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Volumn 94, Issue 6, 1998, Pages 829-839

Structure of type IIβ phosphatidylinositol phosphate kinase: A protein kinase fold flattened for interfacial phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHATIDYLINOSITOL 4 PHOSPHATE KINASE; POLYPHOSPHOINOSITIDE; PROTEIN KINASE; 1-PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; BACTERIAL PROTEIN; PHOSPHOTRANSFERASE;

EID: 0032544230     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81741-9     Document Type: Article
Times cited : (199)

References (57)
  • 1
    • 0025163075 scopus 로고
    • The human erythrocyte contains two forms of phosphatidylinositol-4-phosphate 5-kinase which are differentially active toward membranes
    • Bazenet, C.E., Ruano, A.R., Brockman, J.L., and Anderson, R.A. (1990). The human erythrocyte contains two forms of phosphatidylinositol-4-phosphate 5-kinase which are differentially active toward membranes. J. Biol. Chem. 265, 18012-18022.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18012-18022
    • Bazenet, C.E.1    Ruano, A.R.2    Brockman, J.L.3    Anderson, R.A.4
  • 2
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signaling
    • Berridge, M.J. (1993). Inositol trisphosphate and calcium signaling. Nature 361, 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 4
    • 0028812255 scopus 로고
    • The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases
    • Boronenkov, I.V., and Anderson, R.A. (1995). The sequence of phosphatidylinositol-4-phosphate 5-kinase defines a novel family of lipid kinases. J. Biol. Chem. 270, 2881-2884.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2881-2884
    • Boronenkov, I.V.1    Anderson, R.A.2
  • 5
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 8
    • 0031047829 scopus 로고    scopus 로고
    • A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase
    • Castellino, A.M., Parker, G.J., Boronenkov, I.V., Anderson, R.A., and Chao, M.V. (1997). A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase. J. Biol. Chem. 272, 5861-5870.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5861-5870
    • Castellino, A.M.1    Parker, G.J.2    Boronenkov, I.V.3    Anderson, R.A.4    Chao, M.V.5
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 670-673.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 670-673
  • 12
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli, P., Emr, S.D., McPherson, P.S., and Novick, P. (1996). Phosphoinositides as regulators in membrane traffic. Science 271, 1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 13
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 14
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha, N., and Irvine, R.F. (1995). Phospholipid signaling. Cell 80, 269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 15
    • 0030669546 scopus 로고    scopus 로고
    • Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis
    • Dove, S.K., Cooke, F.T., Douglas, M.R., Sayers, L.G., Parker, P.J., and Michell, R.H. (1997). Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis. Nature 390, 187-192.
    • (1997) Nature , vol.390 , pp. 187-192
    • Dove, S.K.1    Cooke, F.T.2    Douglas, M.R.3    Sayers, L.G.4    Parker, P.J.5    Michell, R.H.6
  • 16
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R., and Huber, R. (1991). Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallogr. A47, 392-400.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 17
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ
    • Essen, L.O., Perisic, O., Cheung, R., Katan, M., and Williams, R.L. (1996). Crystal structure of a mammalian phosphoinositide-specific phospholipase Cδ. Nature 380, 595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 18
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, K.M., Lemmon, M.A., Schlessinger, J., and Sigler, P.B. (1995). Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 19
    • 0030818593 scopus 로고    scopus 로고
    • PHASES-95: A program package for the processing and analysis of diffraction data from macromolecules
    • Furey, W., and Swaminathan, S. (1997). PHASES-95: a program package for the processing and analysis of diffraction data from macromolecules. Methods Enzymol. 277, 590-620.
    • (1997) Methods Enzymol. , vol.277 , pp. 590-620
    • Furey, W.1    Swaminathan, S.2
  • 21
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase catalytic domain structure and classification
    • Hanks, S.K., and Hunter, T. (1995). Protein kinases 6. The eukaryotic protein kinase superfamily: kinase catalytic domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 22
    • 0030682410 scopus 로고    scopus 로고
    • Inositol lipid pathways turn turtle
    • Hinchliffe, K., and Irvine, R. (1997). Inositol lipid pathways turn turtle. Nature 390, 123-124.
    • (1997) Nature , vol.390 , pp. 123-124
    • Hinchliffe, K.1    Irvine, R.2
  • 23
    • 0032546932 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis
    • Homma, K., Terui, S., Minemura, M., Qadota, H., Anraku, Y., Kanaho, Y., and Ohya, Y.J. (1998). Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis. J. Biol. Chem. 273, 15779-15786.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15779-15786
    • Homma, K.1    Terui, S.2    Minemura, M.3    Qadota, H.4    Anraku, Y.5    Kanaho, Y.6    Ohya, Y.J.7
  • 24
    • 0030830868 scopus 로고    scopus 로고
    • Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
    • Hon, W.-C., McKay, G.A., Thompson, P.R., Sweet, R.M., Yang, S.C., Wright, G.D., and Berghuis, A.M. (1997). Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell 89, 887-895.
    • (1997) Cell , vol.89 , pp. 887-895
    • Hon, W.-C.1    McKay, G.A.2    Thompson, P.R.3    Sweet, R.M.4    Yang, S.C.5    Wright, G.D.6    Berghuis, A.M.7
  • 25
    • 0027361002 scopus 로고
    • Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85
    • Hu, P., Mondino, A., Skolnik, E.Y., and Schlessinger, J. (1993). Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol. Cell. Biol. 13, 7677-7688.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7677-7688
    • Hu, P.1    Mondino, A.2    Skolnik, E.Y.3    Schlessinger, J.4
  • 26
    • 0030755311 scopus 로고    scopus 로고
    • Protein kinase C and phospholipase C: Bilayer interactions and regulation
    • Hurley, J.H., and Grobler, J.A. (1997). Protein kinase C and phospholipase C: bilayer interactions and regulation. Curr. Opin. Struct. Biol. 7, 557-565.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 557-565
    • Hurley, J.H.1    Grobler, J.A.2
  • 27
    • 0032502721 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases: Cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family
    • Ishihara, H., Shibasaki, Y., Kizuki, N., Wada, T., Yazaki, Y., Asano, T., and Oka, Y. (1998). Type I phosphatidylinositol-4-phosphate 5-kinases: cloning of the third isoform and deletion/substitution analysis of members of this novel lipid kinase family. J. Biol. Chem. 273, 8741-8748.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8741-8748
    • Ishihara, H.1    Shibasaki, Y.2    Kizuki, N.3    Wada, T.4    Yazaki, Y.5    Asano, T.6    Oka, Y.7
  • 28
    • 0026206788 scopus 로고
    • Sparse matrix sampling: A screening method for crystallization of proteins
    • Jancarik, J., and Kim, S.-H. (1991). Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Crystallogr. 24, 409-411.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 409-411
    • Jancarik, J.1    Kim, S.-H.2
  • 29
    • 0028346383 scopus 로고
    • Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid
    • Jenkins, G.H., Fisette, P.L., and Anderson, R.A. (1994). Type I phosphatidylinositol 4-phosphate 5-kinase isoforms are specifically stimulated by phosphatidic acid. J. Biol. Chem. 269, 11547-11554.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11547-11554
    • Jenkins, G.H.1    Fisette, P.L.2    Anderson, R.A.3
  • 30
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L.N., Noble, M.E.M., and Owen, D.J. (1996). Active and inactive protein kinases: structural basis for regulation. Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 31
    • 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. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 32
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J.H., Ten Eyck, L.F., Ashford, V.A., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991a). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-414.
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 33
    • 0026326821 scopus 로고
    • Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • Knighton, D.R., Zheng, J.H., Ten Eyck, L.F., Xuong, N.H., Taylor, S.S., and Sowadski, J.M. (1991b). Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420.
    • (1991) Science , vol.253 , pp. 414-420
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Xuong, N.H.4    Taylor, S.S.5    Sowadski, J.M.6
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 35
    • 0001513484 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1993) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 36
    • 16944365378 scopus 로고    scopus 로고
    • Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family
    • Loijens, J.C., and Anderson, R.A. (1996). Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of this novel lipid kinase family. J. Biol. Chem. 271, 32937-32943.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32937-32943
    • Loijens, J.C.1    Anderson, R.A.2
  • 38
    • 0023714421 scopus 로고
    • A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha
    • Maldonado, F., and Hanks, S.K. (1988). A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha. Nucleic Acids Res. 16, 8189-8190.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 8189-8190
    • Maldonado, F.1    Hanks, S.K.2
  • 39
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 40
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • Merritt, E.A., and Bacon, D.J. (1997). Raster3D version 2.0: a program for photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 41
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray, D., Ben-Tal, N., Honig, B., and McLaughlin, S. (1997). Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure 5, 985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 42
    • 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 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 43
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. (1995). Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9, 484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 44
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 45
    • 0018788297 scopus 로고
    • The molecular structure of lecithin hydrates
    • Pascher, I., and Pearson, R.H. (1979). The molecular structure of lecithin hydrates. Nature 281, 499-501.
    • (1979) Nature , vol.281 , pp. 499-501
    • Pascher, I.1    Pearson, R.H.2
  • 46
    • 0030721527 scopus 로고    scopus 로고
    • A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate
    • Rameh, L.E., Tolias, K.F., Duckworth, B.C., and Cantley, L.C. (1997). A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390, 192-196.
    • (1997) Nature , vol.390 , pp. 192-196
    • Rameh, L.E.1    Tolias, K.F.2    Duckworth, B.C.3    Cantley, L.C.4
  • 47
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPs34 gene essential for protein sorting
    • Schu, P.W., Takegawa, K., Fry, M.J., Stack, J.H., Waterfield, M.D., and Emr, S.D. (1993). Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260, 88-91.
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.W.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 48
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I., and Kuriyan, J. (1997). Crystal structure of the Src family tyrosine kinase Hck. Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 49
    • 0028233432 scopus 로고
    • Annexin structure and membrane interactions: A molecular perspective
    • Swairjo, M.A.,and Seaton, B.A. (1994). Annexin structure and membrane interactions: a molecular perspective. Annu. Rev. Biophys. Biomol. Struct. 23, 193-213.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 193-213
    • Swairjo, M.A.1    Seaton, B.A.2
  • 50
    • 0030499814 scopus 로고    scopus 로고
    • Correlated phasing of multiple isomorphous replacement data
    • Terwilliger, T.C., and Berendzen, J. (1996). Correlated phasing of multiple isomorphous replacement data. Acta Crystallogr. D52, 749-757.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 749-757
    • Terwilliger, T.C.1    Berendzen, J.2
  • 52
    • 0028032480 scopus 로고
    • Cloning and characterization of a human phosphatidylinositol 4-kinase
    • Wong, K., and Cantley, L.C. (1994). Cloning and characterization of a human phosphatidylinositol 4-kinase. J. Biol. Chem. 269, 2881-2884.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2881-2884
    • Wong, K.1    Cantley, L.C.2
  • 53
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • Wymann, M.P., Bulgarelli-Leva, G., Zvelebil, M.J., Pirola, L., Vanhaesebroeck, B., Waterfield, M.D., and Panayotou, G. (1996). Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol. 16, 1722-1733.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722-1733
    • Wymann, M.P.1    Bulgarelli-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroeck, B.5    Waterfield, M.D.6    Panayotou, G.7
  • 54
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S.C., and Eck, M.J. (1997). Three-dimensional structure of the tyrosine kinase c-Src. Nature 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 55
    • 0029024442 scopus 로고
    • Novel PI(4)P 5-kinase homolog, Fab1p, is essential for normal vacuole function and morphology in yeast
    • Yamamoto, A., Dewald, A.B., Boronenkov, I.V., Anderson, R.A., Emr, S.D., and Koshland, D.E. (1995). Novel PI(4)P 5-kinase homolog, Fab1p, is essential for normal vacuole function and morphology in yeast. Mol. Biol. Cell. 6, 525-539.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 525-539
    • Yamamoto, A.1    Dewald, A.B.2    Boronenkov, I.V.3    Anderson, R.A.4    Emr, S.D.5    Koshland, D.E.6
  • 56
    • 0028218165 scopus 로고
    • Genetic interactions among genes involved in the STT4-PKC1 pathway of saccharomyces cerevisiae
    • Yoshida, S., Ohya, Y., Nakano, A., and Anraku, Y. (1994). Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae. Mol. Gen. Genet. 242, 631-640.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 631-640
    • Yoshida, S.1    Ohya, Y.2    Nakano, A.3    Anraku, Y.4


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