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Volumn 182, Issue 3, 2000, Pages 704-713

Geranylgeranyltransferase I of Candida albicans: Null mutants or enzyme inhibitors produce unexpected phenotypes

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; GERANYLTRANSFERASE;

EID: 0033964481     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.3.704-713.2000     Document Type: Article
Times cited : (41)

References (54)
  • 1
    • 0029039625 scopus 로고
    • Evaluation of water-soluble pneumocandins L-733,560, L-705,589, and L-731,373 in mouse models of disseminated aspergillosis, candidiasis, and cryptococcosis
    • Abruzzo, G. K., A. M. Flattery, C. J. Gill, L. Kong, J. G. Smith, D. Krupa, V. B. Pikounis, H. Krupp, and K. Bartizal. 1995. Evaluation of water-soluble pneumocandins L-733,560, L-705,589, and L-731,373 in mouse models of disseminated aspergillosis, candidiasis, and cryptococcosis. Antimicrob. Agents Chemother. 39:1077-1081.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1077-1081
    • Abruzzo, G.K.1    Flattery, A.M.2    Gill, C.J.3    Kong, L.4    Smith, J.G.5    Krupa, D.6    Pikounis, V.B.7    Krupp, H.8    Bartizal, K.9
  • 2
    • 0025294640 scopus 로고
    • CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae
    • Adams, E. M., D. I. Johnson, R. M. Longnecker, B. F. Sloat, and J. R. Pringle. 1990. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J. Cell Biol. 111:131-142.
    • (1990) J. Cell Biol. , vol.111 , pp. 131-142
    • Adams, E.M.1    Johnson, D.I.2    Longnecker, R.M.3    Sloat, B.F.4    Pringle, J.R.5
  • 4
    • 0031696971 scopus 로고    scopus 로고
    • Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe
    • Arellano, M., P. M. Coll, W. Yang, A. Duran, F. Tamanoi, and P. Perez. 1998. Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe. Mol. Microbiol. 29:1357-1367.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1357-1367
    • Arellano, M.1    Coll, P.M.2    Yang, W.3    Duran, A.4    Tamanoi, F.5    Perez, P.6
  • 5
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D., F. LaCroute, and G. R. Fink. 1984. A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    Lacroute, F.2    Fink, G.R.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye hinding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye hinding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0028199774 scopus 로고
    • Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase
    • Capita, B. E., L. A. Hettich, and M. S. Marshall. 1994. Substrate characterization of the Saccharomyces cerevisiae protein farnesyltransferase and type-I protein geranylgeranyltransferase. Biochim. Biophys. Acta 1205:39-48.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 39-48
    • Capita, B.E.1    Hettich, L.A.2    Marshall, M.S.3
  • 8
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke, S. 1992. Protein isoprenylation and methylation at carboxyl-terminal cysteine residues, Annu. Rev. Biochem. 61:355-386.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 11
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble, R. 1992. A simple and efficient procedure for transformation of yeasts. Biotechniques 13:18-20.
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 12
    • 0028135348 scopus 로고
    • Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A
    • Farnsworth, C. C., M. C. Seabra, L. H. Ericsson, M. H. Gelb, and J. A. Glomset. 1994. Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc. Natl. Acad. Sci. USA 91:11963-11967.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11963-11967
    • Farnsworth, C.C.1    Seabra, M.C.2    Ericsson, L.H.3    Gelb, M.H.4    Glomset, J.A.5
  • 13
    • 0025829655 scopus 로고
    • Geranylgeranylprotein transferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product, but not the DPRI gene product
    • Finegold, A. A., D. I. Johnson, C. C. Farnsworth, M. H. Gelb, S. R. Judd, J. A. Glomset, and F. Tamanoi. 1991. Geranylgeranylprotein transferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product, but not the DPRI gene product. Proc. Natl. Acad. Sci. USA 88:4448-4452.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4448-4452
    • Finegold, A.A.1    Johnson, D.I.2    Farnsworth, C.C.3    Gelb, M.H.4    Judd, S.R.5    Glomset, J.A.6    Tamanoi, F.7
  • 14
    • 0027192868 scopus 로고
    • Isogenic strain construction and gene mapping in Candida albicans
    • Fonzi, W. A., and M. Y. Irwin. 1993. Isogenic strain construction and gene mapping in Candida albicans. Gene 134:717-728.
    • (1993) Gene , vol.134 , pp. 717-728
    • Fonzi, W.A.1    Irwin, M.Y.2
  • 15
    • 0026345033 scopus 로고
    • RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins
    • He, B., P. Chen, S. Chen, K. L. Vancura, S. Michaelis, and S. Powers. 1991. RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins. Proc. Natl. Acad. Sci. USA 88:11373-11377.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11373-11377
    • He, B.1    Chen, P.2    Chen, S.3    Vancura, K.L.4    Michaelis, S.5    Powers, S.6
  • 16
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmid for transformation of Escherichia coti
    • Hoffman, C. S., and F. Winston. 1987. A ten-minute DNA preparation from yeast efficiently releases autonomous plasmid for transformation of Escherichia coti. Gene 57:267-272.
    • (1987) Gene , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 17
    • 0030927327 scopus 로고    scopus 로고
    • Bnilp and Bnilp: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura, H., K. Tanaka, T. Hihara, M. Umikawa, T. Kamei, K. Takahashi, T. Sasaki, and Y. Takai. 1997. Bnilp and Bnilp: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16:2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 19
    • 0023081618 scopus 로고
    • Directed mutagenesis in Candida albicans: One-step gene disruption to isolate ura3 mutants
    • Kelly, R., S. M. Miller, M. B. Kurtz, and D. R. Kirsch. 1987. Directed mutagenesis in Candida albicans: one-step gene disruption to isolate ura3 mutants. Mol. Cell. Biol. 7:199-208.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 199-208
    • Kelly, R.1    Miller, S.M.2    Kurtz, M.B.3    Kirsch, D.R.4
  • 22
    • 0030785108 scopus 로고    scopus 로고
    • Cloning of the RHO1 gene from Candida albicans and its regulation of β-1,3-glucan synthesis
    • Kondoh, O., Y. Tachibana, Y. Ohya, M. Arisawa, and T. Watanabe. 1997. Cloning of the RHO1 gene from Candida albicans and its regulation of β-1,3-glucan synthesis. J. Bacteriol. 179:7734-7741.
    • (1997) J. Bacteriol. , vol.179 , pp. 7734-7741
    • Kondoh, O.1    Tachibana, Y.2    Ohya, Y.3    Arisawa, M.4    Watanabe, T.5
  • 23
    • 0030916369 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB
    • Lebowitz, P. F., P. J. Casey, G. C. Prendergast, and J. A. Thissen. 1997. Farnesyltransferase inhibitors alter the prenylation and growth-stimulating function of RhoB. J. Biol. Chem. 272:15591-15594.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15591-15594
    • Lebowitz, P.F.1    Casey, P.J.2    Prendergast, G.C.3    Thissen, J.A.4
  • 24
    • 0030910236 scopus 로고    scopus 로고
    • Prenylation of RhoB is required for its cell transforming function but not its ability to activate serum response element-dependent transcription
    • Lebowitz, P. F., W. Du, and G. C. Prendergast. 1997. Prenylation of RhoB is required for its cell transforming function but not its ability to activate serum response element-dependent transcription. J. Biol. Chem. 272:16093-16095.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16093-16095
    • Lebowitz, P.F.1    Du, W.2    Prendergast, G.C.3
  • 25
    • 0026688456 scopus 로고
    • CDC43 and RAM2 encode the polypeptide subunits of a yeast type I protein geranylgeranyltransferase
    • Mayer, M. L., B. E. Caplin, and M. S. Marshall. 1992. CDC43 and RAM2 encode the polypeptide subunits of a yeast type I protein geranylgeranyltransferase. J. Biol. Chem. 267:20589-20593.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20589-20593
    • Mayer, M.L.1    Caplin, B.E.2    Marshall, M.S.3
  • 26
    • 15844412765 scopus 로고    scopus 로고
    • In vitro activity of 1,3-β-D glucan synthase requires the GTP-binding protein Rho1
    • Mazur, P., and W. Baginsky. 1996. In vitro activity of 1,3-β-D glucan synthase requires the GTP-binding protein Rho1. J. Biol. Chem. 271:14604-14609.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14604-14609
    • Mazur, P.1    Baginsky, W.2
  • 27
    • 0032899654 scopus 로고    scopus 로고
    • Purification of geranylgeranyltransferase I from Candida albicans and cloning of the CaRAM2 and CaCDC43 genes encoding its subunits
    • Mazur, P., E. Register, C. A. Bonflglio, X. Yuan, M. B. Kurtz, J. M. Williamson, and R. Kelly. 1999. Purification of geranylgeranyltransferase I from Candida albicans and cloning of the CaRAM2 and CaCDC43 genes encoding its subunits. Microbiology 145:1123-1135.
    • (1999) Microbiology , vol.145 , pp. 1123-1135
    • Mazur, P.1    Register, E.2    Bonflglio, C.A.3    Yuan, X.4    Kurtz, M.B.5    Williamson, J.M.6    Kelly, R.7
  • 28
    • 79961234502 scopus 로고    scopus 로고
    • Molecular cloning of a Rho family, CDC42Ca gene from Candida albicans and its mRNA expression changes during morphogenesis
    • Mirbod, F., S, Nakashima, Y. Kitajima, R. D. Cannon, and Y. Nozawa. 1997. Molecular cloning of a Rho family, CDC42Ca gene from Candida albicans and its mRNA expression changes during morphogenesis. J. Med. Vet. Mycol. 35:173-179.
    • (1997) J. Med. Vet. Mycol. , vol.35 , pp. 173-179
    • Mirbod, F.1    Kitajima, Y.2    Cannon, R.D.3    Nozawa, Y.4
  • 30
    • 0031937062 scopus 로고    scopus 로고
    • Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase homologues, from the pathogenic fungus Candida albicans
    • Nagahashi, S., T. Mio, N. Ono, T. Yamada-Okabe, M. Arisawa, H. Bussey, and H. Yamada-Okabe. 1998. Isolation of CaSLN1 and CaNIK1, the genes for osmosensing histidine kinase homologues, from the pathogenic fungus Candida albicans. Microbiology 144:425-432.
    • (1998) Microbiology , vol.144 , pp. 425-432
    • Nagahashi, S.1    Mio, T.2    Ono, N.3    Yamada-Okabe, T.4    Arisawa, M.5    Bussey, H.6    Yamada-Okabe, H.7
  • 32
    • 0028829555 scopus 로고
    • A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Sacchammyces cerevisiae
    • Nonaka, H., K. Tanaka, H. Hirano, T. Fujiwara, H. Kohno, M. Umikawa, A. Mino, and Y. Takai. 1995. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Sacchammyces cerevisiae. EMBO J. 14:5931-5938.
    • (1995) EMBO J. , vol.14 , pp. 5931-5938
    • Nonaka, H.1    Tanaka, K.2    Hirano, H.3    Fujiwara, T.4    Kohno, H.5    Umikawa, M.6    Mino, A.7    Takai, Y.8
  • 34
    • 0025823167 scopus 로고
    • Yeast CAL1 is a structural and functional homologue to the DPRI (RAM) gene involved in ras processing
    • Ohya, Y., M. Goebl, L. E. Goodman, S. Peterson-Bjorn, J. D. Firesen, F. Tamanoi, and Y. Anraku. 1991. Yeast CAL1 is a structural and functional homologue to the DPRI (RAM) gene involved in ras processing. J. Biol. Chem. 266:12356-12360.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12356-12360
    • Ohya, Y.1    Goebl, M.2    Goodman, L.E.3    Peterson-Bjorn, S.4    Firesen, J.D.5    Tamanoi, F.6    Anraku, Y.7
  • 35
    • 0027371012 scopus 로고
    • Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases. Rho1p and Cdc42p
    • Ohya, Y., H. Qadota, Y. Anraku, J. R. Pringle, and D. Botstein. 1993. Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases. Rho1p and Cdc42p. Mol. Biol. Cell 4:1017-1025.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1017-1025
    • Ohya, Y.1    Qadota, H.2    Anraku, Y.3    Pringle, J.R.4    Botstein, D.5
  • 36
    • 0028232081 scopus 로고
    • Protein prenylation in eukaryotic microorganisms: Genetics, biology and biochemistry
    • Omer, C., and J. Gibbs. 1994. Protein prenylation in eukaryotic microorganisms: genetics, biology and biochemistry. Mol. Microbiol. 11:219-225.
    • (1994) Mol. Microbiol. , vol.11 , pp. 219-225
    • Omer, C.1    Gibbs, J.2
  • 40
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • Rowell, C. A., J. J. Kowalczyk, M. D. Lewis, and A. M. Garcia. 1997. Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo. J. Biol. Chem. 272:14093-14097.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 42
    • 0027076554 scopus 로고
    • Protein prenylation: Genes, enzymes, targets, and functions
    • Schafer, W. R., and J. Rine. 1992. Protein prenylation: genes, enzymes, targets, and functions. Annu. Rev. Genet. 30:209-237.
    • (1992) Annu. Rev. Genet. , vol.30 , pp. 209-237
    • Schafer, W.R.1    Rine, J.2
  • 43
    • 0028595952 scopus 로고
    • Molecular cloning and analysis of CDC28 and cyclin ho-mologues from the human fungal pathogen Candida albicans
    • Sherlock, G., A. M. Gahman, A. Mahal, J. Shieh, M. Ferreira, and J. Rosamond. 1994. Molecular cloning and analysis of CDC28 and cyclin ho-mologues from the human fungal pathogen Candida albicans. Mol. Gen. Genet. 245:716-723.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 716-723
    • Sherlock, G.1    Gahman, A.M.2    Mahal, A.3    Shieh, J.4    Ferreira, M.5    Rosamond, J.6
  • 44
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
    • (1991) Methods Enzymol. , vol.194 , pp. 3-21
    • Sherman, F.1
  • 45
    • 0032580437 scopus 로고    scopus 로고
    • An improved protocol for the preparation of yeast cells for transformation by electroporation
    • Thompson, J. R., E. Register, J. Curotto, M. Kurtz, and R. Kelly. 1998. An improved protocol for the preparation of yeast cells for transformation by electroporation. Yeast 14:565-571.
    • (1998) Yeast , vol.14 , pp. 565-571
    • Thompson, J.R.1    Register, E.2    Curotto, J.3    Kurtz, M.4    Kelly, R.5
  • 46
    • 0027299926 scopus 로고
    • Genetic evidence for in vivo cross-specificity of the CaaX-hox protein prenyltransferases farnesyltransferase and geranylgeranyltransferase-I in Saccharomyces cerevisiae
    • Trueblood, C. A., Y. Ohya, and J. Rine. 1993. Genetic evidence for in vivo cross-specificity of the CaaX-hox protein prenyltransferases farnesyltransferase and geranylgeranyltransferase-I in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:4260-4275.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4260-4275
    • Trueblood, C.A.1    Ohya, Y.2    Rine, J.3
  • 48
    • 0020060160 scopus 로고
    • Studies on the mechanism of antifungal action of aculeacin A
    • Yamaguchi, H., T. Hiratani, K. Iwata, and Y. Yamamoto. 1982. Studies on the mechanism of antifungal action of aculeacin A. J. Antibiot. 35:210-219.
    • (1982) J. Antibiot. , vol.35 , pp. 210-219
    • Yamaguchi, H.1    Hiratani, T.2    Iwata, K.3    Yamamoto, Y.4
  • 49
    • 0028228614 scopus 로고
    • Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae
    • Yamochi, W., K. Tanaka, H. Nonaka, A. Maeda, T. Musha, and Y. Takai. 1994. Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae. J. Cell Biol. 125: 1077-1093.
    • (1994) J. Cell Biol. , vol.125 , pp. 1077-1093
    • Yamochi, W.1    Tanaka, K.2    Nonaka, H.3    Maeda, A.4    Musha, T.5    Takai, Y.6
  • 50
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 51
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity
    • Yokoyama, K., G. W. Goodwin, F. Ghomashci, and J. Glomset. 1991. A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity. Proc. Natl. Acad. Sci. USA 88:5302-5306.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5302-5306
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashci, F.3    Glomset, J.4
  • 52
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F. L., and P. J. Casey. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 53
    • 0025847665 scopus 로고
    • Mutational analysis of CDC42Sc, a sacckaromyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity
    • Ziman, M., J. M. O'Brien, L. A. Ouellette, W. R. Church, and D. I. Johnson. 1991. Mutational analysis of CDC42Sc, a Sacckaromyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Mol. Cell. Biol. 11:3537-3544.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3537-3544
    • Ziman, M.1    O'Brien, J.M.2    Ouellette, L.A.3    Church, W.R.4    Johnson, D.I.5
  • 54
    • 0027744475 scopus 로고
    • Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity
    • Ziman, M., D. Preuss, J. Mulholland, J. M. O'Brien, D. Bostein, and D. I. Johnson. 1993. Subcellular localization of Cdc42p, a Saccharomyces cerevisiae GTP-binding protein involved in the control of cell polarity. Mol. Biol. Cell. 4:1307-1316.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 1307-1316
    • Ziman, M.1    Preuss, D.2    Mulholland, J.3    O'Brien, J.M.4    Bostein, D.5    Johnson, D.I.6


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