714 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 22709-22714
    • Denning, G.1    Jamieson, L.2    Maquat, L.E.3    Thompson, E.A.4    Fields, A.P.5
  • 9
    • 0037279012 scopus 로고    scopus 로고
    • Characterization of human Smg5/7a: A protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1
    • Chiu, S.Y., Serin, G., Ohara, O. & Maquat, L.E. Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1. RNA 9, 77-87 (2003).
    • (2003) RNA , vol.9 , pp. 77-87
    • Chiu, S.Y.1    Serin, G.2    Ohara, O.3    Maquat, L.E.4
  • 10
    • 0037415691 scopus 로고    scopus 로고
    • SMG-5, required for C. elegans nonsense-mediated mRNA decay, associates with SMG-2 and protein phosphatase 2A
    • Anders, K.R., Grimson, A. & Anderson, P. SMG-5, required for C. elegans nonsense-mediated mRNA decay, associates with SMG-2 and protein phosphatase 2A. EMBO J. 22, 641-650 (2003).
    • (2003) EMBO J. , vol.22 , pp. 641-650
    • Anders, K.R.1    Grimson, A.2    Anderson, P.3
  • 11
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • Le Hir, H., Gatfield, D., Izaurralde, E. & Moore, M.J. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. EMBO J. 20, 4987-4997 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 12
    • 0035823036 scopus 로고    scopus 로고
    • Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP 80 and CBP20
    • Ishigaki, Y., Li, X., Serin, G. & Maquat, L.E. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell 106, 607-617 (2001).
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 13
    • 2642656314 scopus 로고    scopus 로고
    • The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs
    • Czaplinski, K. et al. The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev. 12, 1665-1677 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1665-1677
    • Czaplinski, K.1
  • 14
    • 0035823150 scopus 로고    scopus 로고
    • Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
    • Kim, V.N., Kataoka, N. & Dreyfuss, G. Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. Science 293, 1832-1836 (2001).
    • (2001) Science , vol.293 , pp. 1832-1836
    • Kim, V.N.1    Kataoka, N.2    Dreyfuss, G.3
  • 15
    • 0035865408 scopus 로고    scopus 로고
    • The role of Upf proteins in modulating the translation read-through of nonsense-containing transcripts
    • Wang, W., Czaplinski, K., Rao, Y. & Peltz, S.W. The role of Upf proteins in modulating the translation read-through of nonsense-containing transcripts. EMBO J. 20, 880-890(2001).
    • (2001) EMBO J. , vol.20 , pp. 880-890
    • Wang, W.1    Czaplinski, K.2    Rao, Y.3    Peltz, S.W.4
  • 16
    • 0032104190 scopus 로고    scopus 로고
    • A rule for termination-codon position within intron-containing genes: When nonsense affects RNA abundance
    • Nagy, E. & Maquat, L.E. A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem. Sci. 23, 198-199 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 198-199
    • Nagy, E.1    Maquat, L.E.2
  • 17
    • 0028945345 scopus 로고
    • Identification and characterization of a sequence motif involved in nonsense-mediated mRNA decay
    • Zhang, S., Ruiz-Echevarria, M.J., Quan, Y. & Peltz, S.W. Identification and characterization of a sequence motif involved in nonsense-mediated mRNA decay. Mol. Cell. Biol. 15, 2231-2244 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2231-2244
    • Zhang, S.1    Ruiz-Echevarria, M.J.2    Quan, Y.3    Peltz, S.W.4
  • 18
    • 0042068262 scopus 로고    scopus 로고
    • Complexes between the nonsense-mediated mRNA decay pathway factor human upf1 (up-frameshift protein 1) and essential nonsense-mediated mRNA decay factors in HeLa cells
    • Schell, T. et al. Complexes between the nonsense-mediated mRNA decay pathway factor human upf1 (up-frameshift protein 1) and essential nonsense-mediated mRNA decay factors in HeLa cells. Biochem. J. 373, 775-783 (2003).
    • (2003) Biochem. J. , vol.373 , pp. 775-783
    • Schell, T.1
  • 19
    • 0036086410 scopus 로고    scopus 로고
    • Recent improvements to the SMART domain-based sequence annotation resource
    • Letunic, I. et al. Recent improvements to the SMART domain-based sequence annotation resource. Nucleic Acids Res. 30, 242-244 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 242-244
    • Letunic, I.1
  • 20
    • 0034284394 scopus 로고    scopus 로고
    • Novel elF4G domain homologues linking mRNA translation with non-sense-mediated mRNA decay
    • Ponting, C.P. Novel elF4G domain homologues linking mRNA translation with non-sense-mediated mRNA decay. Trends Biochem. Sci. 25, 423-426 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 423-426
    • Ponting, C.P.1
  • 21
    • 0035105502 scopus 로고    scopus 로고
    • A conserved HEAT domain within elF4G directs assembly of the translation initiation machinery
    • Marcotrigiano, J. et al. A conserved HEAT domain within elF4G directs assembly of the translation initiation machinery, Mol. Cell 7, 193-203 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 193-203
    • Marcotrigiano, J.1
  • 22
    • 0034852936 scopus 로고    scopus 로고
    • Crystal structure of the human nuclear cap binding complex
    • Mazza, C., Ohno, M., Segref, A., Mattaj, I.W. & Cusack, S. Crystal structure of the human nuclear cap binding complex. Mol. Cell 8, 383-396 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 383-396
    • Mazza, C.1    Ohno, M.2    Segref, A.3    Mattaj, I.W.4    Cusack, S.5
  • 23
    • 0031025296 scopus 로고    scopus 로고
    • Upf1p, Nmd2p, and Upf3p are interacting components of the yeast nonsense-mediated mRNA decay pathway
    • He, F., Brown, A.H. & Jacobson, A. Upf1p, Nmd2p, and Upf3p are interacting components of the yeast nonsense-mediated mRNA decay pathway. Mol. Cell. Biol. 17, 1580-1594 (1997).
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1580-1594
    • He, F.1    Brown, A.H.2    Jacobson, A.3
  • 24
    • 0029842901 scopus 로고    scopus 로고
    • Interaction between Nmd2p and Upf1p is required for activity but not for dominant-negative inhibition of the nonsense-mediated mRNA decay pathway in yeast
    • He, F., Brown, A.H. & Jacobson, A. Interaction between Nmd2p and Upf1p is required for activity but not for dominant-negative inhibition of the nonsense-mediated mRNA decay pathway in yeast. RNA 2, 153-170 (1996).
    • (1996) RNA , vol.2 , pp. 153-170
    • He, F.1    Brown, A.H.2    Jacobson, A.3
  • 25
    • 0036600739 scopus 로고    scopus 로고
    • RNA-protein interactions
    • Hall, K.B. RNA-protein interactions. Curr. Opin. Struct. Biol. 12, 283-288 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 283-288
    • Hall, K.B.1
  • 26
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 0033560881 scopus 로고    scopus 로고
    • Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein
    • Handa, N. et al. Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein. Nature 398, 579-585 (1999).
    • (1999) Nature , vol.398 , pp. 579-585
    • Handa, N.1
  • 28
    • 0342927495 scopus 로고    scopus 로고
    • Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold
    • Conte, M.R. et al. Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. EMBO J. 19, 3132-3141 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3132-3141
    • Conte, M.R.1
  • 29
    • 0037850982 scopus 로고    scopus 로고
    • Structure of the y14-magoh core of the exon junction complex
    • Lau, C.K., Diem, M.D., Dreyfuss, G. & Van Duyne, G.D. Structure of the y14-magoh core of the exon junction complex. Curr. Biol., 933-941 (2003).
    • (2003) Curr. Biol. , pp. 933-941
    • Lau, C.K.1    Diem, M.D.2    Dreyfuss, G.3    Van Duyne, G.D.4
  • 30
    • 0037447151 scopus 로고    scopus 로고
    • Crystal structure of the Orosophila Mago nashi-Y 14 complex
    • Shi, H. & Xu, R.M. Crystal structure of the Orosophila Mago nashi-Y14 complex. Genes Dev. 17, 971-976 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 971-976
    • Shi, H.1    Xu, R.M.2
  • 31
    • 0035975970 scopus 로고    scopus 로고
    • Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport
    • Hachet, O. & Ephrussi, A. Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr. Biol. 11, 1666-1674 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1666-1674
    • Hachet, O.1    Ephrussi, A.2
  • 32
    • 0038298868 scopus 로고    scopus 로고
    • Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP
    • Selenko, P. et al. Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP. Mol Cell. 11, 965-976 (2003).
    • (2003) Mol. Cell. , vol.11 , pp. 965-976
    • Selenko, P.1
  • 33
    • 0037107401 scopus 로고    scopus 로고
    • Large-scale induced fit recognition of an m(7)GPG cap analogue by the human nuclear cap-binding complex
    • Mazza, C., Segref, A., Mattaj, I.W. & Cusack, S. Large-scale induced fit recognition of an m(7)GPG cap analogue by the human nuclear cap-binding complex. EMBO J. 21, 5548-5557 (2002).
    • (2002) EMBO J. , vol.21 , pp. 5548-5557
    • Mazza, C.1    Segref, A.2    Mattaj, I.W.3    Cusack, S.4
  • 34
    • 0031720742 scopus 로고    scopus 로고
    • A factor required for nonsense-mediated mRNA decay in yeast is exported from the nucleus to the cytoplasm by a nuclear export signal sequence
    • Shirley, R.L., Lelivelt, M.J., Schenkman, L.R., Dahlseid, J.N. & Culbertson, M.R. A factor required for nonsense-mediated mRNA decay in yeast is exported from the nucleus to the cytoplasm by a nuclear export signal sequence. J. Cell Sci. 111, 3129-3143 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 3129-3143
    • Shirley, R.L.1    Lelivelt, M.J.2    Schenkman, L.R.3    Dahlseid, J.N.4    Culbertson, M.R.5
  • 35
    • 0036670621 scopus 로고    scopus 로고
    • Nuclear import of Upf3p is mediated by importin-α/-β and export to the cytoplasm is required for a functional nonsense-mediated mRNA decay pathway in yeast
    • Shirley, R.L., Ford, A.S., Richards, M.R., Albertini, M. & Culbertson, M.R. Nuclear import of Upf3p is mediated by importin-α/ -β and export to the cytoplasm is required for a functional nonsense-mediated mRNA decay pathway in yeast. Genetics 161, 1465-1482 (2002).
    • (2002) Genetics , vol.161 , pp. 1465-1482
    • Shirley, R.L.1    Ford, A.S.2    Richards, M.R.3    Albertini, M.4    Culbertson, M.R.5
  • 36
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 37
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Uson, I. & Sheldrick, G.M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9, 643-648 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 643-648
    • Uson, I.1    Sheldrick, G.M.2
  • 38
    • 80055004570 scopus 로고
    • Generalized method of determining heavy-atom positions using the difference Patterson function
    • Terwilliger, T.C., Kim, S.H. & Eisenberg, D. Generalized method of determining heavy-atom positions using the difference Patterson function. Acta Crystallogr. A 43, 1-5 (1987).
    • (1987) Acta Crystallogr. A , vol.43 , pp. 1-5
    • Terwilliger, T.C.1    Kim, S.H.2    Eisenberg, D.3
  • 39
    • 0033229974 scopus 로고    scopus 로고
    • Reciprocal-space solvent flattening
    • Terwilliger, T.C. Reciprocal-space solvent flattening. Acta Crystallogr. D 55, 1863-1871 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 1863-1871
    • Terwilliger, T.C.1
  • 40
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R. & Lamzin, V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458-463 (1999).
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 41
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 0024851833 scopus 로고
    • Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA
    • Scherly, D. et al. Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA. EMBO J. 8, 4163-4170 (1989).
    • (1989) EMBO J. , vol.8 , pp. 4163-4170
    • Scherly, D.1
  • 44
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. & Higgins, D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 45
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D.I. & Metoz, F. ESPript: multiple sequence alignments in PostScript. Bioinformatics 15, 305-308 (1999).
    • (1999) Bioinformatics , vol.15 , pp. 305-308
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Metoz, F.4
  • 46
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 47
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf, R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D 55, 938-940 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 938-940
    • Esnouf, R.M.1
  • 48
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Gen. 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Gen. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 49
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs, K. & Karplus, P.A. Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat. Struct. Biol. 4, 269-275 (1997).
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2


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