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Volumn 13, Issue 24, 2003, Pages 2148-2158

Structure and Function of the Conserved Core of Histone Deposition Protein Asf1

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES;

EID: 9144251600     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2003.11.027     Document Type: Article
Times cited : (126)

References (60)
  • 1
    • 0018036390 scopus 로고
    • Assembly of newly replicated chromatin
    • Worcel, A., Han, S., and Wong, M.L. (1978). Assembly of newly replicated chromatin. Cell 15, 969-977.
    • (1978) Cell , vol.15 , pp. 969-977
    • Worcel, A.1    Han, S.2    Wong, M.L.3
  • 2
    • 0028921083 scopus 로고
    • Replication of transcriptionally active chromatin
    • Lucchini, R., and Sogo, J.M. (1995). Replication of transcriptionally active chromatin. Nature 274, 276-280.
    • (1995) Nature , vol.274 , pp. 276-280
    • Lucchini, R.1    Sogo, J.M.2
  • 3
    • 0001778031 scopus 로고    scopus 로고
    • DNA replication, nucleotide excision repair, and nucleosome assembly
    • S.C.R. Elgin and J.L. Workman, eds. (Oxford: Oxford University Press)
    • Kaufman, P.D., and Almouzni, G. (2000). DNA replication, nucleotide excision repair, and nucleosome assembly. In Chromatin Structure and Gene Expression, Second Edition, S.C.R. Elgin and J.L. Workman, eds. (Oxford: Oxford University Press) pp. 24-48.
    • (2000) Chromatin Structure and Gene Expression, Second Edition , pp. 24-48
    • Kaufman, P.D.1    Almouzni, G.2
  • 4
    • 0037238123 scopus 로고    scopus 로고
    • Chromatin proteins are determinants of centromere function
    • Sharp, J.A., and Kaufman, P.D. (2003). Chromatin proteins are determinants of centromere function. Curr. Top. Microbiol. Immunol. 274, 24-52.
    • (2003) Curr. Top. Microbiol. Immunol. , vol.274 , pp. 24-52
    • Sharp, J.A.1    Kaufman, P.D.2
  • 5
    • 0030862060 scopus 로고    scopus 로고
    • Two new S-phase-specific genes from Saccharomyces cerevisiae
    • Le, S., Davis, C., Konopka, J.B., and Sternglanz, R. (1997). Two new S-phase-specific genes from Saccharomyces cerevisiae. Yeast 13, 1029-1042.
    • (1997) Yeast , vol.13 , pp. 1029-1042
    • Le, S.1    Davis, C.2    Konopka, J.B.3    Sternglanz, R.4
  • 7
    • 0038312215 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae chromatin-assembly factors that act during DNA replication function in the maintenance of genome stability
    • Published online May 15, 2003. 10.1073/pnas.1232239100
    • Myung, K., Pennaneach, V., Kats, E.S., and Kolodner, R.D. (2003). Saccharomyces cerevisiae chromatin-assembly factors that act during DNA replication function in the maintenance of genome stability. Proc. Natl. Acad. Sci. USA 100, 6640-6645. Published online May 15, 2003. 10.1073/pnas.1232239100.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6640-6645
    • Myung, K.1    Pennaneach, V.2    Kats, E.S.3    Kolodner, R.D.4
  • 8
    • 0036888874 scopus 로고    scopus 로고
    • Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair
    • Qin, S., and Parthun, M.R. (2002). Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair. Mol. Cell. Biol. 22, 8353-8365.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8353-8365
    • Qin, S.1    Parthun, M.R.2
  • 9
    • 0036964090 scopus 로고    scopus 로고
    • Defects in SPT16 or POB3 (yFACT) cause dependence on the Hir/Hpc pathway: Accessing DNA may degrade chromatin structure
    • Formosa, T., Ruone, S., Adams, M.D., Olsen, A.E., Eriksson, P., Yu, Y., Rhoades, A., Kaufman, P.D., and Stillman, D.J. (2002). Defects in SPT16 or POB3 (yFACT) cause dependence on the Hir/Hpc pathway: accessing DNA may degrade chromatin structure. Genetics 162, 1557-1571.
    • (2002) Genetics , vol.162 , pp. 1557-1571
    • Formosa, T.1    Ruone, S.2    Adams, M.D.3    Olsen, A.E.4    Eriksson, P.5    Yu, Y.6    Rhoades, A.7    Kaufman, P.D.8    Stillman, D.J.9
  • 10
    • 0036163533 scopus 로고    scopus 로고
    • Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro
    • Umehara, T., Chimura, T., Ichikawa, N., and Horikoshi, M. (2002). Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro. Genes Cells 7, 59-73.
    • (2002) Genes Cells , vol.7 , pp. 59-73
    • Umehara, T.1    Chimura, T.2    Ichikawa, N.3    Horikoshi, M.4
  • 11
    • 0033518179 scopus 로고    scopus 로고
    • The RCAF complex mediates chromatin assembly during DNA replication and repair
    • Tyler, J.K., Adams, C.R., Chen, S.R., Kobayashi, R., and Kamakaka, R.T., and Kadonaga, J.T. (1999). The RCAF complex mediates chromatin assembly during DNA replication and repair. Nature 402, 555-560.
    • (1999) Nature , vol.402 , pp. 555-560
    • Tyler, J.K.1    Adams, C.R.2    Chen, S.R.3    Kobayashi, R.4    Kamakaka, R.T.5    Kadonaga, J.T.6
  • 13
    • 0036135016 scopus 로고    scopus 로고
    • Chromatin assembly factor-I mutants defective for PCNA binding require Asf1/Hir proteins for silencing
    • Krawitz, D.C., Kama, T., and Kaufman, P.D. (2002). Chromatin assembly factor-I mutants defective for PCNA binding require Asf1/Hir proteins for silencing. Mol. Cell. Biol. 22, 614-625.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 614-625
    • Krawitz, D.C.1    Kama, T.2    Kaufman, P.D.3
  • 14
    • 0036250827 scopus 로고    scopus 로고
    • Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway
    • Mello, J.A., Sillje, H.H., Roche, D.M., Kirschner, D.B., Nigg, E.A., and Almouzni, G. (2002). Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway. EMBO Rep. 3, 329-334.
    • (2002) EMBO Rep. , vol.3 , pp. 329-334
    • Mello, J.A.1    Sillje, H.H.2    Roche, D.M.3    Kirschner, D.B.4    Nigg, E.A.5    Almouzni, G.6
  • 15
    • 0034977802 scopus 로고    scopus 로고
    • Yeast ASF1 protein is required for cell-cycle regulation of histone gene transcription
    • Sutton, A., Bucaria, J., Osley, M.A., and Sternglanz, R. (2001). Yeast ASF1 protein is required for cell-cycle regulation of histone gene transcription. Genetics 158, 587-596.
    • (2001) Genetics , vol.158 , pp. 587-596
    • Sutton, A.1    Bucaria, J.2    Osley, M.A.3    Sternglanz, R.4
  • 16
    • 0035799281 scopus 로고    scopus 로고
    • Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing
    • Sharp, J.A., Fouts, E.T., Krawitz, D.C., and Kaufman, P.D. (2001). Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing. Curr. Biol. 11, 463-473.
    • (2001) Curr. Biol. , vol.11 , pp. 463-473
    • Sharp, J.A.1    Fouts, E.T.2    Krawitz, D.C.3    Kaufman, P.D.4
  • 17
    • 0031858054 scopus 로고    scopus 로고
    • Hir proteins are required for position-dependent gene silencing in Saccharomyces cerevisiae in the absence of chromatin assembly factor I
    • Kaufman, P.D., Cohen, J.L., and Osley, M.A. (1998). Hir proteins are required for position-dependent gene silencing in Saccharomyces cerevisiae in the absence of chromatin assembly factor I. Mol. Cell. Biol. 18, 4793-4806.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4793-4806
    • Kaufman, P.D.1    Cohen, J.L.2    Osley, M.A.3
  • 18
    • 0035131425 scopus 로고    scopus 로고
    • HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression
    • Hall, C., Nelson, D.M., Ye, X., Baker, K., DeCaprio, J.A., Seeholzer, S., Lipinski, M., and Adams, P.D. (2001). HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression. Mol. Cell. Biol. 21, 1854-1865.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1854-1865
    • Hall, C.1    Nelson, D.M.2    Ye, X.3    Baker, K.4    DeCaprio, J.A.5    Seeholzer, S.6    Lipinski, M.7    Adams, P.D.8
  • 20
    • 0036284794 scopus 로고    scopus 로고
    • HIRa is critical for a nucleosome assembly pathway independent of DNA synthesis
    • Ray-Gallet, D., Quivy, J.P., Scamps, C., Martini, E.M., Lipinski, M., and Almouzni, G. (2002). HIRA is critical for a nucleosome assembly pathway independent of DNA synthesis. Mol. Cell 9, 1091-1100.
    • (2002) Mol. Cell , vol.9 , pp. 1091-1100
    • Ray-Gallet, D.1    Quivy, J.P.2    Scamps, C.3    Martini, E.M.4    Lipinski, M.5    Almouzni, G.6
  • 21
    • 0035101733 scopus 로고    scopus 로고
    • Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1
    • Emili, A., Schieltz, D.M., Yates, J.R., and Hartwell, L. (2001). Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1. Mol. Cell 7, 13-20.
    • (2001) Mol. Cell , vol.7 , pp. 13-20
    • Emili, A.1    Schieltz, D.M.2    Yates, J.R.3    Hartwell, L.4
  • 22
    • 0035336971 scopus 로고    scopus 로고
    • Asf1 links Rad53 to control of chromatin assembly
    • Hu, F., Alcasabas, A.A., and Elledge, S.J. (2001). Asf1 links Rad53 to control of chromatin assembly. Genes Dev. 15, 1061-1066.
    • (2001) Genes Dev. , vol.15 , pp. 1061-1066
    • Hu, F.1    Alcasabas, A.A.2    Elledge, S.J.3
  • 23
    • 0035576789 scopus 로고    scopus 로고
    • The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1
    • Osada, S., Sutton, A., Muster, N., Brown, C.E., Yates, J.R., 3rd, Sternglanz, R., and Workman, J.L. (2001). The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1. Genes Dev. 15, 3155-3168.
    • (2001) Genes Dev. , vol.15 , pp. 3155-3168
    • Osada, S.1    Sutton, A.2    Muster, N.3    Brown, C.E.4    Yates III, J.R.5    Sternglanz, R.6    Workman, J.L.7
  • 24
    • 0035577669 scopus 로고    scopus 로고
    • The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae
    • Meijsing, S.H., and Ehrenhofer-Murray, A.E. (2001). The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae. Genes Dev. 15, 3169-3182.
    • (2001) Genes Dev. , vol.15 , pp. 3169-3182
    • Meijsing, S.H.1    Ehrenhofer-Murray, A.E.2
  • 26
    • 0037047101 scopus 로고    scopus 로고
    • Identification and characterization of CIA/ASF1 as an interactor of bromo-domains associated with TFIID
    • Chimura, T., Kuzuhara, T., and Horikoshi, M. (2002). Identification and characterization of CIA/ASF1 as an interactor of bromo-domains associated with TFIID. Proc. Natl. Acad. Sci. USA 99, 9334-9339.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9334-9339
    • Chimura, T.1    Kuzuhara, T.2    Horikoshi, M.3
  • 27
    • 0036269973 scopus 로고    scopus 로고
    • Proteomics of the eukaryotic transcription machinery: Identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry
    • Sanders, S.L., Jennings, J., Canutescu, A., Link, A.J., and Weil, P.A. (2002). Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry. Mol. Cell. Biol. 22, 4723-4738.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4723-4738
    • Sanders, S.L.1    Jennings, J.2    Canutescu, A.3    Link, A.J.4    Weil, P.A.5
  • 28
    • 0037930802 scopus 로고    scopus 로고
    • Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex
    • Sutton, A., Shia, W.J., Band, D., Kaufman, P.D., Osada, S., Workman, J.L., and Sternglanz, R. (2003). Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex. J. Biol. Chem. 278, 16887-16892.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16887-16892
    • Sutton, A.1    Shia, W.J.2    Band, D.3    Kaufman, P.D.4    Osada, S.5    Workman, J.L.6    Sternglanz, R.7
  • 29
    • 0025201982 scopus 로고
    • Position effect at S. cerevisiae telomeres: Reversible repression of PoIII transcription
    • Gottschling, D.E., Aparicio, O.M., Billington, B.L., and Zakian, V.A. (1990). Position effect at S. cerevisiae telomeres: reversible repression of PoIII transcription. Cell 63, 751-762.
    • (1990) Cell , vol.63 , pp. 751-762
    • Gottschling, D.E.1    Aparicio, O.M.2    Billington, B.L.3    Zakian, V.A.4
  • 30
    • 0031043134 scopus 로고    scopus 로고
    • Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cell lacking chromatin assembly factor-I
    • Kaufman, P.D., Kobayashi, R., and Stillman, B. (1997). Ultraviolet radiation sensitivity and reduction of telomeric silencing in Saccharomyces cerevisiae cell lacking chromatin assembly factor-I. Genes Dev. 11, 345-357.
    • (1997) Genes Dev. , vol.11 , pp. 345-357
    • Kaufman, P.D.1    Kobayashi, R.2    Stillman, B.3
  • 31
    • 0034100123 scopus 로고    scopus 로고
    • A human homologue of yeast anti-silencing factor has histone chaperone activity
    • Munakata, T., Adachi, N., Yokoyama, N., Kuzuhara, T., and Horikoshi, M. (2000). A human homologue of yeast anti-silencing factor has histone chaperone activity. Genes Cells 5, 221-233.
    • (2000) Genes Cells , vol.5 , pp. 221-233
    • Munakata, T.1    Adachi, N.2    Yokoyama, N.3    Kuzuhara, T.4    Horikoshi, M.5
  • 33
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork, P., Holm, L., and Sander, C. (1994). The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol. 242, 309-320.
    • (1994) J. Mol. Biol. , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 34
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. (1995). SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 35
    • 0033560794 scopus 로고    scopus 로고
    • NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis
    • Fattorusso, R., Pellecchia, M., Viti, F., Neri, P., Neri, D., and Wuthrich, K. (1999). NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis. Struct. Fold. Des. 7, 381-390.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 381-390
    • Fattorusso, R.1    Pellecchia, M.2    Viti, F.3    Neri, P.4    Neri, D.5    Wuthrich, K.6
  • 36
    • 0031570337 scopus 로고    scopus 로고
    • A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm
    • Keep, N.H., Barnes, M., Barsukov, I., Badii, R., Lian, L.Y., Segal, A.W., Moody, P.C., and Roberts, G.C. (1997). A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5, 623-633.
    • (1997) Structure , vol.5 , pp. 623-633
    • Keep, N.H.1    Barnes, M.2    Barsukov, I.3    Badii, R.4    Lian, L.Y.5    Segal, A.W.6    Moody, P.C.7    Roberts, G.C.8
  • 37
    • 0037311294 scopus 로고    scopus 로고
    • Histone chaperones and nucleosome assembly
    • Akey, C.W., and Luger, K. (2003). Histone chaperones and nucleosome assembly. Curr. Opin. Struct. Biol. 13, 6-14.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 6-14
    • Akey, C.W.1    Luger, K.2
  • 38
    • 0033845836 scopus 로고    scopus 로고
    • CAF-1 and the inheritance of chromatin states: At the crossroads of DNA replication and repair
    • Ridgway, P., and Almouzni, G. (2000). CAF-1 and the inheritance of chromatin states: at the crossroads of DNA replication and repair. J. Cell Sci. 113, 2647-2658.
    • (2000) J. Cell Sci. , vol.113 , pp. 2647-2658
    • Ridgway, P.1    Almouzni, G.2
  • 39
    • 0034659231 scopus 로고    scopus 로고
    • De novo nucleosome assembly: New pieces in an old puzzle
    • Verreault, A. (2000). De novo nucleosome assembly: new pieces in an old puzzle. Genes Dev. 14, 1430-1438.
    • (2000) Genes Dev. , vol.14 , pp. 1430-1438
    • Verreault, A.1
  • 40
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., Schmidt, C.J., Nambudripad, R., and Smith, T.F. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 42
    • 0034761101 scopus 로고    scopus 로고
    • The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly
    • Dutta, S., Akey, I.V., Dingwall, C., Hartman, K.L., Laue, T., Nolte, R.T., Head, J.F., and Akey, C.W. (2001). The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly. Mol. Cell 8, 841-853.
    • (2001) Mol. Cell , vol.8 , pp. 841-853
    • Dutta, S.1    Akey, I.V.2    Dingwall, C.3    Hartman, K.L.4    Laue, T.5    Nolte, R.T.6    Head, J.F.7    Akey, C.W.8
  • 43
    • 0037313853 scopus 로고    scopus 로고
    • The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding
    • Camb
    • Namboodiri, V.M., Dutta, S., Akey, I.V., Head, J.F., and Akey, C.W. (2003). The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding. Structure (Camb) 11, 175-186.
    • (2003) Structure , vol.11 , pp. 175-186
    • Namboodiri, V.M.1    Dutta, S.2    Akey, I.V.3    Head, J.F.4    Akey, C.W.5
  • 44
    • 0023663912 scopus 로고
    • Two complexes that contain histones are required for nucleosome assembly in vitro: Role of nucleoplasmin and N1 in Xenopus egg extracts
    • Dilworth, S.M., Black, S.J., and Laskey, R.A. (1987). Two complexes that contain histones are required for nucleosome assembly in vitro: role of nucleoplasmin and N1 in Xenopus egg extracts. Cell 51, 1009-1018.
    • (1987) Cell , vol.51 , pp. 1009-1018
    • Dilworth, S.M.1    Black, S.J.2    Laskey, R.A.3
  • 45
    • 0029778870 scopus 로고    scopus 로고
    • ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster
    • Ito, T., Tyler, J.K., Bulger, M., Kobayashi, R., and Kadonaga, J.T. (1996). ATP-facilitated chromatin assembly with a nucleoplasmin-like protein from Drosophila melanogaster. J. Biol. Chem. 271, 25041-25048.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25041-25048
    • Ito, T.1    Tyler, J.K.2    Bulger, M.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 46
    • 0242497812 scopus 로고    scopus 로고
    • Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino terminal histone tails
    • Published online August 19, 2003. 10.1074/jbc.M305636200
    • McBryant, S.J., Abernathy, S.M., Laybourn, P.J., Nyborg, J.K., and Luger, K. (2003). Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino terminal histone tails. J. Biol. Chem. 278, 44574-44583. Published online August 19, 2003. 10.1074/jbc.M305636200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44574-44583
    • McBryant, S.J.1    Abernathy, S.M.2    Laybourn, P.J.3    Nyborg, J.K.4    Luger, K.5
  • 47
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 48
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust, R.B., and Waugh, D.S. (1999). Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8, 1668-1674.
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 49
    • 0018435056 scopus 로고
    • A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite
    • Simon, R.H., and Felsenfeld, G. (1979). A new procedure for purifying histone pairs H2A + H2B and H3 + H4 from chromatin using hydroxylapatite. Nucleic Acids Res. 6, 689-696.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 689-696
    • Simon, R.H.1    Felsenfeld, G.2
  • 50
    • 0029973557 scopus 로고    scopus 로고
    • Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors
    • Adams, P.D., Sellers, W.R., Sharma, S.K., Wu, A.D., Nalin, C.M., and Kaelin, W.G., Jr. (1996). Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors. Mol. Cell. Biol. 16, 6623-6633.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6623-6633
    • Adams, P.D.1    Sellers, W.R.2    Sharma, S.K.3    Wu, A.D.4    Nalin, C.M.5    Kaelin Jr., W.G.6
  • 52
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T., and Berendzen, J. (1999). Automated structure solution for MIR and MAD. Acta Crystallogr. D55, 849-861.
    • (1999) Acta Crystallogr. , Issue.D55 , pp. 849-861
    • Terwilliger, T.1    Berendzen, J.2
  • 53
    • 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., and Kjeldgaard, M. (1991). 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) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 55
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R., MacArthur, M., Moss, D., and Thornton, J. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4
  • 56
    • 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., and Higgins, D.G. (1997). The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
    • (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
  • 58
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G.J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 59
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 60
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser, F., Pupko, T., Paz, I., Bell, R.E., Bechor-Shental, D., Martz, E., and Ben-Tal, N. (2003). ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19, 163-164.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7


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