메뉴 건너뛰기




Volumn 31, Issue 4, 1999, Pages 1255-1264

The yeast inositol monophosphatase is a lithium- and sodium-sensitive enzyme encoded by a non-essential gene pair

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; INOSITOL PHOSPHATE; LITHIUM; RECOMBINANT PROTEIN; SODIUM;

EID: 0033067784     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01267.x     Document Type: Article
Times cited : (53)

References (56)
  • 1
    • 0028946336 scopus 로고
    • Structure and mechanism of inositol monophosphatase
    • Atack, J.R., Broughton, H.B., and Pollack, S.J. (1995) Structure and mechanism of inositol monophosphatase. FEBS Lett 361: 1-7.
    • (1995) FEBS Lett , vol.361 , pp. 1-7
    • Atack, J.R.1    Broughton, H.B.2    Pollack, S.J.3
  • 2
    • 0023810846 scopus 로고
    • Purification and properties of myo-inositol-1-phosphatase from bovine brain
    • Attwood, P.V., Ducep, J.B., and Chanal, M.C. (1988) Purification and properties of myo-inositol-1-phosphatase from bovine brain. Biochem J 253: 387-394.
    • (1988) Biochem J , vol.253 , pp. 387-394
    • Attwood, P.V.1    Ducep, J.B.2    Chanal, M.C.3
  • 3
    • 0028236025 scopus 로고
    • Toward a crystal-clear view of lithium's site of action
    • Baraban, J.M. (1994) Toward a crystal-clear view of lithium's site of action. Proc Natl Acad Sci USA 91: 5738-5739.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5738-5739
    • Baraban, J.M.1
  • 4
    • 0029789334 scopus 로고    scopus 로고
    • Yeast respond to hypotonic shock with a calcium pulse
    • Batiza, A.F., Schulz, T., and Masson, P.H. (1996) Yeast respond to hypotonic shock with a calcium pulse. J Biol Chem 271: 23357-23362.
    • (1996) J Biol Chem , vol.271 , pp. 23357-23362
    • Batiza, A.F.1    Schulz, T.2    Masson, P.H.3
  • 6
    • 0027397544 scopus 로고
    • Inositol triphosphate and calcium signalling
    • Berridge, M.J. (1993) Inositol triphosphate and calcium signalling. Nature 361: 315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0028960454 scopus 로고
    • 2+ mobilization pathways at the vacuolar membrane of Candida albicans
    • 2+ mobilization pathways at the vacuolar membrane of Candida albicans. J Biol Chem 270: 7272-7280.
    • (1995) J Biol Chem , vol.270 , pp. 7272-7280
    • Calvert, C.M.1    Sanders, D.2
  • 9
    • 0020078214 scopus 로고
    • Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase
    • Carlson, M., and Botstein, D. (1982) Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28: 145-154.
    • (1982) Cell , vol.28 , pp. 145-154
    • Carlson, M.1    Botstein, D.2
  • 10
    • 0013606754 scopus 로고
    • Biochemical studies on inositol. X. Partial purification of yeast inositol 1-phosphatase and its separation from glucose 6-phosphate cyclase
    • Chen, I.W., and Charalampous, F.C. (1966) Biochemical studies on inositol. X. Partial purification of yeast inositol 1-phosphatase and its separation from glucose 6-phosphate cyclase. Arch Biochem Biophys 117: 154-157.
    • (1966) Arch Biochem Biophys , vol.117 , pp. 154-157
    • Chen, I.W.1    Charalampous, F.C.2
  • 12
    • 0029561101 scopus 로고
    • A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway
    • Davenport, K.R., Sohaskey, M., Kamada, Y., Levin, D.E., and Gustin, M.C. (1995) A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway. J Biol Chem 270: 30157-30161.
    • (1995) J Biol Chem , vol.270 , pp. 30157-30161
    • Davenport, K.R.1    Sohaskey, M.2    Kamada, Y.3    Levin, D.E.4    Gustin, M.C.5
  • 13
    • 0030726285 scopus 로고    scopus 로고
    • Lithium toxicity is due to inhibition of RNA processing enzymes
    • Dichtl, B., Stevens, A., and Tollervey, D. (1997) Lithium toxicity is due to inhibition of RNA processing enzymes. EMBO J 16: 7184-7195.
    • (1997) EMBO J , vol.16 , pp. 7184-7195
    • Dichtl, B.1    Stevens, A.2    Tollervey, D.3
  • 15
    • 0023901622 scopus 로고
    • Rapid changes in polyphosphoinositide metabolism associated with the response of Dunaliella salina to hypoosmotic shock
    • Einspahr, K.J., Peeler, T.C., and Thompson, G.A. (1988) Rapid changes in polyphosphoinositide metabolism associated with the response of Dunaliella salina to hypoosmotic shock. J Biol Chem 263: 5775-5779.
    • (1988) J Biol Chem , vol.263 , pp. 5775-5779
    • Einspahr, K.J.1    Peeler, T.C.2    Thompson, G.A.3
  • 16
    • 0020793569 scopus 로고
    • A technique for radiolabelling DNA restriction endonuclease fragments to high specific activities
    • Feinberg, A.P., and Vogelstein, B. (1983) A technique for radiolabelling DNA restriction endonuclease fragments to high specific activities. Anal Biochem 132: 6-13.
    • (1983) Anal Biochem , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 17
    • 0027304451 scopus 로고
    • Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae
    • Flick, J.S., and Thorner, J. (1993) Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae. Mol Cell Biol 13: 5861-5876.
    • (1993) Mol Cell Biol , vol.13 , pp. 5861-5876
    • Flick, J.S.1    Thorner, J.2
  • 18
    • 0026731477 scopus 로고
    • A novel and conserved salt-induced protein is an important determinant of salt tolerance in yeast
    • Gaxiola, R., de Larrinoa, I.F., Villalba, J.M., and Serrano, R. (1992) A novel and conserved salt-induced protein is an important determinant of salt tolerance in yeast. EMBO J 11: 3157-3164.
    • (1992) EMBO J , vol.11 , pp. 3157-3164
    • Gaxiola, R.1    De Larrinoa, I.F.2    Villalba, J.M.3    Serrano, R.4
  • 19
    • 0024400630 scopus 로고
    • DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa
    • Geever, R.F., Huiet, L., Baum, J.A., Tyler, B.M., Patel, V.B., Rutledge, B.J., et al. (1989) DNA sequence, organization and regulation of the qa gene cluster of Neurospora crassa. J Mol Biol 207: 15-34.
    • (1989) J Mol Biol , vol.207 , pp. 15-34
    • Geever, R.F.1    Huiet, L.2    Baum, J.A.3    Tyler, B.M.4    Patel, V.B.5    Rutledge, B.J.6
  • 20
    • 0029582670 scopus 로고
    • Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a multigene family
    • Gillaspy, G.E., Keddie, J.S., Oda, K., and Gruissem, W. (1995) Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a multigene family. Plant Cell 7: 2175-2185.
    • (1995) Plant Cell , vol.7 , pp. 2175-2185
    • Gillaspy, G.E.1    Keddie, J.S.2    Oda, K.3    Gruissem, W.4
  • 21
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J Biol Chem 260: 3440-3450.
    • (1985) J Biol Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 24
    • 0019127799 scopus 로고
    • The effect of lithium ion and other agents on the activity of myo-inositol 1-phosphatase from bovine brain
    • Hallcher, L.M., and Sherman, W.R. (1980) The effect of lithium ion and other agents on the activity of myo-inositol 1-phosphatase from bovine brain. J Biol Chem 255: 10896-10901.
    • (1980) J Biol Chem , vol.255 , pp. 10896-10901
    • Hallcher, L.M.1    Sherman, W.R.2
  • 25
    • 0026006263 scopus 로고
    • A novel P-type ATPase from yeast involved in sodium transport
    • Haro, R., Garciadeblas, B., and Rodriguez-Navarro, A. (1991) A novel P-type ATPase from yeast involved in sodium transport. FEBS Lett 291: 189-191.
    • (1991) FEBS Lett , vol.291 , pp. 189-191
    • Haro, R.1    Garciadeblas, B.2    Rodriguez-Navarro, A.3
  • 26
    • 0024103054 scopus 로고
    • Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans
    • Hawkins, A.R., Lamb, H.K., Smith, M., Keyte, J.W., and Roberts, C.F. (1988) Molecular organisation of the quinic acid utilization (QUT) gene cluster in Aspergillus nidulans. Mol Gen Genet 214: 224-231.
    • (1988) Mol Gen Genet , vol.214 , pp. 224-231
    • Hawkins, A.R.1    Lamb, H.K.2    Smith, M.3    Keyte, J.W.4    Roberts, C.F.5
  • 27
    • 0025324408 scopus 로고
    • 2+] rise in maintaining viability of yeast cells late in the mating pheromone response pathway
    • 2+] rise in maintaining viability of yeast cells late in the mating pheromone response pathway. J Biol Chem 265: 13391-13399.
    • (1990) J Biol Chem , vol.265 , pp. 13391-13399
    • Iida, H.1    Yagawa, Y.2    Anraku, Y.3
  • 28
    • 0025483120 scopus 로고
    • Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers
    • Jones, J.S., and Prakash, L. (1990) Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers. Yeast 6: 363-366.
    • (1990) Yeast , vol.6 , pp. 363-366
    • Jones, J.S.1    Prakash, L.2
  • 29
    • 0000538964 scopus 로고    scopus 로고
    • Biogenesis and function of the yeast vacuole
    • Pringle, J.R., Broach, J.R., and Jones, E.W. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Jones, E.W., Webb, G.C., and Hiller, M.A. (1997) Biogenesis and function of the yeast vacuole. In The Molecular and Cellular Biology of the Yeast Saccharomyces Cell Cycle and Cell Biology. Pringle, J.R., Broach, J.R., and Jones, E.W. (eds). Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, pp. 363-470.
    • (1997) The Molecular and Cellular Biology of the Yeast Saccharomyces Cell Cycle and Cell Biology , pp. 363-470
    • Jones, E.W.1    Webb, G.C.2    Hiller, M.A.3
  • 30
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein, P.S., and Melton, D.A. (1996) A molecular mechanism for the effect of lithium on development. Proc Natl Acad Sci USA 93: 8455-8459.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 31
    • 0011330351 scopus 로고
    • Isolation of the yeast INO1 gene: Located on an autonomous plasmid, the gene is fully regulated
    • Klig, L.S., and Henry, S.A. (1984) Isolation of the yeast INO1 gene: located on an autonomous plasmid, the gene is fully regulated. Proc Natl Acad Sci USA 81: 3816-3820.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 3816-3820
    • Klig, L.S.1    Henry, S.A.2
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0001356288 scopus 로고
    • Myo-inositol: Its biosynthesis and metabolism
    • Loewus, F.A., and Loewus, M.W. (1983) myo-inositol: its biosynthesis and metabolism. Annu Rev Plant Physiol 34: 137-161.
    • (1983) Annu Rev Plant Physiol , vol.34 , pp. 137-161
    • Loewus, F.A.1    Loewus, M.W.2
  • 34
    • 0040936917 scopus 로고    scopus 로고
    • Multiple transduction pathways regulate the sodium-extrusion gene PMR2/ENA1 during salt stress in yeast
    • Marquez, J.A., and Serrano, R. (1996) Multiple transduction pathways regulate the sodium-extrusion gene PMR2/ENA1 during salt stress in yeast. FEBS Lett 382: 89-92.
    • (1996) FEBS Lett , vol.382 , pp. 89-92
    • Marquez, J.A.1    Serrano, R.2
  • 35
    • 0028800519 scopus 로고
    • Inositol monophosphatase activity from the Escherichia coli suhB gene product
    • Matsuhisa, A., Suzuki, N., Noda, T., and Shiba, K. (1995) Inositol monophosphatase activity from the Escherichia coli suhB gene product. J Bacteriol 177: 200-205.
    • (1995) J Bacteriol , vol.177 , pp. 200-205
    • Matsuhisa, A.1    Suzuki, N.2    Noda, T.3    Shiba, K.4
  • 36
    • 0028286249 scopus 로고
    • The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae
    • Mendoza, I., Rubio, F., Rodriguez-Navarro, A., and Pardo, J.M. (1994) The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae. J Biol Chem 269: 8792-8796.
    • (1994) J Biol Chem , vol.269 , pp. 8792-8796
    • Mendoza, I.1    Rubio, F.2    Rodriguez-Navarro, A.3    Pardo, J.M.4
  • 38
    • 0022504637 scopus 로고
    • Genealogy of principal strains of the yeast genetic stock center
    • Mortimer, R.K., and Johnston, J.R. (1986) Genealogy of principal strains of the yeast genetic stock center. Genetics 113: 35-43.
    • (1986) Genetics , vol.113 , pp. 35-43
    • Mortimer, R.K.1    Johnston, J.R.2
  • 39
    • 0028912113 scopus 로고
    • A salt-sensitive 3′ (2′), 5′-bisphosphate nucleotidase involved in sulfate activation
    • Murguia, J.R., Bellés, J.M., and Serrano, R. (1995) A salt-sensitive 3′ (2′), 5′-bisphosphate nucleotidase involved in sulfate activation. Science 287: 232-234.
    • (1995) Science , vol.267 , pp. 232-234
    • Murguia, J.R.1    Bellés, J.M.2    Serrano, R.3
  • 40
    • 0029824147 scopus 로고    scopus 로고
    • The yeast HAL2 nucleotidase is an in vivo target of salt toxicity
    • Murguia, J.R., Bellés, J.M., and Serrano, R. (1996) The yeast HAL2 nucleotidase is an in vivo target of salt toxicity. J Biol Chem 271: 29029-29033.
    • (1996) J Biol Chem , vol.271 , pp. 29029-29033
    • Murguia, J.R.1    Bellés, J.M.2    Serrano, R.3
  • 41
    • 0030764899 scopus 로고    scopus 로고
    • Regulation of inositol monophosphatase in Saccharomyces cerevisiae
    • Murray, M., and Greenberg, M.L. (1997) Regulation of inositol monophosphatase in Saccharomyces cerevisiae. Mol Microbiol 25: 541-546.
    • (1997) Mol Microbiol , vol.25 , pp. 541-546
    • Murray, M.1    Greenberg, M.L.2
  • 42
    • 0025912111 scopus 로고
    • Lithium and the phosphoinositide cycle: An example of uncompetitive inhibition and its pharmacological consequences
    • Nahorski, S.R., Ragan, C.I., and Challiss, R.A.J. (1991) Lithium and the phosphoinositide cycle: an example of uncompetitive inhibition and its pharmacological consequences. Trends Pharmacol Sci 12: 297-303.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 297-303
    • Nahorski, S.R.1    Ragan, C.I.2    Challiss, R.A.J.3
  • 43
    • 0027385382 scopus 로고
    • Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt conditions
    • Nakamura, T., Liu, Y., Hirata, D., Namba, H., Harada, S., Hirokawa, T., et al. (1993) Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt conditions. EMBO J 11: 4063-4071.
    • (1993) EMBO J , vol.11 , pp. 4063-4071
    • Nakamura, T.1    Liu, Y.2    Hirata, D.3    Namba, H.4    Harada, S.5    Hirokawa, T.6
  • 44
    • 0031782474 scopus 로고    scopus 로고
    • + homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation anti-porter NhaA
    • + homeostasis in Saccharomyces cerevisiae cells expressing the bacterial cation anti-porter NhaA. J Bacteriol 180: 3131-3136.
    • (1998) J Bacteriol , vol.180 , pp. 3131-3136
    • Ros, R.1    Montesinos, C.2    Rimon, A.3    Padan, E.4    Serrano, R.5
  • 45
    • 0026633081 scopus 로고
    • Cdc25-dependent induction of inositol 1,4,5-trisphosphate and diacyl-glycerol in Saccharomyces cerevisiae
    • Schomerus, C., and Küntzel, H. (1992) Cdc25-dependent induction of inositol 1,4,5-trisphosphate and diacyl-glycerol in Saccharomyces cerevisiae. FEBS Lett 307: 249-252.
    • (1992) FEBS Lett , vol.307 , pp. 249-252
    • Schomerus, C.1    Küntzel, H.2
  • 46
    • 0029922104 scopus 로고    scopus 로고
    • Salt tolerance in plants and microorganisms: Toxicity targets and defense responses
    • Serrano, R. (1996) Salt tolerance in plants and microorganisms: toxicity targets and defense responses. Int Rev Cytol 165: 1-52.
    • (1996) Int Rev Cytol , vol.165 , pp. 1-52
    • Serrano, R.1
  • 47
    • 0029447373 scopus 로고
    • Expression and localization of plant membrane proteins in Saccharomyces
    • Serrano, R., and Villalba, J.M. (1995) Expression and localization of plant membrane proteins in Saccharomyces. Methods Cell Biol 50: 481-496.
    • (1995) Methods Cell Biol , vol.50 , pp. 481-496
    • Serrano, R.1    Villalba, J.M.2
  • 48
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 and mimics Wingless signalling in intact cells
    • Stambolic, V., Ruel, L., and Woodgett, J.R. (1996) Lithium inhibits glycogen synthase kinase-3 and mimics Wingless signalling in intact cells. Curr Biol 6: 1664-1668.
    • (1996) Curr Biol , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.R.3
  • 49
    • 0029926061 scopus 로고    scopus 로고
    • Dictyostelium doscoideum contains three inositol monophosphatase activities with different substrate specificities and sensitivities to lithium
    • Van Dijken, P., Bergsma, J.C.T., Hiemstra, H.S., De Vries, B., and Van der Kaay, and Van Haastert, P.J.M. (1996) Dictyostelium doscoideum contains three inositol monophosphatase activities with different substrate specificities and sensitivities to lithium. Biochem J 314: 491-495.
    • (1996) Biochem J , vol.314 , pp. 491-495
    • Van Dijken, P.1    Bergsma, J.C.T.2    Hiemstra, H.S.3    De Vries, B.4    Van der Kaay5    Van Haastert, P.J.M.6
  • 50
    • 0030920886 scopus 로고    scopus 로고
    • DNA sequencing and analysis of 130 kb from yeast chromosome XV
    • Voss, H., Benes, V., Andrade, M.A., Valencia, A., Rechmann, S., Teodoru, C., et al. (1997) DNA sequencing and analysis of 130 kb from yeast chromosome XV. Yeast 13: 655-672.
    • (1997) Yeast , vol.13 , pp. 655-672
    • Voss, H.1    Benes, V.2    Andrade, M.A.3    Valencia, A.4    Rechmann, S.5    Teodoru, C.6
  • 51
    • 0001868090 scopus 로고
    • Measurement of fluxes across membranes
    • Lüttge, U., and Pitman, M.G. (eds). Berlin: Springer-Verlag
    • Walker, N.A., and Pitman, M.G. (1976) Measurement of fluxes across membranes. In Encyclopedia of Plant Physiology, New Series, Vol, 2, part A. Lüttge, U., and Pitman, M.G. (eds). Berlin: Springer-Verlag, pp. 93-117.
    • (1976) Encyclopedia of Plant Physiology, New Series , vol.2 , Issue.PART A , pp. 93-117
    • Walker, N.A.1    Pitman, M.G.2
  • 52
    • 0024324482 scopus 로고
    • A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase
    • Wallis, J.W., Chrebet, G., Brodsky, G., Rolfe, M., and Rothstein, R. (1989) A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase. Cell 58: 409-419.
    • (1989) Cell , vol.58 , pp. 409-419
    • Wallis, J.W.1    Chrebet, G.2    Brodsky, G.3    Rolfe, M.4    Rothstein, R.5
  • 53
    • 0028179125 scopus 로고
    • 2+ -inducible production of glutathione S-transferase-fusion proteins for single step purification from yeast
    • 2+ -inducible production of glutathione S-transferase-fusion proteins for single step purification from yeast. Yeast 10: 441-449.
    • (1994) Yeast , vol.10 , pp. 441-449
    • Ward, A.C.1    Castelli, L.A.2    Macreadie, I.G.3    Azad, A.A.4
  • 55
    • 0027403714 scopus 로고
    • The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth
    • Yoko-o, T., Matsui, Y., Yagisawa, H., Nojima, H., Uno, I., and Toh-e, A. (1993) The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth. Proc Natl Acad Sci USA 90: 1804-1808.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1804-1808
    • Yoko-O, T.1    Matsui, Y.2    Yagisawa, H.3    Nojima, H.4    Uno, I.5    Toh-E, A.6
  • 56
    • 0029036695 scopus 로고
    • + -inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure
    • + -inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc Natl Acad Sci USA 92: 5149-5153.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5149-5153
    • York, J.D.1    Ponder, J.W.2    Majerus, P.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.