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Volumn 30, Issue , 2011, Pages 231-258

The Ras Converting Enzyme (Rce1p). Orthologs, Enzymology, and Inhibitors.

Author keywords

A Factor; CaaX proteins; Isoprenylation; Rce1p; Ste24p

Indexed keywords

EUKARYOTA; MUS; PROKARYOTA;

EID: 81255170347     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-415922-8.00010-0     Document Type: Chapter
Times cited : (3)

References (98)
  • 2
    • 77956670866 scopus 로고    scopus 로고
    • Postisoprenylation protein processing: CXXX (CaaX) endoproteases and isoprenylcysteine carboxyl methyltransferase
    • Academic Press, New York, NY, F. Tamanoi, D.S. Sigman (Eds.)
    • Young S.G., Ambroziak P., Kim E., Clarke S. Postisoprenylation protein processing: CXXX (CaaX) endoproteases and isoprenylcysteine carboxyl methyltransferase. The Enzymes 2001, Vol. XXI:155-213. Academic Press, New York, NY. F. Tamanoi, D.S. Sigman (Eds.).
    • (2001) The Enzymes , vol.21 , pp. 155-213
    • Young, S.G.1    Ambroziak, P.2    Kim, E.3    Clarke, S.4
  • 3
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann A.M., Casey P.J. Post-prenylation-processing enzymes as new targets in oncogenesis. Nat Rev Cancer 2005, 5:405-412.
    • (2005) Nat Rev Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 4
    • 34347369084 scopus 로고    scopus 로고
    • Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets
    • Konstantinopoulos P.A., Karamouzis M.V., Papavassiliou A.G. Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets. Nat Rev 2007, 6:541-555.
    • (2007) Nat Rev , vol.6 , pp. 541-555
    • Konstantinopoulos, P.A.1    Karamouzis, M.V.2    Papavassiliou, A.G.3
  • 5
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk V.L., Ashby M.N., Rine J. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science 1997, 275:1796-1800.
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 6
    • 0023974052 scopus 로고
    • The a-factor pheromone of Saccharomyces cerevisiae is essential for mating
    • Michaelis S., Herskowitz I. The a-factor pheromone of Saccharomyces cerevisiae is essential for mating. Mol Cell Biol 1988, 8:1309-1318.
    • (1988) Mol Cell Biol , vol.8 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 7
    • 0032530150 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
    • Schmidt W.K., Tam A., Fujimura-Kamada K., Michaelis S. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc Natl Acad Sci USA 1998, 95:11175-11180.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11175-11180
    • Schmidt, W.K.1    Tam, A.2    Fujimura-Kamada, K.3    Michaelis, S.4
  • 8
    • 0033538559 scopus 로고    scopus 로고
    • Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi
    • Choy E., et al. Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi. Cell 1999, 98:69-80.
    • (1999) Cell , vol.98 , pp. 69-80
    • Choy, E.1
  • 9
    • 0033605596 scopus 로고    scopus 로고
    • Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells
    • Kim E., et al. Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. J Biol Chem 1999, 274:8383-8390.
    • (1999) J Biol Chem , vol.274 , pp. 8383-8390
    • Kim, E.1
  • 10
    • 0036132907 scopus 로고    scopus 로고
    • Absence of the CAAX endoprotease Rce1: effects on cell growth and transformation
    • Bergo M.O., et al. Absence of the CAAX endoprotease Rce1: effects on cell growth and transformation. Mol Cell Biol 2002, 22:171-181.
    • (2002) Mol Cell Biol , vol.22 , pp. 171-181
    • Bergo, M.O.1
  • 11
    • 1642326112 scopus 로고    scopus 로고
    • Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf
    • Bergo M.O., et al. Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf. J Clin Invest 2004, 113:539-550.
    • (2004) J Clin Invest , vol.113 , pp. 539-550
    • Bergo, M.O.1
  • 12
    • 16344396081 scopus 로고    scopus 로고
    • Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases
    • Michaelson D., et al. Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases. Mol Biol Cell 2005, 16:1606-1616.
    • (2005) Mol Biol Cell , vol.16 , pp. 1606-1616
    • Michaelson, D.1
  • 13
    • 0024465343 scopus 로고
    • Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis
    • Gutierrez L., Magee A.I., Marshall C.J., Hancock J.F. Post-translational processing of p21ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis. EMBO J 1989, 8:1093-1098.
    • (1989) EMBO J , vol.8 , pp. 1093-1098
    • Gutierrez, L.1    Magee, A.I.2    Marshall, C.J.3    Hancock, J.F.4
  • 14
    • 0025254314 scopus 로고
    • RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine at N terminus and removal of three amino acids at C terminus
    • Fujiyama A., Tamanoi F. RAS2 protein of Saccharomyces cerevisiae undergoes removal of methionine at N terminus and removal of three amino acids at C terminus. J Biol Chem 1990, 265:3362-3368.
    • (1990) J Biol Chem , vol.265 , pp. 3362-3368
    • Fujiyama, A.1    Tamanoi, F.2
  • 15
    • 0026521412 scopus 로고
    • Endoproteolytic processing of a farnesylated peptide in vitro
    • Ashby M., King D., Rine J. Endoproteolytic processing of a farnesylated peptide in vitro. Proc Natl Acad Sci USA 1992, 89:4613-4617.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4613-4617
    • Ashby, M.1    King, D.2    Rine, J.3
  • 16
    • 0026779707 scopus 로고
    • Maturation of isoprenylated proteins in Saccharomyces cerevisiae
    • Hrycyna C.A., Clarke S. Maturation of isoprenylated proteins in Saccharomyces cerevisiae. J Biol Chem 1992, 267:10457-10464.
    • (1992) J Biol Chem , vol.267 , pp. 10457-10464
    • Hrycyna, C.A.1    Clarke, S.2
  • 17
    • 0026680433 scopus 로고
    • A microsomal endoprotease that specifically cleaves isoprenylated peptides
    • Ma Y.T., Rando R.R. A microsomal endoprotease that specifically cleaves isoprenylated peptides. Proc Natl Acad Sci USA 1992, 89:6275-6279.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6275-6279
    • Ma, Y.T.1    Rando, R.R.2
  • 19
    • 0028999661 scopus 로고
    • Ras and a-factor converting enzyme
    • Ashby M.N., Rine J. Ras and a-factor converting enzyme. Methods Enzymol 1995, 250:235-250.
    • (1995) Methods Enzymol , vol.250 , pp. 235-250
    • Ashby, M.N.1    Rine, J.2
  • 20
    • 0031055072 scopus 로고    scopus 로고
    • Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor
    • Chen P., Sapperstein S.K., Choi J.D., Michaelis S. Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor. J Cell Biol 1997, 136:251-269.
    • (1997) J Cell Biol , vol.136 , pp. 251-269
    • Chen, P.1    Sapperstein, S.K.2    Choi, J.D.3    Michaelis, S.4
  • 21
    • 0027546252 scopus 로고
    • STE6, the yeast a-factor transporter
    • Michaelis S. STE6, the yeast a-factor transporter. Semin Cell Biol 1993, 4:17-27.
    • (1993) Semin Cell Biol , vol.4 , pp. 17-27
    • Michaelis, S.1
  • 23
    • 0034052099 scopus 로고    scopus 로고
    • Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis
    • Schmidt W.K., Tam A., Michaelis S. Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis. J Biol Chem 2000, 275:6227-6233.
    • (2000) J Biol Chem , vol.275 , pp. 6227-6233
    • Schmidt, W.K.1    Tam, A.2    Michaelis, S.3
  • 24
    • 0035861547 scopus 로고    scopus 로고
    • The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor
    • Tam A., Schmidt W.K., Michaelis S. The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor. J Biol Chem 2001, 276:46798-46806.
    • (2001) J Biol Chem , vol.276 , pp. 46798-46806
    • Tam, A.1    Schmidt, W.K.2    Michaelis, S.3
  • 25
    • 0033564670 scopus 로고    scopus 로고
    • Identification and chromosomal location of two human genes encoding enzymes potentially involved in proteolytic maturation of farnesylated proteins
    • Freije J.M., Blay P., Pendas A.M., Cadinanos J., Crespo P., Lopez-Otin C. Identification and chromosomal location of two human genes encoding enzymes potentially involved in proteolytic maturation of farnesylated proteins. Genomics 1999, 58:270-280.
    • (1999) Genomics , vol.58 , pp. 270-280
    • Freije, J.M.1    Blay, P.2    Pendas, A.M.3    Cadinanos, J.4    Crespo, P.5    Lopez-Otin, C.6
  • 26
    • 0033605743 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian prenyl protein-specific protease
    • Otto J.C., Kim E., Young S.G., Casey P.J. Cloning and characterization of a mammalian prenyl protein-specific protease. J Biol Chem 1999, 274:8379-8382.
    • (1999) J Biol Chem , vol.274 , pp. 8379-8382
    • Otto, J.C.1    Kim, E.2    Young, S.G.3    Casey, P.J.4
  • 27
    • 0037444824 scopus 로고    scopus 로고
    • Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans
    • Cadiñanos J., Schmidt W.K., Fueyo A., Varela I., Lopez-Otin C., Freije J.M. Identification, functional expression and enzymic analysis of two distinct CaaX proteases from Caenorhabditis elegans. Biochem J 2003, 370:1047-1054.
    • (2003) Biochem J , vol.370 , pp. 1047-1054
    • Cadiñanos, J.1    Schmidt, W.K.2    Fueyo, A.3    Varela, I.4    Lopez-Otin, C.5    Freije, J.M.6
  • 28
    • 0142211262 scopus 로고    scopus 로고
    • AtFACE-2, a prenylated-protein protease from Arabidopsis thaliana related to Ras converting enzymes
    • Cadiñanos J., et al. AtFACE-2, a prenylated-protein protease from Arabidopsis thaliana related to Ras converting enzymes. J Biol Chem 2003, 278:42091-42097.
    • (2003) J Biol Chem , vol.278 , pp. 42091-42097
    • Cadiñanos, J.1
  • 29
    • 34247482458 scopus 로고    scopus 로고
    • C-terminal proteolysis of prenylated proteins in trypanosomatids and RNA interference of enzymes required for the post-translational processing pathway of farnesylated proteins
    • Gillespie J.R., et al. C-terminal proteolysis of prenylated proteins in trypanosomatids and RNA interference of enzymes required for the post-translational processing pathway of farnesylated proteins. Mol Biochem Parasitol 2007, 153(2):115-124.
    • (2007) Mol Biochem Parasitol , vol.153 , Issue.2 , pp. 115-124
    • Gillespie, J.R.1
  • 30
    • 55549139802 scopus 로고    scopus 로고
    • Functional analysis of Arabidopsis postprenylation CaaX processing enzymes and their function in subcellular protein targeting
    • Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S. Functional analysis of Arabidopsis postprenylation CaaX processing enzymes and their function in subcellular protein targeting. Plant Physiol 2008, 148:119-131.
    • (2008) Plant Physiol , vol.148 , pp. 119-131
    • Bracha-Drori, K.1    Shichrur, K.2    Lubetzky, T.C.3    Yalovsky, S.4
  • 31
    • 0035339494 scopus 로고    scopus 로고
    • Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases
    • Pei J., Grishin N.V. Type II CAAX prenyl endopeptidases belong to a novel superfamily of putative membrane-bound metalloproteases. Trends Biochem Sci 2001, 26:275-277.
    • (2001) Trends Biochem Sci , vol.26 , pp. 275-277
    • Pei, J.1    Grishin, N.V.2
  • 32
    • 79958720098 scopus 로고    scopus 로고
    • Expansion of Type II CAAX Proteases Reveals Evolutionary Origin of gamma-Secretase Subunit APH-1
    • Pei J., Mitchell D.A., Dixon J.E., Grishin N.V. Expansion of Type II CAAX Proteases Reveals Evolutionary Origin of gamma-Secretase Subunit APH-1. J Mol Biol 2011, 410:18-26.
    • (2011) J Mol Biol , vol.410 , pp. 18-26
    • Pei, J.1    Mitchell, D.A.2    Dixon, J.E.3    Grishin, N.V.4
  • 33
    • 0029807312 scopus 로고    scopus 로고
    • AbiG, a genotypically novel abortive infection mechanism encoded by plasmid pCI750 of Lactococcus lactis subsp. cremoris UC653
    • O'Connor L., Coffey A., Daly C., Fitzgerald G.F. AbiG, a genotypically novel abortive infection mechanism encoded by plasmid pCI750 of Lactococcus lactis subsp. cremoris UC653. Appl Environ Microbiol 1996, 62:3075-3082.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3075-3082
    • O'Connor, L.1    Coffey, A.2    Daly, C.3    Fitzgerald, G.F.4
  • 34
    • 77950652492 scopus 로고    scopus 로고
    • The abi proteins and their involvement in bacteriocin self-immunity
    • Kjos M., Snipen L., Salehian Z., Nes I.F., Diep D.B. The abi proteins and their involvement in bacteriocin self-immunity. J Bacteriol 2010, 192:2068-2076.
    • (2010) J Bacteriol , vol.192 , pp. 2068-2076
    • Kjos, M.1    Snipen, L.2    Salehian, Z.3    Nes, I.F.4    Diep, D.B.5
  • 35
    • 33746088411 scopus 로고    scopus 로고
    • Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis
    • Ellermeier C.D., Losick R. Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis. Genes Dev 2006, 20:1911-1922.
    • (2006) Genes Dev , vol.20 , pp. 1911-1922
    • Ellermeier, C.D.1    Losick, R.2
  • 36
    • 0037150534 scopus 로고    scopus 로고
    • Biochemistry. Intramembrane proteases-mixing oil and water
    • Wolfe M.S., Selkoe D.J. Biochemistry. Intramembrane proteases-mixing oil and water. Science 2002, 296:2156-2157.
    • (2002) Science , vol.296 , pp. 2156-2157
    • Wolfe, M.S.1    Selkoe, D.J.2
  • 37
    • 33748767111 scopus 로고    scopus 로고
    • Therapeutic intervention based on protein prenylation and associated modifications
    • Gelb M.H., et al. Therapeutic intervention based on protein prenylation and associated modifications. Nat Chem Biol 2006, 2:518-528.
    • (2006) Nat Chem Biol , vol.2 , pp. 518-528
    • Gelb, M.H.1
  • 38
    • 20144365360 scopus 로고    scopus 로고
    • A small-molecule inhibitor of isoprenylcysteine carboxyl methyltransferase with antitumor activity in cancer cells
    • Winter-Vann A.M., et al. A small-molecule inhibitor of isoprenylcysteine carboxyl methyltransferase with antitumor activity in cancer cells. Proc Natl Acad Sci USA 2005, 102:4336-4341.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4336-4341
    • Winter-Vann, A.M.1
  • 40
    • 33846236895 scopus 로고    scopus 로고
    • Time-dependent inhibition of isoprenylcysteine carboxyl methyltransferase by indole-based small molecules
    • Baron R.A., Peterson Y.K., Otto J.C., Rudolph J., Casey P.J. Time-dependent inhibition of isoprenylcysteine carboxyl methyltransferase by indole-based small molecules. Biochemistry 2007, 46:554-560.
    • (2007) Biochemistry , vol.46 , pp. 554-560
    • Baron, R.A.1    Peterson, Y.K.2    Otto, J.C.3    Rudolph, J.4    Casey, P.J.5
  • 41
    • 1042266632 scopus 로고    scopus 로고
    • On the physiological importance of endoproteolysis of CAAX proteins: heart-specific Rce1 knockout mice develop a lethal cardiomyopathy
    • Bergo M.O., et al. On the physiological importance of endoproteolysis of CAAX proteins: heart-specific Rce1 knockout mice develop a lethal cardiomyopathy. J Biol Chem 2004, 279(6):4729-4736.
    • (2004) J Biol Chem , vol.279 , Issue.6 , pp. 4729-4736
    • Bergo, M.O.1
  • 42
    • 33846191877 scopus 로고    scopus 로고
    • Rce1 deficiency accelerates the development of K-RAS-induced myeloproliferative disease
    • Wahlstrom A.M., et al. Rce1 deficiency accelerates the development of K-RAS-induced myeloproliferative disease. Blood 2007, 109:763-768.
    • (2007) Blood , vol.109 , pp. 763-768
    • Wahlstrom, A.M.1
  • 43
    • 54449089270 scopus 로고    scopus 로고
    • Rho Family GTPase modification and dependence on CAAX motif-signaled posttranslational modification
    • Roberts P.J., et al. Rho Family GTPase modification and dependence on CAAX motif-signaled posttranslational modification. J Biol Chem 2008, 283:25150-25163.
    • (2008) J Biol Chem , vol.283 , pp. 25150-25163
    • Roberts, P.J.1
  • 44
    • 0031756961 scopus 로고    scopus 로고
    • Inhibition of K-ras-transformed rodent and human cancer cell growth via induction of apoptosis by irreversible inhibitors of Ras endoprotease
    • Chen Y. Inhibition of K-ras-transformed rodent and human cancer cell growth via induction of apoptosis by irreversible inhibitors of Ras endoprotease. Cancer Lett 1998, 131:191-200.
    • (1998) Cancer Lett , vol.131 , pp. 191-200
    • Chen, Y.1
  • 45
    • 0033452547 scopus 로고    scopus 로고
    • Selective inhibition of ras-transformed cell growth by a novel fatty acid-based chloromethyl ketone designed to target Ras endoprotease
    • Chen Y. Selective inhibition of ras-transformed cell growth by a novel fatty acid-based chloromethyl ketone designed to target Ras endoprotease. Ann N Y Acad Sci 1999, 886:103-108.
    • (1999) Ann N Y Acad Sci , vol.886 , pp. 103-108
    • Chen, Y.1
  • 46
    • 0037443394 scopus 로고    scopus 로고
    • Hematologic effects of inactivating the Ras processing enzyme Rce1
    • Aiyagari A.L., Taylor B.R., Aurora V., Young S.G., Shannon K.M. Hematologic effects of inactivating the Ras processing enzyme Rce1. Blood 2003, 101:2250-2252.
    • (2003) Blood , vol.101 , pp. 2250-2252
    • Aiyagari, A.L.1    Taylor, B.R.2    Aurora, V.3    Young, S.G.4    Shannon, K.M.5
  • 47
    • 79957771203 scopus 로고    scopus 로고
    • RAS-converting enzyme 1-mediated endoproteolysis is required for trafficking of rod phosphodiesterase 6 to photoreceptor outer segments
    • Christiansen J.R., Kolandaivelu S., Bergo M.O., Ramamurthy V. RAS-converting enzyme 1-mediated endoproteolysis is required for trafficking of rod phosphodiesterase 6 to photoreceptor outer segments. Proc Natl Acad Sci USA 2011, 108(21):8862-8866.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.21 , pp. 8862-8866
    • Christiansen, J.R.1    Kolandaivelu, S.2    Bergo, M.O.3    Ramamurthy, V.4
  • 48
    • 0345073644 scopus 로고    scopus 로고
    • Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics
    • Gelb M.H., et al. Protein farnesyl and N-myristoyl transferases: piggy-back medicinal chemistry targets for the development of antitrypanosomatid and antimalarial therapeutics. Mol Biochem Parasitol 2003, 126:155-163.
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 155-163
    • Gelb, M.H.1
  • 49
    • 73349096578 scopus 로고    scopus 로고
    • Heterologous expression studies of Saccharomyces cerevisiae reveal two distinct trypanosomatid CaaX protease activities and identify their potential targets
    • Mokry D.Z., Manandhar S.P., Chicola K.A., Santangelo G.M., Schmidt W.K. Heterologous expression studies of Saccharomyces cerevisiae reveal two distinct trypanosomatid CaaX protease activities and identify their potential targets. Eukaryot Cell 2009, 8:1891-1900.
    • (2009) Eukaryot Cell , vol.8 , pp. 1891-1900
    • Mokry, D.Z.1    Manandhar, S.P.2    Chicola, K.A.3    Santangelo, G.M.4    Schmidt, W.K.5
  • 50
    • 77949527805 scopus 로고    scopus 로고
    • Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria
    • Yang S.H., Chang S.Y., Andres D.A., Spielmann H.P., Young S.G., Fong L.G. Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria. J Lipid Res 2010, 51:400-405.
    • (2010) J Lipid Res , vol.51 , pp. 400-405
    • Yang, S.H.1    Chang, S.Y.2    Andres, D.A.3    Spielmann, H.P.4    Young, S.G.5    Fong, L.G.6
  • 52
    • 77955397296 scopus 로고    scopus 로고
    • Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila
    • Price C.T., Al-Quadan T., Santic M., Jones S.C., Abu Kwaik Y. Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila. J Exp Med 2010, 207:1713-1726.
    • (2010) J Exp Med , vol.207 , pp. 1713-1726
    • Price, C.T.1    Al-Quadan, T.2    Santic, M.3    Jones, S.C.4    Abu Kwaik, Y.5
  • 53
    • 33644784689 scopus 로고    scopus 로고
    • Endoproteolytic processing of RhoA by Rce1 is required for the cleavage of RhoA by Yersinia enterocolitica outer protein T
    • Fueller F., Bergo M.O., Young S.G., Aktories K., Schmidt G. Endoproteolytic processing of RhoA by Rce1 is required for the cleavage of RhoA by Yersinia enterocolitica outer protein T. Infect Immun 2006, 74:1712-1717.
    • (2006) Infect Immun , vol.74 , pp. 1712-1717
    • Fueller, F.1    Bergo, M.O.2    Young, S.G.3    Aktories, K.4    Schmidt, G.5
  • 54
    • 77957233208 scopus 로고    scopus 로고
    • ABI domain-containing proteins contribute to surface protein display and cell division in Staphylococcus aureus
    • Frankel M.B., Wojcik B.M., DeDent A.C., Missiakas D.M., Schneewind O. ABI domain-containing proteins contribute to surface protein display and cell division in Staphylococcus aureus. Mol Microbiol 2010, 78:238-252.
    • (2010) Mol Microbiol , vol.78 , pp. 238-252
    • Frankel, M.B.1    Wojcik, B.M.2    DeDent, A.C.3    Missiakas, D.M.4    Schneewind, O.5
  • 55
    • 52449132676 scopus 로고    scopus 로고
    • The impact of antimicrobial-resistant, health care-associated infections on mortality in the United States
    • Klevens R.M., Edwards J.R., Gaynes R.P. The impact of antimicrobial-resistant, health care-associated infections on mortality in the United States. Clin Infect Dis 2008, 47:927-930.
    • (2008) Clin Infect Dis , vol.47 , pp. 927-930
    • Klevens, R.M.1    Edwards, J.R.2    Gaynes, R.P.3
  • 56
    • 61349125517 scopus 로고    scopus 로고
    • New insights into pneumococcal disease
    • Feldman C., Anderson R. New insights into pneumococcal disease. Respirology 2009, 14:167-179.
    • (2009) Respirology , vol.14 , pp. 167-179
    • Feldman, C.1    Anderson, R.2
  • 57
    • 70350498834 scopus 로고    scopus 로고
    • Pathogenesis, treatment, and prevention of pneumococcal pneumonia
    • van der Poll T., Opal S.M. Pathogenesis, treatment, and prevention of pneumococcal pneumonia. Lancet 2009, 374:1543-1556.
    • (2009) Lancet , vol.374 , pp. 1543-1556
    • van der Poll, T.1    Opal, S.M.2
  • 59
    • 0031664339 scopus 로고    scopus 로고
    • Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiaea-factor
    • Boyartchuk V.L., Rine J. Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiaea-factor. Genetics 1998, 150:95-101.
    • (1998) Genetics , vol.150 , pp. 95-101
    • Boyartchuk, V.L.1    Rine, J.2
  • 61
    • 0036791026 scopus 로고    scopus 로고
    • Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect
    • Bergo M.O., et al. Zmpste24 deficiency in mice causes spontaneous bone fractures, muscle weakness, and a prelamin A processing defect. Proc Natl Acad Sci USA 2002, 99:13049-13054.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13049-13054
    • Bergo, M.O.1
  • 62
    • 59249084586 scopus 로고    scopus 로고
    • Ggamma1, a downstream target for the hmgcr-isoprenoid biosynthetic pathway, is required for releasing the Hedgehog ligand and directing germ cell migration
    • Deshpande G., Godishala A., Schedl P. Ggamma1, a downstream target for the hmgcr-isoprenoid biosynthetic pathway, is required for releasing the Hedgehog ligand and directing germ cell migration. PLoS Genet 2009, 5:e1000333.
    • (2009) PLoS Genet , vol.5
    • Deshpande, G.1    Godishala, A.2    Schedl, P.3
  • 63
    • 60149098422 scopus 로고    scopus 로고
    • An ABC transporter controls export of a Drosophila germ cell attractant
    • Ricardo S., Lehmann R. An ABC transporter controls export of a Drosophila germ cell attractant. Science 2009, 323:943-946.
    • (2009) Science , vol.323 , pp. 943-946
    • Ricardo, S.1    Lehmann, R.2
  • 64
    • 0037119482 scopus 로고    scopus 로고
    • The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity
    • Bracha K., Lavy M., Yalovsky S. The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity. J Biol Chem 2002, 277:29856-29864.
    • (2002) J Biol Chem , vol.277 , pp. 29856-29864
    • Bracha, K.1    Lavy, M.2    Yalovsky, S.3
  • 65
    • 33646192360 scopus 로고    scopus 로고
    • Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues
    • Plummer L.J., Hildebrandt E.R., Porter S.B., Rogers V.A., McCracken J., Schmidt W.K. Mutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residues. J Biol Chem 2006, 281:4596-4605.
    • (2006) J Biol Chem , vol.281 , pp. 4596-4605
    • Plummer, L.J.1    Hildebrandt, E.R.2    Porter, S.B.3    Rogers, V.A.4    McCracken, J.5    Schmidt, W.K.6
  • 66
    • 0026747866 scopus 로고
    • Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity
    • Kato K., Cox A., Hisaka M., Graham S., Buss J., Der C. Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity. Proc Natl Acad Sci USA 1992, 89:6403-6407.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6403-6407
    • Kato, K.1    Cox, A.2    Hisaka, M.3    Graham, S.4    Buss, J.5    Der, C.6
  • 67
    • 0032322785 scopus 로고    scopus 로고
    • Functional assays for the analysis of yeast ste6 mutants
    • Nijbroek G.L., Michaelis S. Functional assays for the analysis of yeast ste6 mutants. Methods Enzymol 1998, 292:193-212.
    • (1998) Methods Enzymol , vol.292 , pp. 193-212
    • Nijbroek, G.L.1    Michaelis, S.2
  • 68
    • 0025860189 scopus 로고
    • Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiaea-factor mating pheromone
    • Marcus S., Caldwell G.A., Miller D., Xue C.-B., Naider F., Becker J.M. Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiaea-factor mating pheromone. Mol Cell Biol 1991, 11:3603-3612.
    • (1991) Mol Cell Biol , vol.11 , pp. 3603-3612
    • Marcus, S.1    Caldwell, G.A.2    Miller, D.3    Xue, C.-B.4    Naider, F.5    Becker, J.M.6
  • 69
    • 0035800833 scopus 로고    scopus 로고
    • Biochemical studies of Zmpste24-deficient mice
    • Leung G.K., et al. Biochemical studies of Zmpste24-deficient mice. J Biol Chem 2001, 276:29051-29058.
    • (2001) J Biol Chem , vol.276 , pp. 29051-29058
    • Leung, G.K.1
  • 70
    • 75149142796 scopus 로고    scopus 로고
    • Differential requirement of CAAX-mediated posttranslational processing for Rheb localization and signaling
    • Hanker A.B., et al. Differential requirement of CAAX-mediated posttranslational processing for Rheb localization and signaling. Oncogene 2010, 29:380-391.
    • (2010) Oncogene , vol.29 , pp. 380-391
    • Hanker, A.B.1
  • 71
  • 72
    • 0034636066 scopus 로고    scopus 로고
    • Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p
    • Dolence J.M., Steward L.E., Dolence E.K., Wong D.H., Poulter C.D. Studies with recombinant Saccharomyces cerevisiae CaaX prenyl protease Rce1p. Biochemistry 2000, 39:4096-4104.
    • (2000) Biochemistry , vol.39 , pp. 4096-4104
    • Dolence, J.M.1    Steward, L.E.2    Dolence, E.K.3    Wong, D.H.4    Poulter, C.D.5
  • 73
    • 0029990398 scopus 로고    scopus 로고
    • Solubilization, partial purification, and affinity labeling of the membrane-bound isoprenylated protein endoprotease
    • Chen Y., Ma Y.T., Rando R.R. Solubilization, partial purification, and affinity labeling of the membrane-bound isoprenylated protein endoprotease. Biochemistry 1996, 35:3227-3237.
    • (1996) Biochemistry , vol.35 , pp. 3227-3237
    • Chen, Y.1    Ma, Y.T.2    Rando, R.R.3
  • 75
    • 0027518956 scopus 로고
    • Inhibitors of the isoprenylated protein endoprotease
    • Ma Y.-T., Gilbert B., Rando R. Inhibitors of the isoprenylated protein endoprotease. Biochemistry 1993, 32:2386-2393.
    • (1993) Biochemistry , vol.32 , pp. 2386-2393
    • Ma, Y.-T.1    Gilbert, B.2    Rando, R.3
  • 76
    • 0034263198 scopus 로고    scopus 로고
    • Solid-phase synthesis of a farnesylated CaaX peptide library: inhibitors of the Ras CaaX endoprotease
    • Dolence E.K., Dolence J.M., Poulter C.D. Solid-phase synthesis of a farnesylated CaaX peptide library: inhibitors of the Ras CaaX endoprotease. J Comb Chem 2000, 2:522-536.
    • (2000) J Comb Chem , vol.2 , pp. 522-536
    • Dolence, E.K.1    Dolence, J.M.2    Poulter, C.D.3
  • 77
    • 0036644114 scopus 로고    scopus 로고
    • Novel sesterterpenoid and norsesterterpenoid RCE-protease inhibitors isolated from the marine sponge Hippospongia sp
    • Craig K.S., et al. Novel sesterterpenoid and norsesterterpenoid RCE-protease inhibitors isolated from the marine sponge Hippospongia sp. Tetrahedron Lett 2002, 43:4801-4804.
    • (2002) Tetrahedron Lett , vol.43 , pp. 4801-4804
    • Craig, K.S.1
  • 78
    • 67650243224 scopus 로고    scopus 로고
    • Scalarane-based sesterterpenoid RCE-protease inhibitors isolated from the Indonesian marine sponge Carteriospongia foliascens
    • Williams D.E., et al. Scalarane-based sesterterpenoid RCE-protease inhibitors isolated from the Indonesian marine sponge Carteriospongia foliascens. J Nat Prod 2009, 72:1106-1109.
    • (2009) J Nat Prod , vol.72 , pp. 1106-1109
    • Williams, D.E.1
  • 79
    • 77955982513 scopus 로고    scopus 로고
    • Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases
    • Dechert A.M., et al. Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases. Bioorg Med Chem 2010, 18:6230-6237.
    • (2010) Bioorg Med Chem , vol.18 , pp. 6230-6237
    • Dechert, A.M.1
  • 80
    • 29444460784 scopus 로고    scopus 로고
    • Activity-based probes that target diverse cysteine protease families
    • Kato D., et al. Activity-based probes that target diverse cysteine protease families. Nat Chem Biol 2005, 1:33-38.
    • (2005) Nat Chem Biol , vol.1 , pp. 33-38
    • Kato, D.1
  • 81
    • 0035847663 scopus 로고    scopus 로고
    • Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1
    • Schlitzer M., Winter-Vann A., Casey P.J. Non-peptidic, non-prenylic inhibitors of the prenyl protein-specific protease Rce1. Bioorg Med Chem Lett 2001, 11:425-427.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 425-427
    • Schlitzer, M.1    Winter-Vann, A.2    Casey, P.J.3
  • 82
    • 0026454274 scopus 로고
    • Substrate specificity of the isoprenylated protein endoprotease
    • Ma Y.T., Chaudhuri A., Rando R.R. Substrate specificity of the isoprenylated protein endoprotease. Biochemistry 1992, 31:11772-11777.
    • (1992) Biochemistry , vol.31 , pp. 11772-11777
    • Ma, Y.T.1    Chaudhuri, A.2    Rando, R.R.3
  • 83
    • 0027527703 scopus 로고
    • A prenylated protein-specific endoprotease in rat liver microsomes that produces a carboxyl-terminal tripeptide
    • Jang G.F., Yokoyama K., Gelb M.H. A prenylated protein-specific endoprotease in rat liver microsomes that produces a carboxyl-terminal tripeptide. Biochemistry 1993, 32:9500-9507.
    • (1993) Biochemistry , vol.32 , pp. 9500-9507
    • Jang, G.F.1    Yokoyama, K.2    Gelb, M.H.3
  • 84
    • 0028916399 scopus 로고
    • Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modification pathway
    • Farh L., Mitchell D.A., Deschenes R.J. Farnesylation and proteolysis are sequential, but distinct steps in the CaaX box modification pathway. Arch Biochem Biophys 1995, 318:113-121.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 113-121
    • Farh, L.1    Mitchell, D.A.2    Deschenes, R.J.3
  • 85
    • 0034327206 scopus 로고    scopus 로고
    • Human ras-converting enzyme (hRCE1) endoproteolytic activity on K-ras-derived peptides
    • Hollander I., Frommer E., Mallon R. Human ras-converting enzyme (hRCE1) endoproteolytic activity on K-ras-derived peptides. Anal Biochem 2000, 286:129-137.
    • (2000) Anal Biochem , vol.286 , pp. 129-137
    • Hollander, I.1    Frommer, E.2    Mallon, R.3
  • 86
    • 1242273732 scopus 로고    scopus 로고
    • Human Ras converting enzyme endoproteolytic specificity at the P2' and P3' positions of K-Ras-derived peptides
    • Hollander I.J., Frommer E., Aulabaugh A., Mallon R. Human Ras converting enzyme endoproteolytic specificity at the P2' and P3' positions of K-Ras-derived peptides. Biochim Biophys Acta 2003, 1649:24-29.
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 24-29
    • Hollander, I.J.1    Frommer, E.2    Aulabaugh, A.3    Mallon, R.4
  • 87
    • 0027253720 scopus 로고
    • Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11
    • Le Moual H., Roques B.P., Crine P., Boileau G. Substitution of potential metal-coordinating amino acid residues in the zinc-binding site of endopeptidase-24.11. FEBS Lett 1993, 324:196-200.
    • (1993) FEBS Lett , vol.324 , pp. 196-200
    • Le Moual, H.1    Roques, B.P.2    Crine, P.3    Boileau, G.4
  • 88
    • 0029930429 scopus 로고    scopus 로고
    • Identification of glutamate residues essential for catalytic activity and zinc coordination in aminopeptidase A
    • Vazeux G., Wang J., Corvol P., Llorens-Cortes C. Identification of glutamate residues essential for catalytic activity and zinc coordination in aminopeptidase A. J Biol Chem 1996, 271:9069-9074.
    • (1996) J Biol Chem , vol.271 , pp. 9069-9074
    • Vazeux, G.1    Wang, J.2    Corvol, P.3    Llorens-Cortes, C.4
  • 89
    • 3843081911 scopus 로고    scopus 로고
    • The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica
    • Bzymek K.P., Holz R.C. The catalytic role of glutamate 151 in the leucine aminopeptidase from Aeromonas proteolytica. J Biol Chem 2004, 279:31018-31025.
    • (2004) J Biol Chem , vol.279 , pp. 31018-31025
    • Bzymek, K.P.1    Holz, R.C.2
  • 90
    • 1542723495 scopus 로고    scopus 로고
    • The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
    • Fujinaga M., Cherney M.M., Oyama H., Oda K., James M.N. The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum. Proc Natl Acad Sci USA 2004, 101:3364-3369.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3364-3369
    • Fujinaga, M.1    Cherney, M.M.2    Oyama, H.3    Oda, K.4    James, M.N.5
  • 91
    • 66249133368 scopus 로고    scopus 로고
    • How intramembrane proteases bury hydrolytic reactions in the membrane
    • Erez E., Fass D., Bibi E. How intramembrane proteases bury hydrolytic reactions in the membrane. Nature 2009, 459:371-378.
    • (2009) Nature , vol.459 , pp. 371-378
    • Erez, E.1    Fass, D.2    Bibi, E.3
  • 92
    • 67649827390 scopus 로고    scopus 로고
    • Intramembrane-cleaving Proteases
    • Wolfe M.S. Intramembrane-cleaving Proteases. Biol Chem 2009, 284:13969-13973.
    • (2009) Biol Chem , vol.284 , pp. 13969-13973
    • Wolfe, M.S.1
  • 93
    • 65549141038 scopus 로고    scopus 로고
    • Protein structures: structures of desire
    • Bhattacharya A. Protein structures: structures of desire. Nature 2009, 459:24-27.
    • (2009) Nature , vol.459 , pp. 24-27
    • Bhattacharya, A.1
  • 94
    • 77955412758 scopus 로고    scopus 로고
    • Photoaffinity labeling of Ras converting enzyme 1 (Rce1p) using a benzophenone-containing peptide substrate
    • Kyro K., Manandhar S.P., Daniel Mullen D., Schmidt W.K., Distefano M.D. Photoaffinity labeling of Ras converting enzyme 1 (Rce1p) using a benzophenone-containing peptide substrate. Bioorg Med Chem 2010, 18(15):5675-5684.
    • (2010) Bioorg Med Chem , vol.18 , Issue.15 , pp. 5675-5684
    • Kyro, K.1    Manandhar, S.P.2    Daniel Mullen, D.3    Schmidt, W.K.4    Distefano, M.D.5
  • 95
    • 66149093056 scopus 로고    scopus 로고
    • USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity
    • Burrows J.F., et al. USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity. J Biol Chem 2009, 284:9587-9595.
    • (2009) J Biol Chem , vol.284 , pp. 9587-9595
    • Burrows, J.F.1
  • 96
    • 77951242559 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP17 blocks N-Ras membrane trafficking and activation but leaves K-Ras unaffected
    • de la Vega M., Burrows J.F., McFarlane C., Govender U., Scott C.J., Johnston J.A. The deubiquitinating enzyme USP17 blocks N-Ras membrane trafficking and activation but leaves K-Ras unaffected. J Biol Chem 2010, 285:12028-12036.
    • (2010) J Biol Chem , vol.285 , pp. 12028-12036
    • de la Vega, M.1    Burrows, J.F.2    McFarlane, C.3    Govender, U.4    Scott, C.J.5    Johnston, J.A.6
  • 97
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: new molecular signals. 'Protein modifications: beyond the usual suspects' review series
    • Ikeda F., Dikic I. Atypical ubiquitin chains: new molecular signals. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 2008, 9:536-542.
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 98
    • 79953235713 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility
    • de la Vega M., et al. The deubiquitinating enzyme USP17 is essential for GTPase subcellular localization and cell motility. Nat Commun 2011, 2:259.
    • (2011) Nat Commun , vol.2 , pp. 259
    • de la Vega, M.1


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