메뉴 건너뛰기




Volumn 126, Issue 2, 2003, Pages 155-163

Protein farnesyl and N-myristoyl transferases: Piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics

Author keywords

N Myristoyl transferase; Protein farnesyl transferase; Protein prenylation

Indexed keywords

ANTIFUNGAL AGENT; ANTIMALARIAL AGENT; ANTITRYPANOSOMAL AGENT; ENZYME INHIBITOR; PROTEIN FARNESYLTRANSFERASE INHIBITOR; PROTEIN N MYRISTOYLTRANSFERASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0345073644     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(02)00282-7     Document Type: Review
Times cited : (133)

References (55)
  • 1
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • Casey P.J. Biochemistry of protein prenylation. J. Lipid Res. 33:1992;1731-1740.
    • (1992) J. Lipid Res. , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 2
    • 0025277259 scopus 로고
    • Prenyl protein in eukaryotic cells: A new type of membrane anchor
    • Glomset J.A., Gelb M.H., Farnsworth C.C. Prenyl protein in eukaryotic cells: a new type of membrane anchor. Trends Biochem. Sci. 15:1990;139-142.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 139-142
    • Glomset, J.A.1    Gelb, M.H.2    Farnsworth, C.C.3
  • 5
    • 0025375466 scopus 로고
    • Brain G protein γ-subunits contain an all-trans-geranylgeranyl cysteine methyl ester a their carboxyl termini
    • Yamane H.K.et al. Brain G protein γ-subunits contain an all-trans-geranylgeranyl cysteine methyl ester a their carboxyl termini. Proc. Natl. Acad. Sci. U.S.A. 87:1990;5868-5872.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5868-5872
    • Yamane, H.K.1
  • 6
    • 0025145610 scopus 로고
    • Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein
    • Sasaki T.et al. Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein. J. Biol. Chem. 265:1990;2333-2337.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2333-2337
    • Sasaki, T.1
  • 7
    • 0034619580 scopus 로고    scopus 로고
    • Binding of the delta subunit to rod phosphodiesterase catalytic subunits requires methylated, prenylated C-termini of the catalytic subunits
    • Cook T.A., Ghomashchi F., Gelb M.H., Florio S.K., Beavo J.A. Binding of the delta subunit to rod phosphodiesterase catalytic subunits requires methylated, prenylated C-termini of the catalytic subunits. Biochemistry. 39:2000;13516-13523.
    • (2000) Biochemistry , vol.39 , pp. 13516-13523
    • Cook, T.A.1    Ghomashchi, F.2    Gelb, M.H.3    Florio, S.K.4    Beavo, J.A.5
  • 8
    • 0035895891 scopus 로고    scopus 로고
    • The delta subunit of type 6 phosphodiesterase reduces light-induced cGMP hydrolysis in rod outer segments
    • Cook T.A., Ghomashchi F., Gelb M.H., Florio S.K., Beavo J.A. The delta subunit of type 6 phosphodiesterase reduces light-induced cGMP hydrolysis in rod outer segments. J. Biol. Chem. 276:2001;5248-5255.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5248-5255
    • Cook, T.A.1    Ghomashchi, F.2    Gelb, M.H.3    Florio, S.K.4    Beavo, J.A.5
  • 10
    • 0030581643 scopus 로고    scopus 로고
    • Characterisation of protein isoprenylation in procyclic form Trypanosoma brucei
    • Field H., Blench I., Croft S., Field M.C. Characterisation of protein isoprenylation in procyclic form Trypanosoma brucei. Mol. Biochem. Parasitol. 82:1996;67-80.
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 67-80
    • Field, H.1    Blench, I.2    Croft, S.3    Field, M.C.4
  • 11
    • 0032128169 scopus 로고    scopus 로고
    • The effects of protein farnesyltransferase inhibitors on trypanosomatids: Inhibition of protein farnesylation and cell growth
    • Yokoyama K.et al. The effects of protein farnesyltransferase inhibitors on trypanosomatids: inhibition of protein farnesylation and cell growth. Mol. Biochem. Parasitol. 94:1998;87-97.
    • (1998) Mol. Biochem. Parasitol. , vol.94 , pp. 87-97
    • Yokoyama, K.1
  • 13
    • 0029150669 scopus 로고
    • Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice
    • Kohl N.E.et al. Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice. Nat. Med. 1:1995;792-797.
    • (1995) Nat. Med. , vol.1 , pp. 792-797
    • Kohl, N.E.1
  • 14
    • 0029817090 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: A new class of cancer chemotherapeutics
    • Koblan K.S.et al. Farnesyltransferase inhibitors: a new class of cancer chemotherapeutics. Biochem. Soc. Trans. 24:1996;688-692.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 688-692
    • Koblan, K.S.1
  • 15
    • 0034754072 scopus 로고    scopus 로고
    • Current status of clinical trials of farnesyltransferase inhibitors
    • Karp J.E.et al. Current status of clinical trials of farnesyltransferase inhibitors. Curr. Opin. Oncol. 13:2001;470-476.
    • (2001) Curr. Opin. Oncol. , vol.13 , pp. 470-476
    • Karp, J.E.1
  • 16
    • 0034698159 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma brucei
    • Buckner F.S.et al. Cloning, heterologous expression, and distinct substrate specificity of protein farnesyltransferase from Trypanosoma brucei. J. Biol. Chem. 275:2000;21870-21876.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21870-21876
    • Buckner, F.S.1
  • 17
    • 0032564385 scopus 로고    scopus 로고
    • Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue
    • Strickland C.L.et al. Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. Biochemistry. 37:1998;16601-16611.
    • (1998) Biochemistry , vol.37 , pp. 16601-16611
    • Strickland, C.L.1
  • 18
    • 0030952552 scopus 로고    scopus 로고
    • Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CaaX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines
    • Lerner E.C.et al. Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CaaX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines. Oncogene. 15:1997;1283-1288.
    • (1997) Oncogene , vol.15 , pp. 1283-1288
    • Lerner, E.C.1
  • 19
    • 0033198291 scopus 로고    scopus 로고
    • GTPases in protozoan parasites: Tools for cell biology and chemotherapy
    • Field M.C., Ali B.R.S., Field H. GTPases in protozoan parasites: tools for cell biology and chemotherapy. Parasitol. Today. 15:1999;365-371.
    • (1999) Parasitol. Today , vol.15 , pp. 365-371
    • Field, M.C.1    Ali, B.R.S.2    Field, H.3
  • 20
    • 0035839566 scopus 로고    scopus 로고
    • TcRho1, a farnesylated Rho family homologue from Trypanosoma cruzi: Cloning, trans-splicing, and prenylation studies
    • Nepomuceno-Silva J.L.et al. TcRho1, a farnesylated Rho family homologue from Trypanosoma cruzi: cloning, trans-splicing, and prenylation studies. J. Biol. Chem. 276:2001;29711-29718.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29711-29718
    • Nepomuceno-Silva, J.L.1
  • 21
    • 0035953020 scopus 로고    scopus 로고
    • Peptidomimetic inhibitors of protein farnesyltransferase show potent antimalarial activity
    • Ohkanda J.et al. Peptidomimetic inhibitors of protein farnesyltransferase show potent antimalarial activity. Bioorg. Med. Chem. Lett. 11:2001;761-764.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 761-764
    • Ohkanda, J.1
  • 24
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • Farazi T.A., Waksman G., Gordon J.I. The biology and enzymology of protein N-myristoylation. J. Biol. Chem. 276:2001;39501-39504.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 25
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta. 1451:1999;1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 26
    • 0031571632 scopus 로고    scopus 로고
    • Electrostatic interaction of myristoylated proteins with membranes: Simple physics, complicated biology
    • Murray D., Ben-Tal N., Honig B., McLaughlin S. Electrostatic interaction of myristoylated proteins with membranes: simple physics, complicated biology. Structure. 5:1997;985-989.
    • (1997) Structure , vol.5 , pp. 985-989
    • Murray, D.1    Ben-Tal, N.2    Honig, B.3    McLaughlin, S.4
  • 27
    • 0029058605 scopus 로고
    • The myristoyl-electrostatic switch: A modulator of reversible protein-membrane interactions
    • McLaughlin S., Aderem A. The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions. Trends Biochem. Sci. 20:1995;272-276.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 272-276
    • McLaughlin, S.1    Aderem, A.2
  • 28
    • 0025834950 scopus 로고
    • Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl CoA:protein N-myristoyltransferase
    • Rudnick D.A.et al. Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl CoA:protein N-myristoyltransferase. J. Biol. Chem. 266:1991;9732-9739.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9732-9739
    • Rudnick, D.A.1
  • 30
    • 0031889926 scopus 로고    scopus 로고
    • Crystal structure of the antifungal target N-myristoyl transferase
    • Weston S.A.et al. Crystal structure of the antifungal target N-myristoyl transferase. Nat. Struct. Biol. 5:1998;213-221.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 213-221
    • Weston, S.A.1
  • 31
    • 0035862198 scopus 로고    scopus 로고
    • Drosophila embryos lacking N-myristoyltransferase have multiple developmental defects
    • Ntwasa M., Aapies S., Schiffmann D.A., Gay N.J. Drosophila embryos lacking N-myristoyltransferase have multiple developmental defects. Exp. Cell Res. 262:2001;134-144.
    • (2001) Exp. Cell Res. , vol.262 , pp. 134-144
    • Ntwasa, M.1    Aapies, S.2    Schiffmann, D.A.3    Gay, N.J.4
  • 32
    • 0024590280 scopus 로고
    • Disruption of the yeast N-myristoyl transferase gene causes recessive lethality
    • Duronio R.J., Towler D.A., Heuckeroth R.O., Gordon J.I. Disruption of the yeast N-myristoyl transferase gene causes recessive lethality. Science. 243:1989;796-800.
    • (1989) Science , vol.243 , pp. 796-800
    • Duronio, R.J.1    Towler, D.A.2    Heuckeroth, R.O.3    Gordon, J.I.4
  • 33
    • 0028000667 scopus 로고
    • Comparison of myristoyl CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans
    • Lodge J.K., Johnson R.L., Weinberg R.A., Gordon J.I. Comparison of myristoyl CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans. J. Biol. Chem. 269:1994;2996-3009.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2996-3009
    • Lodge, J.K.1    Johnson, R.L.2    Weinberg, R.A.3    Gordon, J.I.4
  • 34
    • 0029070249 scopus 로고
    • Genetic studies reveal that myristoyl CoA:protein N-myristoyltransferase is an essential enzyme in Candida albicans
    • Weinberg R.A.et al. Genetic studies reveal that myristoyl CoA:protein N-myristoyltransferase is an essential enzyme in Candida albicans. Mol. Microbiol. 16:1995;241-250.
    • (1995) Mol. Microbiol. , vol.16 , pp. 241-250
    • Weinberg, R.A.1
  • 35
    • 0034737580 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization, and biochemical characterization of myristoyl CoA:protein N-myristoyltransferase from Arabidopsis thaliana
    • Qi Q.et al. Molecular cloning, genomic organization, and biochemical characterization of myristoyl CoA:protein N-myristoyltransferase from Arabidopsis thaliana. J. Biol. Chem. 275:2000;9673-9683.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9673-9683
    • Qi, Q.1
  • 36
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyltransferase
    • Giang D.K., Cravatt B.F. A second mammalian N-myristoyltransferase. J. Biol. Chem. 273:1998;6595-6598.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 37
    • 0025245802 scopus 로고
    • Metabolic activation of 2-substituted derivatives of myristic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase
    • Paige L.A., Zheng G.Q., DeFrees S.A., Cassady J.M., Geahlen R.L. Metabolic activation of 2-substituted derivatives of myristic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase. Biochemistry. 29:1990;10566-10573.
    • (1990) Biochemistry , vol.29 , pp. 10566-10573
    • Paige, L.A.1    Zheng, G.Q.2    DeFrees, S.A.3    Cassady, J.M.4    Geahlen, R.L.5
  • 38
    • 15144355281 scopus 로고    scopus 로고
    • Design and synthesis of novel imidazole-substituted dipeptide amides as potent and selective inhibitors of Candida albicans myristoyl CoA:protein N-myristoyltransferase and identification of related tripeptide inhibitors with mechanism-based antifungal activity
    • Devadas B.et al. Design and synthesis of novel imidazole-substituted dipeptide amides as potent and selective inhibitors of Candida albicans myristoyl CoA:protein N-myristoyltransferase and identification of related tripeptide inhibitors with mechanism-based antifungal activity. J. Med. Chem. 40:1997;2609-2625.
    • (1997) J. Med. Chem. , vol.40 , pp. 2609-2625
    • Devadas, B.1
  • 39
    • 0032697710 scopus 로고    scopus 로고
    • Myristic acid analogs are inhibitors of Junin virus replication
    • Cordo S.M., Candurra N.A., Damonte E.B. Myristic acid analogs are inhibitors of Junin virus replication. Microbes Infect. 1:1999;609-614.
    • (1999) Microbes Infect. , vol.1 , pp. 609-614
    • Cordo, S.M.1    Candurra, N.A.2    Damonte, E.B.3
  • 40
    • 0031043522 scopus 로고    scopus 로고
    • N-Myristoylation of Arf proteins in Candida albicans: An in vivo assay for evaluating antifungal inhibitors of myristoyl CoA:protein N-myristoyltransferase
    • Lodge J.K.et al. N-Myristoylation of Arf proteins in Candida albicans: an in vivo assay for evaluating antifungal inhibitors of myristoyl CoA:protein N-myristoyltransferase. Microbiology. 143(Pt 2):1997;357-366.
    • (1997) Microbiology , vol.143 , Issue.PART 2 , pp. 357-366
    • Lodge, J.K.1
  • 41
    • 0032524623 scopus 로고    scopus 로고
    • Genetic and biochemical studies establish that the fungicidal effect of a fully depeptidized inhibitor of Cryptococcus neoformans myristoyl CoA:protein N-myristoyltransferase (Nmt) is Nmt-dependent
    • Lodge J.K.et al. Genetic and biochemical studies establish that the fungicidal effect of a fully depeptidized inhibitor of Cryptococcus neoformans myristoyl CoA:protein N-myristoyltransferase (Nmt) is Nmt-dependent. J. Biol. Chem. 273:1998;12482-12491.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12482-12491
    • Lodge, J.K.1
  • 42
    • 0035414280 scopus 로고    scopus 로고
    • Fatty acid synthesis in African trypanosomes: A solution to the myristate mystery
    • Paul K.S., Jiang D., Morita Y.S., Englund P.T. Fatty acid synthesis in African trypanosomes: a solution to the myristate mystery. Trends Parasitol. 17:2001;381-387.
    • (2001) Trends Parasitol. , vol.17 , pp. 381-387
    • Paul, K.S.1    Jiang, D.2    Morita, Y.S.3    Englund, P.T.4
  • 43
    • 0025870305 scopus 로고
    • An analog of myristic acid with selective toxicity for African trypanosomes
    • Doering T.L.et al. An analog of myristic acid with selective toxicity for African trypanosomes. Science. 252:1991;1851-1854.
    • (1991) Science , vol.252 , pp. 1851-1854
    • Doering, T.L.1
  • 44
    • 0027984029 scopus 로고
    • Toxicity of myristic acid analogs toward African trypanosomes
    • Doering T.L.et al. Toxicity of myristic acid analogs toward African trypanosomes. Proc. Natl. Acad. Sci. U.S.A. 91:1994;9735-9739.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 9735-9739
    • Doering, T.L.1
  • 45
    • 0028361293 scopus 로고
    • Expression of a hydrophilic surface protein in infective stages of Leishmania major
    • Flinn H.M., Rangarajan D., Smith D.F. Expression of a hydrophilic surface protein in infective stages of Leishmania major. Mol. Biochem. Parasitol. 65:1994;259-270.
    • (1994) Mol. Biochem. Parasitol. , vol.65 , pp. 259-270
    • Flinn, H.M.1    Rangarajan, D.2    Smith, D.F.3
  • 46
    • 0030932219 scopus 로고    scopus 로고
    • Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major
    • McKean P.G., Delahay R., Pimenta P.F., Smith D.F. Characterisation of a second protein encoded by the differentially regulated LmcDNA16 gene family of Leishmania major. Mol. Biochem. Parasitol. 85:1997;221-231.
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 221-231
    • McKean, P.G.1    Delahay, R.2    Pimenta, P.F.3    Smith, D.F.4
  • 47
    • 0034671822 scopus 로고    scopus 로고
    • Immunization with a recombinant stage-regulated surface protein from Leishmania donovani induces protection against visceral leishmaniasis
    • Stager S., Smith D.F., Kaye P.M. Immunization with a recombinant stage-regulated surface protein from Leishmania donovani induces protection against visceral leishmaniasis. J. Immunol. 165:2000;7064-7071.
    • (2000) J. Immunol. , vol.165 , pp. 7064-7071
    • Stager, S.1    Smith, D.F.2    Kaye, P.M.3
  • 49
    • 0033560770 scopus 로고    scopus 로고
    • Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism
    • Godsel L.M., Engman D.M. Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism. EMBO. J. 18:1999;2057-2065.
    • (1999) EMBO. J. , vol.18 , pp. 2057-2065
    • Godsel, L.M.1    Engman, D.M.2
  • 50
    • 0034010126 scopus 로고    scopus 로고
    • A novel phosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation
    • Furuya T., Kashuba C., Docampo R., Moreno S.N. A novel phosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation. J. Biol. Chem. 275:2000;6428-6438.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6428-6438
    • Furuya, T.1    Kashuba, C.2    Docampo, R.3    Moreno, S.N.4
  • 51
    • 0034895593 scopus 로고    scopus 로고
    • CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei
    • Hertz-Fowler C., Ersfeld K., Gull K. CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei. Mol. Biochem. Parasitol. 116:2001;25-34.
    • (2001) Mol. Biochem. Parasitol. , vol.116 , pp. 25-34
    • Hertz-Fowler, C.1    Ersfeld, K.2    Gull, K.3
  • 52
    • 0034212670 scopus 로고    scopus 로고
    • Characterization of N-myristoyltransferase from Plasmodium falciparum
    • Gunaratne R.S.et al. Characterization of N-myristoyltransferase from Plasmodium falciparum. Biochem. J. 348(Pt 2):2000;459-463.
    • (2000) Biochem. J. , vol.348 , Issue.PART 2 , pp. 459-463
    • Gunaratne, R.S.1
  • 53
    • 0037470198 scopus 로고    scopus 로고
    • Myristoyl CoA:protein N-myristoyltransferase: An essential enzyme and potential drug target in kinetoplastid parasites
    • in press
    • Price HP, et al. Myristoyl CoA:protein N-myristoyltransferase: an essential enzyme and potential drug target in kinetoplastid parasites. J Biol Chem, in press.
    • J Biol Chem
    • Price, H.P.1
  • 54
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A., Blundell T.L. Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 55
    • 0030657584 scopus 로고    scopus 로고
    • Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
    • Glover C.J., Hartman K.D., Felsted R.L. Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction. J. Biol. Chem. 272:1997;28680-28689.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28680-28689
    • Glover, C.J.1    Hartman, K.D.2    Felsted, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.