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Volumn 9, Issue 1, 1999, Pages 48-55

Combinatorial gene regulation by eukaryotic transcription factors

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 0032848185     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)80007-4     Document Type: Article
Times cited : (50)

References (52)
  • 1
    • 0028337542 scopus 로고
    • Transcriptional activation: A complex puzzle with few easy pieces
    • Tjian R, Maniatis T Transcriptional activation: a complex puzzle with few easy pieces. Cell. 77:1994;5-8.
    • (1994) Cell , vol.77 , pp. 5-8
    • Tjian, R.1    Maniatis, T.2
  • 3
    • 0029870514 scopus 로고    scopus 로고
    • Crystal structure of a yeast TFIIA/TBP/DNA complex
    • Tan S, Hunziker Y, Sargent DF, Richmond TJ Crystal structure of a yeast TFIIA/TBP/DNA complex. Nature. 381:1996;127-151.
    • (1996) Nature , vol.381 , pp. 127-151
    • Tan, S.1    Hunziker, Y.2    Sargent, D.F.3    Richmond, T.J.4
  • 4
    • 0029930779 scopus 로고    scopus 로고
    • Crystal structure of the yeast TFIIA/TBP/DNA complex
    • Geiger JH, Hahn S, Lee S, Sigler PB Crystal structure of the yeast TFIIA/TBP/DNA complex. Science. 272:1996;830-836.
    • (1996) Science , vol.272 , pp. 830-836
    • Geiger, J.H.1    Hahn, S.2    Lee, S.3    Sigler, P.B.4
  • 5
    • 0032483544 scopus 로고    scopus 로고
    • Crystal structure of a Smad MH1 domain bound to DNA: Insights on DNA binding in TGF-β signaling
    • This paper describes the first crystal structure of the DNA-binding domain from a Smad family protein in complex with DNA, showing a novel DNA-binding mode involving a β hairpin bound in the major groove.
    • Shi Y, Wang YF, Jayaraman L, Yang H, Massague J, Pavletich NP Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-β signaling. Cell. 94:1998;585-594. This paper describes the first crystal structure of the DNA-binding domain from a Smad family protein in complex with DNA, showing a novel DNA-binding mode involving a β hairpin bound in the major groove.
    • (1998) Cell , vol.94 , pp. 585-594
    • Shi, Y.1    Wang, Y.F.2    Jayaraman, L.3    Yang, H.4    Massague, J.5    Pavletich, N.P.6
  • 6
    • 0031933646 scopus 로고    scopus 로고
    • Structure of IRF-1 with bound DNA reveals determinants of interferon regulation
    • The first crystal structure determination of a DNA-binding domain from the interferon regulatory factor (IRF) family of proteins in complex with DNA, showing a variant of the 'helix-turn-helix' DNA-binding motif.
    • Escalante CR, Yie J, Thanos D, Aggarwal AK Structure of IRF-1 with bound DNA reveals determinants of interferon regulation. Nature. 391:1998;103-106. The first crystal structure determination of a DNA-binding domain from the interferon regulatory factor (IRF) family of proteins in complex with DNA, showing a variant of the 'helix-turn-helix' DNA-binding motif.
    • (1998) Nature , vol.391 , pp. 103-106
    • Escalante, C.R.1    Yie, J.2    Thanos, D.3    Aggarwal, A.K.4
  • 7
    • 0032556894 scopus 로고    scopus 로고
    • Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA
    • Chen FE, Huang DB, Chen YQ, Ghosh G Crystal structure of p50/p65 heterodimer of transcription factor NF-κB bound to DNA. Nature. 391:1998;410-413.
    • (1998) Nature , vol.391 , pp. 410-413
    • Chen, F.E.1    Huang, D.B.2    Chen, Y.Q.3    Ghosh, G.4
  • 8
    • 0032524465 scopus 로고    scopus 로고
    • Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 Å resolution
    • A recent example showing that binding to a nonconsensus DNA site by a transcription factor involves only localized changes at the protein-DNA interface.
    • Parraga A, Bellsolell L, Ferre-D'Amare AR, Burley SK Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 Å resolution. Structure. 6:1998;661-672. A recent example showing that binding to a nonconsensus DNA site by a transcription factor involves only localized changes at the protein-DNA interface.
    • (1998) Structure , vol.6 , pp. 661-672
    • Parraga, A.1    Bellsolell, L.2    Ferre-D'Amare, A.R.3    Burley, S.K.4
  • 9
    • 0032509980 scopus 로고    scopus 로고
    • Crystal structure of the yeast MATα2/MCM1/ DNA ternary complex
    • A higher order eukaryotic transcription factor complex bound to DNA, demonstrating the importance of protein-protein interactions in the assembly.
    • Tan S, Richmond TJ Crystal structure of the yeast MATα2/MCM1/ DNA ternary complex. Nature. 391:1998;660-666. A higher order eukaryotic transcription factor complex bound to DNA, demonstrating the importance of protein-protein interactions in the assembly.
    • (1998) Nature , vol.391 , pp. 660-666
    • Tan, S.1    Richmond, T.J.2
  • 10
    • 0032485391 scopus 로고    scopus 로고
    • Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
    • A higher order eukaryotic transcription factor complex bound to DNA, demonstrating the importance of protein-protein interactions in the assembly.
    • Chen L, Glover JN, Hogan PG, Rao A, Harrison SC Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature. 392:1998;42-48. A higher order eukaryotic transcription factor complex bound to DNA, demonstrating the importance of protein-protein interactions in the assembly.
    • (1998) Nature , vol.392 , pp. 42-48
    • Chen, L.1    Glover, J.N.2    Hogan, P.G.3    Rao, A.4    Harrison, S.C.5
  • 11
    • 0032512459 scopus 로고    scopus 로고
    • The structure of GABPα/β: An ETS domain-ankyrin repeat heterodimer bound to DNA
    • ••], in that one component does not bind DNA directly; however, the protein-protein interactions are equally important for the assembly and the enhanced DNA binding. It is also one of the first two structures to show the detailed protein-protein interactions mediated by ankyrin repeats that play important roles in a wide range of physiologically important protein complexes.
    • ••], in that one component does not bind DNA directly; however, the protein-protein interactions are equally important for the assembly and the enhanced DNA binding. It is also one of the first two structures to show the detailed protein-protein interactions mediated by ankyrin repeats that play important roles in a wide range of physiologically important protein complexes.
    • (1998) Science , vol.279 , pp. 1037-1041
    • Batchelor, A.H.1    Piper, D.E.2    De La Brousse, F.C.3    McKnight, S.L.4    Wolberger, C.5
  • 12
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator-coactivator interactions
    • The first detailed structural characterization of the interactions between an activation domain (CREB) and a coactivator (CBP).
    • Radhakrishnan I, Perez AG, Parker D, Dyson HJ, Montminy MR, Wright PE Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator-coactivator interactions. Cell. 91:1997;741-752. The first detailed structural characterization of the interactions between an activation domain (CREB) and a coactivator (CBP).
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Perez, A.G.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 13
    • 0030756675 scopus 로고    scopus 로고
    • Induced α helix in the VP16 activation domain upon binding to a human TAF
    • The first structural characterization of the interactions between VP16 and TAF31, using NMR spectroscopy and biochemical methods.
    • Uesugi M, Nyanguile O, Lu H, Levine AJ, Verdine GL Induced α helix in the VP16 activation domain upon binding to a human TAF. Science. 277:1997;1310-1313. The first structural characterization of the interactions between VP16 and TAF31, using NMR spectroscopy and biochemical methods.
    • (1997) Science , vol.277 , pp. 1310-1313
    • Uesugi, M.1    Nyanguile, O.2    Lu, H.3    Levine, A.J.4    Verdine, G.L.5
  • 16
    • 0031310825 scopus 로고    scopus 로고
    • The mechanism of transcriptional synergy of an in vitro assembled interferon-β enhanceosome
    • A detailed biochemical study on enhanceosome assembly, demonstrating a direct correlation between cooperative DNA binding and transcriptional synergy in the context of an assembled enhancer.
    • Kim TK, Maniatis T The mechanism of transcriptional synergy of an in vitro assembled interferon-β enhanceosome. Mol Cell. 1:1997;119-129. A detailed biochemical study on enhanceosome assembly, demonstrating a direct correlation between cooperative DNA binding and transcriptional synergy in the context of an assembled enhancer.
    • (1997) Mol Cell , vol.1 , pp. 119-129
    • Kim, T.K.1    Maniatis, T.2
  • 17
    • 0028329603 scopus 로고
    • Interleukin-2 transcription is regulated in vivo at the level of coordinated binding of both constitutive and regulated factors
    • Garrity PA, Chen D, Rothenberg EV, Wold BJ Interleukin-2 transcription is regulated in vivo at the level of coordinated binding of both constitutive and regulated factors. Mol Cell Biol. 14:1994;2159-2169.
    • (1994) Mol Cell Biol , vol.14 , pp. 2159-2169
    • Garrity, P.A.1    Chen, D.2    Rothenberg, E.V.3    Wold, B.J.4
  • 18
    • 0029060412 scopus 로고
    • Higher-order nucleoprotein complexes in transcription: Analogies with site-specific recombination
    • Grosschedl R Higher-order nucleoprotein complexes in transcription: analogies with site-specific recombination. Curr Opin Cell Biol. 7:1995;362-370.
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 362-370
    • Grosschedl, R.1
  • 19
    • 0029617947 scopus 로고
    • Virus induction of human IFNβ gene expression requires the assembly of an enhanceosome
    • Thanos D, Maniatis T Virus induction of human IFNβ gene expression requires the assembly of an enhanceosome. Cell. 83:1995;1091-1100.
    • (1995) Cell , vol.83 , pp. 1091-1100
    • Thanos, D.1    Maniatis, T.2
  • 20
    • 0000017176 scopus 로고
    • Combinatorial regulation at a mammalian composite response element
    • S.L. McKnight, & K.R. Yamamoto. New York: Cold Spring Harbor Laboratory Press
    • Yamamoto KR, Pearce D, Thomas J, Miner JN Combinatorial regulation at a mammalian composite response element. McKnight SL, Yamamoto KR Transcriptional Regulation. 1992;1169-1192 Cold Spring Harbor Laboratory Press, New York.
    • (1992) Transcriptional Regulation , pp. 1169-1192
    • Yamamoto, K.R.1    Pearce, D.2    Thomas, J.3    Miner, J.N.4
  • 21
    • 0001294043 scopus 로고
    • A combinatorial regulatory circuit in budding yeast
    • S.L. McKnight, & K.R. Yamamoto. New York: Cold Spring Harbor Laboratory Press
    • Johnson A A combinatorial regulatory circuit in budding yeast. McKnight SL, Yamamoto KR Transcriptional Regulation, vol 2. 1992;975-1006 Cold Spring Harbor Laboratory Press, New York.
    • (1992) Transcriptional Regulation, Vol 2 , pp. 975-1006
    • Johnson, A.1
  • 22
    • 0022521842 scopus 로고
    • Cooperative binding of lambda repressors to sites separated by integral turns of the DNA helix
    • Hochschild A, Ptashne M Cooperative binding of lambda repressors to sites separated by integral turns of the DNA helix. Cell. 44:1986;681-687.
    • (1986) Cell , vol.44 , pp. 681-687
    • Hochschild, A.1    Ptashne, M.2
  • 23
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne M, Gann A Transcriptional activation by recruitment. Nature. 386:1997;569-577.
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 24
    • 0029154633 scopus 로고
    • Molecular mechanisms of cell-type determination in budding yeast
    • Johnson AD Molecular mechanisms of cell-type determination in budding yeast. Curr Opin Genet Dev. 5:1995;552-558.
    • (1995) Curr Opin Genet Dev , vol.5 , pp. 552-558
    • Johnson, A.D.1
  • 25
    • 0028828745 scopus 로고
    • Crystal structure of the MATa1/MAT α2 homeodomain heterodimer bound to DNA
    • Li T, Stark MR, Johnson AD, Wolberger C Crystal structure of the MATa1/MAT α2 homeodomain heterodimer bound to DNA. Science. 270:1995;262-269.
    • (1995) Science , vol.270 , pp. 262-269
    • Li, T.1    Stark, M.R.2    Johnson, A.D.3    Wolberger, C.4
  • 26
    • 0027509952 scopus 로고
    • A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein
    • Vershon AK, Johnson AD A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein. Cell. 72:1993;105-112.
    • (1993) Cell , vol.72 , pp. 105-112
    • Vershon, A.K.1    Johnson, A.D.2
  • 27
    • 0028342952 scopus 로고
    • Signal transmission between the plasma membrane and nucleus of T lymphocytes
    • Crabtree GR, Clipstone NA Signal transmission between the plasma membrane and nucleus of T lymphocytes. Annu Rev Biochem. 63:1994;1045-1083.
    • (1994) Annu Rev Biochem , vol.63 , pp. 1045-1083
    • Crabtree, G.R.1    Clipstone, N.A.2
  • 28
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol. 15:1997;707-747.
    • (1997) Annu Rev Immunol , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 29
    • 0030482408 scopus 로고    scopus 로고
    • The leucine zipper domain controls the orientation of AP-1 in the NFAT-AP-1-DNA complex
    • Erlanson DA, Chytil M, Verdine GL The leucine zipper domain controls the orientation of AP-1 in the NFAT-AP-1-DNA complex. Chem Biol. 3:1996;981-991.
    • (1996) Chem Biol , vol.3 , pp. 981-991
    • Erlanson, D.A.1    Chytil, M.2    Verdine, G.L.3
  • 30
    • 12644271902 scopus 로고    scopus 로고
    • A critical arginine residue mediates cooperativity in the contact interface between transcription factors NFAT and AP-1
    • Peterson BR, Sun LJ, Verdine GL A critical arginine residue mediates cooperativity in the contact interface between transcription factors NFAT and AP-1. Proc Natl Acad Sci USA. 93:1996;13671-13676.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13671-13676
    • Peterson, B.R.1    Sun, L.J.2    Verdine, G.L.3
  • 31
    • 0030974118 scopus 로고    scopus 로고
    • Dual role of the nuclear factor of activated T cells insert region in DNA recognition and cooperative contacts to activator protein 1
    • Sun LJ, Peterson BR, Verdine GL Dual role of the nuclear factor of activated T cells insert region in DNA recognition and cooperative contacts to activator protein 1. Proc Natl Acad Sci USA. 94:1997;4919-4924.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4919-4924
    • Sun, L.J.1    Peterson, B.R.2    Verdine, G.L.3
  • 33
    • 0025081214 scopus 로고
    • Transcription factor interactions: Selectors of positive or negative regulation from a single DNA element
    • Diamond MI, Miner JN, Yoshinaga SK, Yamamoto KR Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science. 249:1990;1266-1272.
    • (1990) Science , vol.249 , pp. 1266-1272
    • Diamond, M.I.1    Miner, J.N.2    Yoshinaga, S.K.3    Yamamoto, K.R.4
  • 34
    • 0025217856 scopus 로고
    • The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation
    • Davis RL, Cheng PF, Lassar AB, Weintraub H The MyoD DNA binding domain contains a recognition code for muscle-specific gene activation. Cell. 60:1990;733-746.
    • (1990) Cell , vol.60 , pp. 733-746
    • Davis, R.L.1    Cheng, P.F.2    Lassar, A.B.3    Weintraub, H.4
  • 35
    • 0028790477 scopus 로고
    • Altered DNA recognition and bending by insertions in the α2 tail of the yeast α1/α2 homeodomain heterodimer
    • Jin Y, Mead J, Li T, Wolberger C, Vershon AK Altered DNA recognition and bending by insertions in the α2 tail of the yeast α1/α2 homeodomain heterodimer. Science. 270:1995;290-293.
    • (1995) Science , vol.270 , pp. 290-293
    • Jin, Y.1    Mead, J.2    Li, T.3    Wolberger, C.4    Vershon, A.K.5
  • 36
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad F, Perlmann T, Evans RM, Sigler PB Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature. 375:1995;203-211.
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 38
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover JN, Harrison SC Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature. 373:1995;257-261.
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2
  • 40
    • 0032499801 scopus 로고    scopus 로고
    • Three-dimensional structure of the Stat3β homodimer bound to DNA
    • ••], the first for the STAT family, show the unique features of the STAT family proteins, whose multiple functional domains are highly integrated at the structural level.
    • ••], the first for the STAT family, show the unique features of the STAT family proteins, whose multiple functional domains are highly integrated at the structural level.
    • (1998) Nature , vol.394 , pp. 145-151
    • Becker, S.1    Groner, B.2    Muller, C.W.3
  • 41
    • 0032512661 scopus 로고    scopus 로고
    • Structure of the amino-terminal protein interaction domain of STAT-4
    • This is the first crystallographic study of potential protein-binding surfaces from the conserved STAT N-terminal domain. The structural features of the dimer interface observed in the crystal structure have general implications for the DNA-binding-dependent, higher order complex assembly of transcription factors.
    • Vinkemeier U, Moarefi I, Darnell J Jr., Kuriyan J Structure of the amino-terminal protein interaction domain of STAT-4. Science. 279:1998;1048-1052. This is the first crystallographic study of potential protein-binding surfaces from the conserved STAT N-terminal domain. The structural features of the dimer interface observed in the crystal structure have general implications for the DNA-binding-dependent, higher order complex assembly of transcription factors.
    • (1998) Science , vol.279 , pp. 1048-1052
    • Vinkemeier, U.1    Moarefi, I.2    Darnell J., Jr.3    Kuriyan, J.4
  • 42
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin JA, Yamamoto KR Allosteric effects of DNA on transcriptional regulators. Nature. 392:1998;885-888.
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 43
    • 0028979479 scopus 로고
    • Structure of NF-κB p50 homodimer bound to a κb site
    • Ghosh G, van Duyne G, Ghosh S, Sigler PB Structure of NF-κB p50 homodimer bound to a κB site. Nature. 373:1995;303-310.
    • (1995) Nature , vol.373 , pp. 303-310
    • Ghosh, G.1    Van Duyne, G.2    Ghosh, S.3    Sigler, P.B.4
  • 45
    • 0029053852 scopus 로고
    • Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins
    • Hoey T, Sun YL, Williamson K, Xu X Isolation of two new members of the NF-AT gene family and functional characterization of the NF-AT proteins. Immunity. 2:1995;461-472.
    • (1995) Immunity , vol.2 , pp. 461-472
    • Hoey, T.1    Sun, Y.L.2    Williamson, K.3    Xu, X.4
  • 46
    • 0028857929 scopus 로고
    • Novel NFAT sites that mediate activation of the interleukin-2 promoter in response to T-cell receptor stimulation
    • Rooney JW, Sun YL, Glimcher LH, Hoey T Novel NFAT sites that mediate activation of the interleukin-2 promoter in response to T-cell receptor stimulation. Mol Cell Biol. 15:1995;6299-6310.
    • (1995) Mol Cell Biol , vol.15 , pp. 6299-6310
    • Rooney, J.W.1    Sun, Y.L.2    Glimcher, L.H.3    Hoey, T.4
  • 47
    • 0039706410 scopus 로고    scopus 로고
    • Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor
    • The structure not only expands the Ig DNA-binding protein family, but it also reveals unusual minor groove DNA binding by an α helix. This observation is important for understanding the general mechanisms of DNA recognition by proteins.
    • Muller CW, Herrmann BG Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor. Nature. 389:1997;884-888. The structure not only expands the Ig DNA-binding protein family, but it also reveals unusual minor groove DNA binding by an α helix. This observation is important for understanding the general mechanisms of DNA recognition by proteins.
    • (1997) Nature , vol.389 , pp. 884-888
    • Muller, C.W.1    Herrmann, B.G.2
  • 48
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y, Gorina S, Jeffrey PD, Pavletich NP Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science. 265:1994;346-355.
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 49
    • 0031749528 scopus 로고    scopus 로고
    • A new DNA-binding motif in the Skn-1 binding domain-DNA complex
    • This structure shows a novel DNA-binding domain that can be regarded as a hybridization of parts of other known DNA-binding motifs, illustrating a unique way of varying DNA-binding motifs in order to generate new DNA-binding functions by nature.
    • Rupert PB, Daughdrill GW, Bowerman B, Matthews BW A new DNA-binding motif in the Skn-1 binding domain-DNA complex. Nat Struct Biol. 5:1998;484-491. This structure shows a novel DNA-binding domain that can be regarded as a hybridization of parts of other known DNA-binding motifs, illustrating a unique way of varying DNA-binding motifs in order to generate new DNA-binding functions by nature.
    • (1998) Nat Struct Biol , vol.5 , pp. 484-491
    • Rupert, P.B.1    Daughdrill, G.W.2    Bowerman, B.3    Matthews, B.W.4
  • 51
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery DM, Kalkhoven E, Hoare S, Parker MG A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature. 387:1997;733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 52
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1


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