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Volumn 288, Issue 22, 2013, Pages 15430-15436

Structure and mechanism of rhomboid protease

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL ASSAY; BIOLOGICAL FUNCTIONS; CATALYTIC MECHANISMS; CONFORMATIONAL CHANGE; CRYSTALLOGRAPHIC ANALYSIS; MEMBRANE PROTEINS; MEMBRANE-SPANNING SEGMENTS; TRANS-MEMBRANE DOMAINS;

EID: 84878404648     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R112.422378     Document Type: Review
Times cited : (31)

References (62)
  • 1
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases
    • DOI 10.1016/S0092-8674(01)00525-6
    • Urban, S., Lee, J. R., and Freeman, M. (2001) Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107, 173-182 (Pubitemid 33035944)
    • (2001) Cell , vol.107 , Issue.2 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 2
    • 0024114027 scopus 로고
    • A group of genes required for pattern formation in the ventral ectoderm of the Drosophila embryo
    • Mayer, U., and Nüsslein-Volhard, C. (1988) A group of genes required for pattern formation in the ventral ectoderm of the Drosophila embryo. Genes Dev. 2, 1496-1511
    • (1988) Genes Dev. , vol.2 , pp. 1496-1511
    • Mayer, U.1    Nüsslein-Volhard, C.2
  • 3
    • 0037264371 scopus 로고    scopus 로고
    • The rhomboids: A nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers
    • Koonin, E. V., Makarova, K. S., Rogozin, I. B., Davidovic, L., Letellier, M. C., and Pellegrini, L. (2003) The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers. Genome Biol. 4, R19
    • (2003) Genome Biol. , vol.4
    • Koonin, E.V.1    Makarova, K.S.2    Rogozin, I.B.3    Davidovic, L.4    Letellier, M.C.5    Pellegrini, L.6
  • 4
    • 35948982252 scopus 로고    scopus 로고
    • Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
    • DOI 10.1101/gr.6425307
    • Lemberg, M. K., and Freeman, M. (2007) Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases. Genome Res. 17, 1634-1646 (Pubitemid 350074859)
    • (2007) Genome Research , vol.17 , Issue.11 , pp. 1634-1646
    • Lemberg, M.K.1    Freeman, M.2
  • 6
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • DOI 10.1038/nature01633
    • McQuibban, G. A., Saurya, S., and Freeman, M. (2003) Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423, 537-541 (Pubitemid 36648577)
    • (2003) Nature , vol.423 , Issue.6939 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 8
    • 40449124712 scopus 로고    scopus 로고
    • Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons
    • DOI 10.1038/nature06604, PII NATURE06604
    • Chao, J. R., Parganas, E., Boyd, K., Hong, C. Y., Opferman, J. T., and Ihle, J. N. (2008) Hax1-mediated processing of HtrA2 by Parl allows survival of lymphocytes and neurons. Nature 452, 98-102 (Pubitemid 351355088)
    • (2008) Nature , vol.452 , Issue.7183 , pp. 98-102
    • Chao, J.-R.1    Parganas, E.2    Boyd, K.3    Hong, C.Y.4    Opferman, J.T.5    Ihle, J.N.6
  • 9
    • 79953269767 scopus 로고    scopus 로고
    • Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling
    • Zettl, M., Adrain, C., Strisovsky, K., Lastun, V., and Freeman, M. (2011) Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling. Cell 145, 79-91
    • (2011) Cell , vol.145 , pp. 79-91
    • Zettl, M.1    Adrain, C.2    Strisovsky, K.3    Lastun, V.4    Freeman, M.5
  • 10
    • 84855822415 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE
    • Adrain, C., Zettl, M., Christova, Y., Taylor, N., and Freeman, M. (2012) Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE. Science 335, 225-228
    • (2012) Science , vol.335 , pp. 225-228
    • Adrain, C.1    Zettl, M.2    Christova, Y.3    Taylor, N.4    Freeman, M.5
  • 12
    • 79251602713 scopus 로고    scopus 로고
    • Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode
    • Santos, J. M., Ferguson, D. J., Blackman, M. J., and Soldati-Favre, D. (2011) Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode. Science 331, 473-477
    • (2011) Science , vol.331 , pp. 473-477
    • Santos, J.M.1    Ferguson, D.J.2    Blackman, M.J.3    Soldati-Favre, D.4
  • 13
    • 77954078996 scopus 로고    scopus 로고
    • Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii
    • Buguliskis, J. S., Brossier, F., Shuman, J., and Sibley, L. D. (2010) Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii. PLoS Pathog. 6, e1000858
    • (2010) PLoS Pathog. , vol.6
    • Buguliskis, J.S.1    Brossier, F.2    Shuman, J.3    Sibley, L.D.4
  • 15
    • 58549108805 scopus 로고    scopus 로고
    • Rhomboid proteases and their biological functions
    • Freeman, M. (2008) Rhomboid proteases and their biological functions. Annu. Rev. Genet. 42, 191-210
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 191-210
    • Freeman, M.1
  • 16
    • 77955280924 scopus 로고    scopus 로고
    • The PARL family of mitochondrial rhomboid proteases
    • Hill, R. B., and Pellegrini, L. (2010) The PARL family of mitochondrial rhomboid proteases. Semin. Cell Dev. Biol. 21, 582-592
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 582-592
    • Hill, R.B.1    Pellegrini, L.2
  • 17
    • 33751246749 scopus 로고    scopus 로고
    • Rhomboid proteins: Conserved membrane proteases with divergent biological functions
    • Urban, S. (2006) Rhomboid proteins: conserved membrane proteases with divergent biological functions. Genes Dev. 20, 3054-3068
    • (2006) Genes Dev. , vol.20 , pp. 3054-3068
    • Urban, S.1
  • 18
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown, M. S., Ye, J., Rawson, R. B., and Goldstein, J. L. (2000) Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100, 391-398
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 19
    • 4143084775 scopus 로고    scopus 로고
    • Intramembrane proteolysis: Theme and variations
    • DOI 10.1126/science.1096187
    • Wolfe, M. S., and Kopan, R. (2004) Intramembrane proteolysis: theme and variations. Science 305, 1119-1123 (Pubitemid 39100316)
    • (2004) Science , vol.305 , Issue.5687 , pp. 1119-1123
    • Wolfe, M.S.1    Kopan, R.2
  • 20
    • 63649088506 scopus 로고    scopus 로고
    • Structure and mechanism of intramembrane protease
    • Ha, Y. (2009) Structure and mechanism of intramembrane protease. Semin. Cell Dev. Biol. 20, 240-250
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 240-250
    • Ha, Y.1
  • 21
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang, Y., Zhang, Y., and Ha, Y. (2006) Crystal structure of a rhomboid family intramembrane protease. Nature 444, 179-180
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 25
  • 26
    • 79952316125 scopus 로고    scopus 로고
    • Structure of rhomboid protease in a lipid environment
    • Vinothkumar, K. R. (2011) Structure of rhomboid protease in a lipid environment. J. Mol. Biol. 407, 232-247
    • (2011) J. Mol. Biol. , vol.407 , pp. 232-247
    • Vinothkumar, K.R.1
  • 27
    • 14844300797 scopus 로고    scopus 로고
    • Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
    • DOI 10.1038/sj.emboj.7600537
    • Lemberg, M. K., Menendez, J., Misik, A., Garcia, M., Koth, C. M., and Freeman, M. (2005) Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases. EMBO J. 24, 464-472 (Pubitemid 40343249)
    • (2005) EMBO Journal , vol.24 , Issue.3 , pp. 464-472
    • Lemberg, M.K.1    Menendez, J.2    Misik, A.3    Garcia, M.4    Koth, C.M.5    Freeman, M.6
  • 28
    • 26644441432 scopus 로고    scopus 로고
    • Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane
    • DOI 10.1021/bi051363k
    • Maegawa, S., Ito, K., and Akiyama, Y. (2005) Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane. Biochemistry 44, 13543-13552 (Pubitemid 41443681)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13543-13552
    • Maegawa, S.1    Ito, K.2    Akiyama, Y.3
  • 30
    • 13844306483 scopus 로고    scopus 로고
    • Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
    • DOI 10.1073/pnas.0408306102
    • Urban, S., and Wolfe, M. S. (2005) Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc. Natl. Acad. Sci. U.S.A. 102, 1883-1888 (Pubitemid 40261981)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.6 , pp. 1883-1888
    • Urban, S.1    Wolfe, M.S.2
  • 31
    • 0022271601 scopus 로고
    • Reaction of serine with substituted isocoumarins: Discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor
    • DOI 10.1021/bi00329a005
    • Harper, J. W., Hemmi, K., and Powers, J. C. (1985) Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor. Biochemistry 24, 1831-1841 (Pubitemid 15019774)
    • (1985) Biochemistry , vol.24 , Issue.8 , pp. 1831-1841
    • Harper, J.W.1    Hemmi, K.2    Powers, J.C.3
  • 33
    • 84856292019 scopus 로고    scopus 로고
    • Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
    • Xue, Y., and Ha, Y. (2012) Catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate. J. Biol. Chem. 287, 3099-3107
    • (2012) J. Biol. Chem. , vol.287 , pp. 3099-3107
    • Xue, Y.1    Ha, Y.2
  • 35
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a β- lactam inhibitor
    • DOI 10.1038/24196
    • Paetzel, M., Dalbey, R. E., and Strynadka, N. C. (1998) Crystal structure of a bacterial signal peptidase in complex with a β-lactam inhibitor. Nature 396, 186-190 (Pubitemid 28523623)
    • (1998) Nature , vol.396 , Issue.6707 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.J.3
  • 37
    • 84860711067 scopus 로고    scopus 로고
    • Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S′ subsites
    • Xue, Y., Chowdhury, S., Liu, X., Akiyama, Y., Ellman, J., and Ha, Y. (2012) Conformational change in rhomboid protease GlpG induced by inhibitor binding to its S′ subsites. Biochemistry 51, 3723-3731
    • (2012) Biochemistry , vol.51 , pp. 3723-3731
    • Xue, Y.1    Chowdhury, S.2    Liu, X.3    Akiyama, Y.4    Ellman, J.5    Ha, Y.6
  • 38
    • 84878409837 scopus 로고    scopus 로고
    • Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease
    • 10.1074/jbc.M112.438127
    • Xue, Y., and Ha, Y. (2012) Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease. J. Biol. Chem. 10.1074/jbc.M112.438127
    • (2012) J. Biol. Chem.
    • Xue, Y.1    Ha, Y.2
  • 39
    • 34247370690 scopus 로고    scopus 로고
    • The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates
    • DOI 10.1111/j.1365-2958.2007.05679.x
    • Maegawa, S., Koide, K., Ito, K., and Akiyama, Y. (2007) The intramembrane active site of GlpG, an E. coli rhomboid protease, is accessible to water and hydrolyses an extramembrane peptide bond of substrates. Mol. Microbiol. 64, 435-447 (Pubitemid 46632636)
    • (2007) Molecular Microbiology , vol.64 , Issue.2 , pp. 435-447
    • Maegawa, S.1    Koide, K.2    Ito, K.3    Akiyama, Y.4
  • 40
    • 79955526700 scopus 로고    scopus 로고
    • Mammalian EGF receptor activation by the rhomboid protease RHBDL2
    • Adrain, C., Strisovsky, K., Zettl, M., Hu, L., Lemberg, M. K., and Freeman, M. (2011) Mammalian EGF receptor activation by the rhomboid protease RHBDL2. EMBO Rep. 12, 421-427
    • (2011) EMBO Rep. , vol.12 , pp. 421-427
    • Adrain, C.1    Strisovsky, K.2    Zettl, M.3    Hu, L.4    Lemberg, M.K.5    Freeman, M.6
  • 41
    • 35748974498 scopus 로고    scopus 로고
    • The Role of L1 Loop in the Mechanism of Rhomboid Intramembrane Protease GlpG
    • DOI 10.1016/j.jmb.2007.10.014, PII S0022283607013356
    • Wang, Y., Maegawa, S., Akiyama, Y., and Ha, Y. (2007) The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG. J. Mol. Biol. 374, 1104-1113 (Pubitemid 350052106)
    • (2007) Journal of Molecular Biology , vol.374 , Issue.4 , pp. 1104-1113
    • Wang, Y.1    Maegawa, S.2    Akiyama, Y.3    Ha, Y.4
  • 42
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • Bondar, A. N., del Val, C., and White, S. H. (2009) Rhomboid protease dynamics and lipid interactions. Structure 17, 395-405
    • (2009) Structure , vol.17 , pp. 395-405
    • Bondar, A.N.1    Del Val, C.2    White, S.H.3
  • 43
    • 0022510143 scopus 로고
    • Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman, D. M., Steitz, T. A., and Goldman, A. (1986) Identifying non-polar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15, 321-353
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 45
    • 84865328335 scopus 로고    scopus 로고
    • Architectural and thermodynamic principles underlying intramembrane protease function
    • Baker, R. P., and Urban, S. (2012) Architectural and thermodynamic principles underlying intramembrane protease function. Nat. Chem. Biol. 8, 759-768
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 759-768
    • Baker, R.P.1    Urban, S.2
  • 46
    • 50849109498 scopus 로고    scopus 로고
    • In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells
    • Urban, S., and Baker, R. P. (2008) In vivo analysis reveals substrate-gating mutants of a rhomboid intramembrane protease display increased activity in living cells. Biol. Chem. 389, 1107-1115
    • (2008) Biol. Chem. , vol.389 , pp. 1107-1115
    • Urban, S.1    Baker, R.P.2
  • 47
    • 0037015265 scopus 로고    scopus 로고
    • Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids
    • DOI 10.1016/S0960-9822(02)01092-8, PII S0960982202010928
    • Urban, S., Schlieper, D., and Freeman, M. (2002) Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids. Curr. Biol. 12, 1507-1512 (Pubitemid 35036649)
    • (2002) Current Biology , vol.12 , Issue.17 , pp. 1507-1512
    • Urban, S.1    Schlieper, D.2    Freeman, M.3
  • 48
    • 0037126036 scopus 로고    scopus 로고
    • A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes
    • Gallio, M., Sturgill, G., Rather, P., and Kylsten, P. (2002) A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes. Proc. Natl. Acad. Sci. U.S.A. 99, 12208-12213
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12208-12213
    • Gallio, M.1    Sturgill, G.2    Rather, P.3    Kylsten, P.4
  • 49
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of Rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • DOI 10.1016/S1097-2765(03)00181-3
    • Urban, S., and Freeman, M. (2003) Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol. Cell 11, 1425-1434 (Pubitemid 36776530)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 50
    • 34248371981 scopus 로고    scopus 로고
    • Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease
    • DOI 10.1111/j.1365-2958.2007.05715.x
    • Akiyama, Y., and Maegawa, S. (2007) Sequence features of substrates required for cleavage by GlpG, an Escherichia coli rhomboid protease. Mol. Microbiol. 64, 1028-1037 (Pubitemid 46743969)
    • (2007) Molecular Microbiology , vol.64 , Issue.4 , pp. 1028-1037
    • Akiyama, Y.1    Maegawa, S.2
  • 51
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • Strisovsky, K., Sharpe, H. J., and Freeman, M. (2009) Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates. Mol. Cell 36, 1048-1059
    • (2009) Mol. Cell , vol.36 , pp. 1048-1059
    • Strisovsky, K.1    Sharpe, H.J.2    Freeman, M.3
  • 52
    • 1242288387 scopus 로고    scopus 로고
    • Diverse Substrate Recognition Mechanisms for Rhomboids: Thrombomodulin Is Cleaved by Mammalian Rhomboids
    • DOI 10.1016/S0960-9822(04)00008-9
    • Lohi, O., Urban, S., and Freeman, M. (2004) Diverse substrate recognition mechanisms for rhomboids: thrombomodulin is cleaved by mammalian rhomboids. Curr. Biol. 14, 236-241 (Pubitemid 38215352)
    • (2004) Current Biology , vol.14 , Issue.3 , pp. 236-241
    • Lohi, O.1    Urban, S.2    Freeman, M.3
  • 53
    • 77955085749 scopus 로고    scopus 로고
    • Intramembrane proteolysis of Mgm1 by the mitochondrial rhomboid protease is highly promiscuous regarding the sequence of the cleaved hydrophobic segment
    • Schäfer, A., Zick, M., Kief, J., Steger, M., Heide, H., Duvezin-Caubet, S., Neupert, W., and Reichert, A. S. (2010) Intramembrane proteolysis of Mgm1 by the mitochondrial rhomboid protease is highly promiscuous regarding the sequence of the cleaved hydrophobic segment. J. Mol. Biol. 401, 182-193
    • (2010) J. Mol. Biol. , vol.401 , pp. 182-193
    • Schäfer, A.1    Zick, M.2    Kief, J.3    Steger, M.4    Heide, H.5    Duvezin-Caubet, S.6    Neupert, W.7    Reichert, A.S.8
  • 55
    • 2142710081 scopus 로고    scopus 로고
    • Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
    • DOI 10.1083/jcb.200403022
    • Herlan, M., Bornhövd, C., Hell, K., Neupert, W., and Reichert, A. S. (2004) Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165, 167-173 (Pubitemid 38544519)
    • (2004) Journal of Cell Biology , vol.165 , Issue.2 , pp. 167-173
    • Herlan, M.1    Bornhovd, C.2    Hell, K.3    Neupert, W.4    Reichert, A.S.5
  • 56
    • 73149105938 scopus 로고    scopus 로고
    • Cleavage of a multispanning membrane protein by an intramembrane serine protease
    • Erez, E., and Bibi, E. (2009) Cleavage of a multispanning membrane protein by an intramembrane serine protease. Biochemistry 48, 12314-12322
    • (2009) Biochemistry , vol.48 , pp. 12314-12322
    • Erez, E.1    Bibi, E.2
  • 57
    • 84862064898 scopus 로고    scopus 로고
    • Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis
    • Wan, C., Fu, J., Wang, Y., Miao, S., Song, W., and Wang, L. (2012) Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis. PLoS ONE 7, e37452
    • (2012) PLoS ONE , vol.7
    • Wan, C.1    Fu, J.2    Wang, Y.3    Miao, S.4    Song, W.5    Wang, L.6
  • 58
    • 33846490396 scopus 로고    scopus 로고
    • m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria
    • DOI 10.1038/sj.emboj.7601514, PII 7601514
    • Tatsuta, T., Augustin, S., Nolden, M., Friedrichs, B., and Langer, T. (2007) m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J. 26, 325-335 (Pubitemid 46160934)
    • (2007) EMBO Journal , vol.26 , Issue.2 , pp. 325-335
    • Tatsuta, T.1    Augustin, S.2    Nolden, M.3    Friedrichs, B.4    Langer, T.5
  • 59
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • Baker, R. P., Wijetilaka, R., and Urban, S. (2006) Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria. PLoS Pathog. 2, e113
    • (2006) PLoS Pathog. , vol.2
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 60
    • 33751436135 scopus 로고    scopus 로고
    • Solution Structure and Dynamics of the N-terminal Cytosolic Domain of Rhomboid Intramembrane Protease from Pseudomonas aeruginosa: Insights into a Functional Role in Intramembrane Proteolysis
    • DOI 10.1016/j.jmb.2006.09.047, PII S0022283606012563
    • Del Rio, A., Dutta, K., Chavez, J., Ubarretxena-Belandia, I., and Ghose, R. (2007) Solution structure and dynamics of the N-terminal cytosolic domain of rhomboid intramembrane protease from Pseudomonas aeruginosa: insights into a functional role in intramembrane proteolysis. J. Mol. Biol. 365, 109-122 (Pubitemid 44821200)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.1 , pp. 109-122
    • Del, R.A.1    Dutta, K.2    Chavez, J.3    Ubarretxena-Belandia, I.4    Ghose, R.5
  • 61
    • 71149098713 scopus 로고    scopus 로고
    • Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain
    • Sherratt, A. R., Braganza, M. V., Nguyen, E., Ducat, T., and Goto, N. K. (2009) Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain. Biochim. Biophys. Acta 1788, 2444-2453
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2444-2453
    • Sherratt, A.R.1    Braganza, M.V.2    Nguyen, E.3    Ducat, T.4    Goto, N.K.5
  • 62
    • 84867073516 scopus 로고    scopus 로고
    • Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core
    • Sherratt, A. R., Blais, D. R., Ghasriani, H., Pezacki, J. P., and Goto, N. K. (2012) Activity-based protein profiling of the Escherichia coli GlpG rhomboid protein delineates the catalytic core. Biochemistry 51, 7794-7803
    • (2012) Biochemistry , vol.51 , pp. 7794-7803
    • Sherratt, A.R.1    Blais, D.R.2    Ghasriani, H.3    Pezacki, J.P.4    Goto, N.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.