메뉴 건너뛰기




Volumn 19, Issue 9, 2012, Pages 916-924

PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53

Author keywords

[No Author keywords available]

Indexed keywords

ACYLTRANSFERASE; HOMODIMER; LYSINE; PHF20 PROTEIN; PROTEIN MDM2; PROTEIN P53; UNCLASSIFIED DRUG;

EID: 84866091585     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2353     Document Type: Article
Times cited : (78)

References (60)
  • 1
    • 65349103899 scopus 로고    scopus 로고
    • Blinded by the light: The growing complexity of p53
    • Vousden, K.H. & Prives, C. Blinded by the light: the growing complexity of p53. Cell 137, 413-431 (2009).
    • (2009) Cell , vol.137 , pp. 413-431
    • Vousden, K.H.1    Prives, C.2
  • 3
    • 33845204856 scopus 로고    scopus 로고
    • Repression of p53 activity by Smyd2-mediated methylation
    • Huang, J. et al. Repression of p53 activity by Smyd2-mediated methylation. Nature 444, 629-632 (2006).
    • (2006) Nature , vol.444 , pp. 629-632
    • Huang, J.1
  • 4
    • 34548513035 scopus 로고    scopus 로고
    • P53 is regulated by the lysine demethylase LSD1
    • Huang, J. et al. p53 is regulated by the lysine demethylase LSD1. Nature 449, 105-108 (2007).
    • (2007) Nature , vol.449 , pp. 105-108
    • Huang, J.1
  • 5
    • 34547809957 scopus 로고    scopus 로고
    • Modulation of p53 function by SET8-mediated methylation at lysine 382
    • Shi, X. et al. Modulation of p53 function by SET8-mediated methylation at lysine 382. Mol. Cell 27, 636-646 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 636-646
    • Shi, X.1
  • 6
    • 58049203867 scopus 로고    scopus 로고
    • Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling
    • Kachirskaia, I. et al. Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling. J. Biol. Chem. 283, 34660-34666 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 34660-34666
    • Kachirskaia, I.1
  • 7
    • 77951921958 scopus 로고    scopus 로고
    • Structural insight into p53 recognition by the 53BP1 tandem Tudor domain
    • Roy, S. et al. Structural insight into p53 recognition by the 53BP1 tandem Tudor domain. J. Mol. Biol. 398, 489-496 (2010).
    • (2010) J. Mol. Biol. , vol.398 , pp. 489-496
    • Roy, S.1
  • 8
    • 79959984411 scopus 로고    scopus 로고
    • Regulation of p53 function by lysine methylation
    • West, L.E. & Gozani, O. Regulation of p53 function by lysine methylation. Epigenomics 3, 361-369 (2011).
    • (2011) Epigenomics , vol.3 , pp. 361-369
    • West, L.E.1    Gozani, O.2
  • 9
    • 0036500691 scopus 로고    scopus 로고
    • Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure
    • Joo, W.S. et al. Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure. Genes Dev. 16, 583-593 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 583-593
    • Joo, W.S.1
  • 10
    • 0037099666 scopus 로고    scopus 로고
    • Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor
    • Derbyshire, D.J. et al. Crystal structure of human 53BP1 BRCT domains bound to p53 tumour suppressor. EMBO J. 21, 3863-3872 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3863-3872
    • Derbyshire, D.J.1
  • 12
    • 33645502395 scopus 로고    scopus 로고
    • Tudor MBT and chromo domains gauge the degree of lysine methylation
    • Kim, J. et al. Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 7, 397-403 (2006).
    • (2006) EMBO Rep. , vol.7 , pp. 397-403
    • Kim, J.1
  • 13
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specifc recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan, M.V. et al. Structural basis for the methylation state-specifc recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 127, 1361-1373 (2006).
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1
  • 14
    • 0034772612 scopus 로고    scopus 로고
    • Glioma-expressed antigen 2 (GLEA2): A novel protein that can elicit immune responses in glioblastoma patients and some controls
    • Fischer, U. et al. Glioma-expressed antigen 2 (GLEA2): a novel protein that can elicit immune responses in glioblastoma patients and some controls. Clin. Exp. Immunol. 126, 206-213 (2001).
    • (2001) Clin. Exp. Immunol. , vol.126 , pp. 206-213
    • Fischer, U.1
  • 15
    • 26444586707 scopus 로고    scopus 로고
    • Autoantibodies against GLEA2 and PHF3 in glioblastoma: Tumor-associated autoantibodies correlated with prolonged survival
    • Pallasch, C.P. et al. Autoantibodies against GLEA2 and PHF3 in glioblastoma: Tumor-associated autoantibodies correlated with prolonged survival. Int. J. Cancer 117, 456-459 (2005).
    • (2005) Int. J. Cancer , vol.117 , pp. 456-459
    • Pallasch, C.P.1
  • 16
    • 47749144792 scopus 로고    scopus 로고
    • Increased seroreactivity to glioma-expressed antigen 2 in brain tumor patients under radiation
    • Heisel, S.M. et al. Increased seroreactivity to glioma-expressed antigen 2 in brain tumor patients under radiation. PLoS ONE 3, e2164 (2008).
    • (2008) PLoS ONE , vol.3
    • Heisel, S.M.1
  • 17
    • 84859499770 scopus 로고    scopus 로고
    • Identifcation of an Akt interaction protein, PHF20/TZP, that transcriptionally regulates p53
    • Park, S. et al. Identifcation of an Akt interaction protein, PHF20/TZP, that transcriptionally regulates p53. J. Biol. Chem. 287, 11151-11163 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 11151-11163
    • Park, S.1
  • 18
    • 20444397430 scopus 로고    scopus 로고
    • Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
    • Dou, Y. et al. Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121, 873-885 (2005).
    • (2005) Cell , vol.121 , pp. 873-885
    • Dou, Y.1
  • 19
    • 22544480772 scopus 로고    scopus 로고
    • HMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells
    • Taipale, M. et al. hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells. Mol. Cell. Biol. 25, 6798-6810 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6798-6810
    • Taipale, M.1
  • 20
    • 33644870525 scopus 로고    scopus 로고
    • Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila
    • Mendjan, S. et al. Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila. Mol. Cell 21, 811-823 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 811-823
    • Mendjan, S.1
  • 21
    • 70350012477 scopus 로고    scopus 로고
    • Two mammalian MOF complexes regulate transcription activation by distinct mechanisms
    • Li, X., Wu, L., Corsa, C.A., Kunkel, S. & Dou, Y. Two mammalian MOF complexes regulate transcription activation by distinct mechanisms. Mol. Cell 36, 290-301 (2009).
    • (2009) Mol. Cell , vol.36 , pp. 290-301
    • Li, X.1    Wu, L.2    Corsa, C.A.3    Kunkel, S.4    Dou, Y.5
  • 22
    • 77951182263 scopus 로고    scopus 로고
    • Subunit composition and substrate specifcity of a MOF-containing histone acetyltransferase distinct from the male-specifc lethal (MSL) complex
    • Cai, Y. et al. Subunit composition and substrate specifcity of a MOF-containing histone acetyltransferase distinct from the male-specifc lethal (MSL) complex. J. Biol. Chem. 285, 4268-4272 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 4268-4272
    • Cai, Y.1
  • 23
    • 33845656738 scopus 로고    scopus 로고
    • Acetylation of the p53 DNA-binding domain regulates apoptosis induction
    • Sykes, S.M. et al. Acetylation of the p53 DNA-binding domain regulates apoptosis induction. Mol. Cell 24, 841-851 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 841-851
    • Sykes, S.M.1
  • 24
    • 33749160125 scopus 로고    scopus 로고
    • Modifcation of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability
    • Yang, W.H. et al. Modifcation of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability. Nat. Cell Biol. 8, 1074-1083 (2006).
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1074-1083
    • Yang, W.H.1
  • 25
    • 84855279809 scopus 로고    scopus 로고
    • Loss of the methyl lysine effector protein PHF20 impacts the expression of genes regulated by the lysine acetyltransferase MOF
    • Badeaux, A.I. et al. Loss of the methyl lysine effector protein PHF20 impacts the expression of genes regulated by the lysine acetyltransferase MOF. J. Biol. Chem. 287, 429-437 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 429-437
    • Badeaux, A.I.1
  • 26
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang, Y., Fang, J., Bedford, M.T., Zhang, Y. & Xu, R.M. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 312, 748-751 (2006).
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 27
    • 37849015924 scopus 로고    scopus 로고
    • Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor
    • Lee, J., Thompson, J.R., Botuyan, M.V. & Mer, G. Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor. Nat. Struct. Mol. Biol. 15, 109-111 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 109-111
    • Lee, J.1    Thompson, J.R.2    Botuyan, M.V.3    Mer, G.4
  • 28
    • 33746832077 scopus 로고    scopus 로고
    • Identifcation and characterization of Smyd2: A split SET/MYND domain-containing histone H3 lysine 36-specifc methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown, M.A., Sims, R.J. III, Gottlieb, P.D. & Tucker, P.W. Identifcation and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specifc methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol. Cancer 5, 26 (2006).
    • (2006) Mol. Cancer , vol.5 , pp. 26
    • Brown, M.A.1    Sims III, R.J.2    Gottlieb, P.D.3    Tucker, P.W.4
  • 29
    • 22344455665 scopus 로고    scopus 로고
    • Specifcity and mechanism of the histone methyltransferase Pr-Set7
    • Xiao, B. et al. Specifcity and mechanism of the histone methyltransferase Pr-Set7. Genes Dev. 19, 1444-1454 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 1444-1454
    • Xiao, B.1
  • 30
    • 22344454519 scopus 로고    scopus 로고
    • Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
    • Couture, J.F., Collazo, E., Brunzelle, J.S. & Trievel, R.C. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes Dev. 19, 1455-1465 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 1455-1465
    • Couture, J.F.1    Collazo, E.2    Brunzelle, J.S.3    Trievel, R.C.4
  • 31
    • 40949165264 scopus 로고    scopus 로고
    • In situ observation of protein phosphorylation by high-resolution NMR spectroscopy
    • Selenko, P. et al. In situ observation of protein phosphorylation by high-resolution NMR spectroscopy. Nat. Struct. Mol. Biol. 15, 321-329 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 321-329
    • Selenko, P.1
  • 33
    • 77958493434 scopus 로고    scopus 로고
    • Simultaneous detection of protein phosphorylation and acetylation by high-resolution NMR spectroscopy
    • Liokatis, S., Dose, A., Schwarzer, D. & Selenko, P. Simultaneous detection of protein phosphorylation and acetylation by high-resolution NMR spectroscopy. J. Am. Chem. Soc. 132, 14704-14705 (2010).
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14704-14705
    • Liokatis, S.1    Dose, A.2    Schwarzer, D.3    Selenko, P.4
  • 34
    • 55249111484 scopus 로고    scopus 로고
    • Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S
    • Xu, C., Cui, G., Botuyan, M.V. & Mer, G. Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S. Structure 16, 1740-1750 (2008).
    • (2008) Structure , vol.16 , pp. 1740-1750
    • Xu, C.1    Cui, G.2    Botuyan, M.V.3    Mer, G.4
  • 35
    • 31544457877 scopus 로고    scopus 로고
    • P53 ubiquitination: Mdm2 and beyond
    • Brooks, C.L. & Gu, W. p53 ubiquitination: Mdm2 and beyond. Mol. Cell 21, 307-315 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 36
    • 77955858336 scopus 로고    scopus 로고
    • Posttranslational modifcation of p53: Cooperative integrators of function
    • Meek, D.W. & Anderson, C.W. Posttranslational modifcation of p53: cooperative integrators of function. Cold Spring Harb. Perspect. Biol. 1, a000950 (2009).
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1
    • Meek, D.W.1    Anderson, C.W.2
  • 37
    • 77955418479 scopus 로고    scopus 로고
    • The C terminus of p53 binds the N-terminal domain of MDM2
    • Poyurovsky, M.V. et al. The C terminus of p53 binds the N-terminal domain of MDM2. Nat. Struct. Mol. Biol. 17, 982-989 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 982-989
    • Poyurovsky, M.V.1
  • 38
    • 78249286851 scopus 로고    scopus 로고
    • Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2
    • Adams-Cioaba, M.A. et al. Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2. PLoS ONE 5, e13559 (2010).
    • (2010) PLoS ONE , vol.5
    • Adams-Cioaba, M.A.1
  • 39
    • 82955233813 scopus 로고    scopus 로고
    • Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins
    • Tripsianes, K. et al. Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nat. Struct. Mol. Biol. 18, 1414-1420 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1414-1420
    • Tripsianes, K.1
  • 40
    • 34249099730 scopus 로고    scopus 로고
    • Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin
    • Li, B. et al. Combined action of PHD and chromo domains directs the Rpd3S HDAC to transcribed chromatin. Science 316, 1050-1054 (2007).
    • (2007) Science , vol.316 , pp. 1050-1054
    • Li, B.1
  • 41
    • 36448949026 scopus 로고    scopus 로고
    • Multivalent engagement of chromatin modifcations by linked binding modules
    • Ruthenburg, A.J., Li, H., Patel, D.J. & Allis, C.D. Multivalent engagement of chromatin modifcations by linked binding modules. Nat. Rev. Mol. Cell Biol. 8, 983-994 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 983-994
    • Ruthenburg, A.J.1    Li, H.2    Patel, D.J.3    Allis, C.D.4
  • 42
    • 79956326021 scopus 로고    scopus 로고
    • Combinatorial readout of dual histone modifcations by paired chromatin-associated modules
    • Wang, Z. & Patel, D.J. Combinatorial readout of dual histone modifcations by paired chromatin-associated modules. J. Biol. Chem. 286, 18363-18368 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 18363-18368
    • Wang, Z.1    Patel, D.J.2
  • 43
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specifcity of a family of jumonji histone lysine demethylases
    • Horton, J.R. et al. Enzymatic and structural insights for substrate specifcity of a family of jumonji histone lysine demethylases. Nat. Struct. Mol. Biol. 17, 38-43 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 38-43
    • Horton, J.R.1
  • 44
    • 0028575413 scopus 로고
    • An intermolecular disulfde bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures
    • Benezra, R. An intermolecular disulfde bond stabilizes E2A homodimers and is required for DNA binding at physiological temperatures. Cell 79, 1057-1067 (1994).
    • (1994) Cell , vol.79 , pp. 1057-1067
    • Benezra, R.1
  • 45
    • 0035949588 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus
    • Mayo, L.D. & Donner, D.B. A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus. Proc. Natl. Acad. Sci. USA 98, 11598-11603 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11598-11603
    • Mayo, L.D.1    Donner, D.B.2
  • 46
    • 3142608985 scopus 로고    scopus 로고
    • Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains
    • Botuyan, M.V. et al. Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Structure 12, 1137-1146 (2004).
    • (2004) Structure , vol.12 , pp. 1137-1146
    • Botuyan, M.V.1
  • 47
    • 33847386172 scopus 로고    scopus 로고
    • The site-specifc installation of methyl-lysine analogs into recombinant histones
    • Simon, M.D. et al. The site-specifc installation of methyl-lysine analogs into recombinant histones. Cell 128, 1003-1012 (2007).
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley, L.A. & Sternberg, M.J. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371 (2009).
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 51
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 52
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 53
    • 34249765651 scopus 로고
    • NMRView: A computer program for visualization and analysis of NMR data
    • Johnson, B.A. & Blevins, R.A. NMRView: a computer program for visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614 (1994).
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 54
    • 0035029325 scopus 로고    scopus 로고
    • SANE (Structure assisted NOE evaluation): An automated model-based approach for NOE assignment
    • Duggan, B.M., Legge, G.B., Dyson, H.J. & Wright, P.E. SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment. J. Biomol. NMR 19, 321-329 (2001).
    • (2001) J. Biomol. NMR , vol.19 , pp. 321-329
    • Duggan, B.M.1    Legge, G.B.2    Dyson, H.J.3    Wright, P.E.4
  • 55
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. & Bax, A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302 (1999).
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 57
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert, P. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278, 353-378 (2004).
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 58
    • 23444454552 scopus 로고    scopus 로고
    • The Amber biomolecular simulation programs
    • Case, D.A. et al. The Amber biomolecular simulation programs. J. Comput. Chem. 26, 1668-1688 (2005).
    • (2005) J. Comput. Chem. , vol.26 , pp. 1668-1688
    • Case, D.A.1
  • 59
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 60
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.