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Volumn 1697, Issue 1-2, 2004, Pages 181-196

Erratum: Plasmodium falciparum glycogen synthase kinase-3: Molecular model, expression, intracellular localisation and selective inhibitors (Biochimica et Biophysica Acta - Proteins and Proteomics (2004) 1697 (181-196) DOI: 10.1016/j.bbapap.2003.11.023);Plasmodium falciparum glycogen synthase kinase-3: Molecular model, expression, intracellular localisation and selective inhibitors

Author keywords

Casein kinase 1 2; CDK; CK1 2; Cyclin dependent kinase; Glycogen synthase kinase; Glycogen synthase kinase 3; GSK 3; Kinase inhibitor; LB; Luria Bertani medium; Malaria; MAPK; Microtubule associated protein kinase; PBS; PfGSK 3; Plasmodium; Protein kinase

Indexed keywords

ALSTERPAULLONE; AMINO ACID; AMINOPURVALANOL; AXIN; FLAVOPIRIDOL; GLYCOGEN SYNTHASE; GLYCOGEN SYNTHASE KINASE 3; GWENNPAULLONE; HYMENIALDISINE; INDIRUBIN; KENPAULLONE; LITHIUM; OLOMOUCINE; PAULLONE; PHOSPHOTRANSFERASE INHIBITOR; PROTOZOAL PROTEIN; PURVALANOL A; ROSCOVITINE; STAUROSPORINE; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 12144287677     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.04.005     Document Type: Erratum
Times cited : (114)

References (71)
  • 2
    • 0034175950 scopus 로고    scopus 로고
    • Chemotherapy for falciparum malaria: The armoury, the problems and the prospects
    • Winstanley P.A. Chemotherapy for falciparum malaria: the armoury, the problems and the prospects. Parasitol. Today. 16:2000;146-153.
    • (2000) Parasitol. Today , vol.16 , pp. 146-153
    • Winstanley, P.A.1
  • 4
    • 0036697233 scopus 로고    scopus 로고
    • Protein kinases as drug targets of parasitic protozoa
    • Doerig C., Meijer L., Mottram J. Protein kinases as drug targets of parasitic protozoa. Trends Parasitol. 18:2002;366-371.
    • (2002) Trends Parasitol. , vol.18 , pp. 366-371
    • Doerig, C.1    Meijer, L.2    Mottram, J.3
  • 5
    • 0037383322 scopus 로고    scopus 로고
    • GSK-3: Tricks of the trade for a multi-tasking kinase
    • Doble B.W., Woodgett J.R. GSK-3: tricks of the trade for a multi-tasking kinase. J. Cell Sci. 116:2003;1175-1186.
    • (2003) J. Cell Sci. , vol.116 , pp. 1175-1186
    • Doble, B.W.1    Woodgett, J.R.2
  • 7
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • Frame S., Cohen P. GSK3 takes centre stage more than 20 years after its discovery. Biochem. J. 359:2001;1-16.
    • (2001) Biochem. J. , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 8
    • 0036629249 scopus 로고    scopus 로고
    • Wnt signal transduction: Kinase cogs in a nano-machine
    • Ding Y., Dale T. Wnt signal transduction: kinase cogs in a nano-machine. Trends Biochem. Sci. 27:2002;327-329.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 327-329
    • Ding, Y.1    Dale, T.2
  • 9
    • 0035967897 scopus 로고    scopus 로고
    • Regulation of GSK-3: A cellular multiprocessor
    • Harwood A.J. Regulation of GSK-3: a cellular multiprocessor. Cell. 29:2001;821-824.
    • (2001) Cell , vol.29 , pp. 821-824
    • Harwood, A.J.1
  • 10
    • 0036090823 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3: An emerging therapeutic target
    • Eldar-Finkelman H. Glycogen synthase kinase 3: an emerging therapeutic target. Trends Mol. Med. 8:2002;126-132.
    • (2002) Trends Mol. Med. , vol.8 , pp. 126-132
    • Eldar-Finkelman, H.1
  • 12
    • 0035006828 scopus 로고    scopus 로고
    • Cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo
    • Ostvold A.C., Norum J.H., Mathiesen S., Wanvik B., Sefland I., Grundt K. Cloning of a mammalian nuclear phosphoprotein NUCKS, which serves as a substrate for Cdk1 in vivo. Eur. J. Biochem. 268:2001;2430-2440.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2430-2440
    • Ostvold, A.C.1    Norum, J.H.2    Mathiesen, S.3    Wanvik, B.4    Sefland, I.5    Grundt, K.6
  • 13
    • 0033614949 scopus 로고    scopus 로고
    • The paullones, a series of cyclin-dependent kinase inhibitors: Synthesis, evaluation of CDK1/cyclin B inhibition, in vitro antitumor activity
    • Schultz C., Link A., Leost M., Zaharevitz D.W., Gussio R., Sausville E.A., Meijer L., Kunick C. The paullones, a series of cyclin-dependent kinase inhibitors: synthesis, evaluation of CDK1/cyclin B inhibition, in vitro antitumor activity. J. Med. Chem. 42:1999;2909-2919.
    • (1999) J. Med. Chem. , vol.42 , pp. 2909-2919
    • Schultz, C.1    Link, A.2    Leost, M.3    Zaharevitz, D.W.4    Gussio, R.5    Sausville, E.A.6    Meijer, L.7    Kunick, C.8
  • 14
    • 0027962346 scopus 로고
    • Plasmodium falciparum: The Pf332 antigen is secreted from the parasite by a brefeldin a - Dependent pathway and is translocated to the erythrocyte membrane via the Maurer's clefts
    • Hinterberg K., Scherf A., Gysin J., Toyoshima T., Aikawa M., Mazie J.C., Pereira da Silva L., Mattei D. Plasmodium falciparum: the Pf332 antigen is secreted from the parasite by a brefeldin A - dependent pathway and is translocated to the erythrocyte membrane via the Maurer's clefts. Exp. Parasitol. 79:1994;279-291.
    • (1994) Exp. Parasitol. , vol.79 , pp. 279-291
    • Hinterberg, K.1    Scherf, A.2    Gysin, J.3    Toyoshima, T.4    Aikawa, M.5    Mazie, J.C.6    Pereira Da Silva, L.7    Mattei, D.8
  • 15
    • 0026536681 scopus 로고
    • The Pf332 gene of Plasmodium falciparum codes for a giant protein that is translocated from parasite to the membrane of infected erythrocytes
    • Mattei D., Scherf A. The Pf332 gene of Plasmodium falciparum codes for a giant protein that is translocated from parasite to the membrane of infected erythrocytes. Gene. 110:1992;71-79.
    • (1992) Gene , vol.110 , pp. 71-79
    • Mattei, D.1    Scherf, A.2
  • 16
    • 0035875098 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase kinase 3 β: Structural basis for phosphate-primed substrate specificity and autoinhibition
    • Dajani R., Fraser E., Roe S.M., Young N., Good V., Dale T.C., Pearl L.H. Crystal structure of glycogen synthase kinase 3 β: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell. 105:2001;721-732.
    • (2001) Cell , vol.105 , pp. 721-732
    • Dajani, R.1    Fraser, E.2    Roe, S.M.3    Young, N.4    Good, V.5    Dale, T.C.6    Pearl, L.H.7
  • 17
    • 0025272167 scopus 로고
    • Chromosome 9 from independent clones and isolates of Plasmodium falciparum undergoes subtelomeric deletions with similar breakpoints in vitro
    • Shirley M.V., Biggs B.A., Forsyth K.P., Brown H.J., Kemp D.J. Chromosome 9 from independent clones and isolates of Plasmodium falciparum undergoes subtelomeric deletions with similar breakpoints in vitro. Mol. Biochem. Parasitol. 40:1990;137-146.
    • (1990) Mol. Biochem. Parasitol. , vol.40 , pp. 137-146
    • Shirley, M.V.1    Biggs, B.A.2    Forsyth, K.P.3    Brown, H.J.4    Kemp, D.J.5
  • 18
    • 0018704491 scopus 로고
    • Synchronisation of Plasmodium falciparum erythrocytic stages in culture
    • Lambros C., Vanderberg J.P. Synchronisation of Plasmodium falciparum erythrocytic stages in culture. J. Parasitol. 65:1979;418-420.
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.P.2
  • 19
    • 0026580539 scopus 로고
    • Baculovirus-mediated expression, characterisation of rat glycogen synthase kinase-3 beta, the mammalian homologues of the Drosophila melanogaster zeste-white 3sgg homeotic gene product
    • Hughes K., Pulverer B.J., Theocharous P., Woodgett J.R. Baculovirus-mediated expression, characterisation of rat glycogen synthase kinase-3 beta, the mammalian homologues of the Drosophila melanogaster zeste-white 3sgg homeotic gene product. Eur. J. Biochem. 203:1992;305-311.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 305-311
    • Hughes, K.1    Pulverer, B.J.2    Theocharous, P.3    Woodgett, J.R.4
  • 21
    • 0017311840 scopus 로고
    • Human malaria parasite in continuous culture
    • Trager W.T., Jensen J.B. Human malaria parasite in continuous culture. Science. 193:1976;673-675.
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.T.1    Jensen, J.B.2
  • 22
    • 0018249537 scopus 로고
    • Separation of viable schizont-infected cells of Plasmodium falciparum from human blood
    • Pasvol G., Wilson R.J.M., Smalley M.E., Brown J. Separation of viable schizont-infected cells of Plasmodium falciparum from human blood. Ann. Trop. Med. Parasitol. 72:1978;87-88.
    • (1978) Ann. Trop. Med. Parasitol. , vol.72 , pp. 87-88
    • Pasvol, G.1    Wilson, R.J.M.2    Smalley, M.E.3    Brown, J.4
  • 24
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • Frame S., Cohen P., Biondi R.M. A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation. Mol. Cell. 7:2001;1321-1327.
    • (2001) Mol. Cell , vol.7 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 26
    • 0034718421 scopus 로고    scopus 로고
    • Regulation, localization of Tyrosine216 phosphorylation of glycogen synthase kinase-3β in cellular and animal models of neuronal degeneration
    • Bhat R.V., Shanley J., Correll M.P., Fieles W.E., Keith R.A., Scott C.W., Lee C.M. Regulation, localization of Tyrosine216 phosphorylation of glycogen synthase kinase-3β in cellular and animal models of neuronal degeneration. Proc. Natl. Acad. Sci. U. S. A. 97:2000;11074-11079.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11074-11079
    • Bhat, R.V.1    Shanley, J.2    Correll, M.P.3    Fieles, W.E.4    Keith, R.A.5    Scott, C.W.6    Lee, C.M.7
  • 27
    • 0032734021 scopus 로고    scopus 로고
    • The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification
    • Kim L., Liu J., Kimmel A.R. The novel tyrosine kinase ZAK1 activates GSK3 to direct cell fate specification. Cell. 99:1999;399-408.
    • (1999) Cell , vol.99 , pp. 399-408
    • Kim, L.1    Liu, J.2    Kimmel, A.R.3
  • 28
    • 0032955426 scopus 로고    scopus 로고
    • Insulin transiently increases tau phosphorylation: Involvement of glycogen synthase kinase-3beta, Fyn tyrosine kinase
    • Lesort M., Jope R.S., Johnson G.V. Insulin transiently increases tau phosphorylation: involvement of glycogen synthase kinase-3beta, Fyn tyrosine kinase. J. Neurochem. 72:1999;576-584.
    • (1999) J. Neurochem. , vol.72 , pp. 576-584
    • Lesort, M.1    Jope, R.S.2    Johnson, G.V.3
  • 29
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature. 378:1995;785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 31
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AKTion blocks apoptosis
    • Franke T.F., Kaplan D.R., Cantley L.C. PI3K: downstream AKTion blocks apoptosis. Cell. 88:1997;435-437.
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 34
    • 0037067733 scopus 로고    scopus 로고
    • Intracellular targets of paullones: Identification by affinity chromatography using immobilized inhibitor
    • Knockaert M., Viking K., Schmitt S., Leost M., Mottram J., Kunick C., Meijer L. Intracellular targets of paullones: identification by affinity chromatography using immobilized inhibitor. J. Biol. Chem. 277:2002;25493-25501.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25493-25501
    • Knockaert, M.1    Viking, K.2    Schmitt, S.3    Leost, M.4    Mottram, J.5    Kunick, C.6    Meijer, L.7
  • 35
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 activity, mimics Wingless signaling in intact cells
    • Stambolic V., Ruel L., Woodgett J.R. Lithium inhibits glycogen synthase kinase-3 activity, mimics Wingless signaling in intact cells. Curr. Biol. 6:1996;1664-1668.
    • (1996) Curr. Biol. , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.R.3
  • 36
    • 0030868557 scopus 로고    scopus 로고
    • Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3
    • Hong M., Chen D.C., Klein P.S., Lee V.M. Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3. J. Biol. Chem. 272:1997;25326-25332.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25326-25332
    • Hong, M.1    Chen, D.C.2    Klein, P.S.3    Lee, V.M.4
  • 37
    • 0034805180 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 by competition for magnesium
    • Ryves W.J., Harwood A.J. Lithium inhibits glycogen synthase kinase-3 by competition for magnesium. Biochem. Biophys. Res. Commun. 280:2001;720-725.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 720-725
    • Ryves, W.J.1    Harwood, A.J.2
  • 42
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase- 3β, CDK5/p25, two kinases involved in abnormal tau phosphorylation in Alzheimer's disease- a property common to most CDK inhibitors?
    • Leclerc S., Garnier M., Hoessel R., Marko D., Bibb J.A., Snyder G.L., Greengard P., Biernat J., Mandelkow E.-M., Eisenbrand G., Meijer L. Indirubins inhibit glycogen synthase kinase- 3β, CDK5/p25, two kinases involved in abnormal tau phosphorylation in Alzheimer's disease- A property common to most CDK inhibitors? J. Biol. Chem. 276:2001;251-260.
    • (2001) J. Biol. Chem. , vol.276 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3    Marko, D.4    Bibb, J.A.5    Snyder, G.L.6    Greengard, P.7    Biernat, J.8    Mandelkow, E.-M.9    Eisenbrand, G.10    Meijer, L.11
  • 46
    • 0023475545 scopus 로고
    • Plasmodium berghei, P chabaudi, and P falciparum: Similarities in phosphoproteins and protein kinase activities and their stage specific expression
    • Wiser M.F., Plitt B. Plasmodium berghei, P chabaudi, and P falciparum: similarities in phosphoproteins and protein kinase activities and their stage specific expression. Exp. Parasitol. 64:1987;328-335.
    • (1987) Exp. Parasitol. , vol.64 , pp. 328-335
    • Wiser, M.F.1    Plitt, B.2
  • 47
    • 0025300514 scopus 로고
    • Protein phosphorylation during the asexual life cycle of the human malarial Plasmodium falciparum
    • Jones G.L., McLemore Edmundson H. Protein phosphorylation during the asexual life cycle of the human malarial Plasmodium falciparum. Biochim. Biophys. Acta. 1053:1990;118-124.
    • (1990) Biochim. Biophys. Acta , vol.1053 , pp. 118-124
    • Jones, G.L.1    McLemore Edmundson, H.2
  • 48
    • 0024521681 scopus 로고
    • Phosphorylation of erythrocyte membrane and cytoskeleton proteins in cells infected with Plasmodium falciparum
    • Murray M.C., Perkins M.E. Phosphorylation of erythrocyte membrane and cytoskeleton proteins in cells infected with Plasmodium falciparum. Mol. Biochem. Parasitol. 34:1989;229-236.
    • (1989) Mol. Biochem. Parasitol. , vol.34 , pp. 229-236
    • Murray, M.C.1    Perkins, M.E.2
  • 49
    • 0026739575 scopus 로고
    • Regulation and post-translational modification of erythrocyte membrane, membrane-skeletal proteins
    • Cohen C.M., Gascard P. Regulation and post-translational modification of erythrocyte membrane, membrane-skeletal proteins. Semin. Hematol. 29:1992;244-292.
    • (1992) Semin. Hematol. , vol.29 , pp. 244-292
    • Cohen, C.M.1    Gascard, P.2
  • 50
    • 0028307510 scopus 로고
    • Phosphorylation of protein 41 in Plasmodium falciparum-infected human red blood cells
    • Chisti A.H., Maalouf G.J., Marfatia S., Palek J., Wang W., Fisher D., Liu S.C. Phosphorylation of protein 41 in Plasmodium falciparum-infected human red blood cells. Blood. 83:1994;3339-3345.
    • (1994) Blood , vol.83 , pp. 3339-3345
    • Chisti, A.H.1    Maalouf, G.J.2    Marfatia, S.3    Palek, J.4    Wang, W.5    Fisher, D.6    Liu, S.C.7
  • 51
    • 0030839074 scopus 로고    scopus 로고
    • Signal transduction in malaria parasites
    • Doerig C.D. Signal transduction in malaria parasites. Parasitol. Today. 13:1997;307-312.
    • (1997) Parasitol. Today , vol.13 , pp. 307-312
    • Doerig, C.D.1
  • 52
  • 53
    • 0032054251 scopus 로고    scopus 로고
    • Characterisation of PfSec61, a Plasmodium falciparum homologue of the translocation machinery at the endoplasmic reticulum membrane of eukaryotic cells
    • Couffin S., Hernandez-Rivas R., Blisnick T., Mattei D. Characterisation of PfSec61, a Plasmodium falciparum homologue of the translocation machinery at the endoplasmic reticulum membrane of eukaryotic cells. Mol. Biochem. Parasitol. 92:1998;89-98.
    • (1998) Mol. Biochem. Parasitol. , vol.92 , pp. 89-98
    • Couffin, S.1    Hernandez-Rivas, R.2    Blisnick, T.3    Mattei, D.4
  • 54
    • 0025204355 scopus 로고
    • Ultrastructure of malaria-infected erythrocytes
    • Atkinson C.T., Aikawa M. Ultrastructure of malaria-infected erythrocytes. Blood Cells. 16:1990;351-368.
    • (1990) Blood Cells , vol.16 , pp. 351-368
    • Atkinson, C.T.1    Aikawa, M.2
  • 56
    • 0024445506 scopus 로고
    • A new blood stage antigen of Plasmodium falciparum transported to the erythrocyte surface
    • Knapp B., Hundt E., Küpper H.A. A new blood stage antigen of Plasmodium falciparum transported to the erythrocyte surface. Mol. Biochem. Parasitol. 37:1989;47-56.
    • (1989) Mol. Biochem. Parasitol. , vol.37 , pp. 47-56
    • Knapp, B.1    Hundt, E.2    Küpper, H.A.3
  • 57
    • 0023441057 scopus 로고
    • Structure and expression of the knob-associated histidine-rich protein of Plasmodium falciparum
    • Ellis J., Irving D.O., Wellems T.E., Howard R.J., Cross G.A. Structure and expression of the knob-associated histidine-rich protein of Plasmodium falciparum. Mol. Biochem. Parasitol. 26:1987;203-214.
    • (1987) Mol. Biochem. Parasitol. , vol.26 , pp. 203-214
    • Ellis, J.1    Irving, D.O.2    Wellems, T.E.3    Howard, R.J.4    Cross, G.A.5
  • 58
    • 0035886970 scopus 로고    scopus 로고
    • Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes
    • Wickham M.E., Rug M., Ralph S.A., Klonis N., McFadden G.I., Tilley L., Cowman A.F. Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes. EMBO J. 20:2001;5636-5649.
    • (2001) EMBO J. , vol.20 , pp. 5636-5649
    • Wickham, M.E.1    Rug, M.2    Ralph, S.A.3    Klonis, N.4    McFadden, G.I.5    Tilley, L.6    Cowman, A.F.7
  • 59
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • Kirk K. Membrane transport in the malaria-infected erythrocyte. Physiol. Rev. 81:2001;495-537.
    • (2001) Physiol. Rev. , vol.81 , pp. 495-537
    • Kirk, K.1
  • 60
    • 0023574139 scopus 로고
    • Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes
    • Atkinson C.T., Aikawa M., Perry G., Fujino T., Bennett V., Davidson E.A., Howard R.J. Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes. Eur. J. Cell Biol. 45:1987;192-199.
    • (1987) Eur. J. Cell Biol. , vol.45 , pp. 192-199
    • Atkinson, C.T.1    Aikawa, M.2    Perry, G.3    Fujino, T.4    Bennett, V.5    Davidson, E.A.6    Howard, R.J.7
  • 61
    • 0034739003 scopus 로고    scopus 로고
    • A voltage-dependent channel involved in nutrient uptake by red blood cells infected with the malaria parasite
    • Desai S.A., Bezrukov S.M., Zimmerberg J. A voltage-dependent channel involved in nutrient uptake by red blood cells infected with the malaria parasite. Nature. 406:2000;1001-1005.
    • (2000) Nature , vol.406 , pp. 1001-1005
    • Desai, S.A.1    Bezrukov, S.M.2    Zimmerberg, J.3
  • 62
    • 0035968076 scopus 로고    scopus 로고
    • Malaria parasite Plasmodium gallinaceum up-regulates host red blood cell channels
    • Thomas S.L., Egee S., Lapaix F., Kaestner L., Staines H.M., Ellory J.C. Malaria parasite Plasmodium gallinaceum up-regulates host red blood cell channels. FEBS Lett. 500:2001;45-51.
    • (2001) FEBS Lett. , vol.500 , pp. 45-51
    • Thomas, S.L.1    Egee, S.2    Lapaix, F.3    Kaestner, L.4    Staines, H.M.5    Ellory, J.C.6
  • 64
    • 0035875069 scopus 로고    scopus 로고
    • A role for the segment polarity gene shaggy/GSK-3 in the Drosophila circadian clock
    • Martinek S., Inonog S., Manoukian A.S., Young M.W. A role for the segment polarity gene shaggy/GSK-3 in the Drosophila circadian clock. Cell. 105:2001;769-779.
    • (2001) Cell , vol.105 , pp. 769-779
    • Martinek, S.1    Inonog, S.2    Manoukian, A.S.3    Young, M.W.4
  • 65
    • 0035458732 scopus 로고    scopus 로고
    • Time zones: A comparative genetics of circadian clocks
    • Young M.W., Kay S.A. Time zones: a comparative genetics of circadian clocks. Nat. Rev., Genet. 2:2001;702-715.
    • (2001) Nat. Rev., Genet. , vol.2 , pp. 702-715
    • Young, M.W.1    Kay, S.A.2
  • 66
    • 0030705190 scopus 로고    scopus 로고
    • Identification, cloning, mutational analysis of the casein kinase 1 cDNA of the malaria parasite, Plasmodium falciparum
    • Barik S., Taylor R.E., Chakrabarti D. Identification, cloning, mutational analysis of the casein kinase 1 cDNA of the malaria parasite, Plasmodium falciparum. J. Biol. Chem. 272:1997;26132-26138.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26132-26138
    • Barik, S.1    Taylor, R.E.2    Chakrabarti, D.3
  • 69
    • 0026244229 scopus 로고
    • MOLSCRIPT-a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. 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
  • 70
    • 0028057108 scopus 로고
    • Raster3D version 20-a program for photorealistic molecular graphics
    • Merrit E.A., Murphy M.E.P. Raster3D version 20-a program for photorealistic molecular graphics. Acta Crystallogr. 50:1994;869-873.
    • (1994) Acta Crystallogr. , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 71
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, Struct., Funct. Genet. 11:1991;281-296.
    • (1991) Proteins, Struct., Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.