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Volumn 29, Issue 22, 2010, Pages 3797-3809

The structural basis for catalysis and substrate specificity of a rhomboid protease

Author keywords

intramembrane protease; isocoumarin; rhomboid; serine protease; substrate specificity

Indexed keywords

PROTEINASE; RHOMBOID PROTEINASE; UNCLASSIFIED DRUG;

EID: 78449268297     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2010.243     Document Type: Article
Times cited : (95)

References (70)
  • 2
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • Baker RP, Wijetilaka R, 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
  • 3
    • 34347250499 scopus 로고    scopus 로고
    • Enzymatic analysis of a rhomboid intramembrane protease implicates trans-membrane helix 5 as the lateral substrate gate
    • Baker RP, Young K, Feng L, Shi Y, Urban S (2007) Enzymatic analysis of a rhomboid intramembrane protease implicates trans-membrane helix 5 as the lateral substrate gate. Proc Natl Acad Sci USA 104: 8257-8262
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8257-8262
    • Baker, R.P.1    Young, K.2    Feng, L.3    Shi, Y.4    Urban, S.5
  • 4
    • 45349108992 scopus 로고    scopus 로고
    • An Entamoeba histolytica rhomboid protease with atypical specificity cleaves a surface lectin involved in phagocytosis and immune evasion
    • Baxt LA, Baker RP, Singh U, Urban S (2008) An Entamoeba histolytica rhomboid protease with atypical specificity cleaves a surface lectin involved in phagocytosis and immune evasion. Genes Dev 22: 1636-1646
    • (2008) Genes Dev , vol.22 , pp. 1636-1646
    • Baxt, L.A.1    Baker, R.P.2    Singh, U.3    Urban, S.4
  • 5
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramem-brane proteolysis by rhomboid serine proteases
    • Ben-Shem A, Fass D, Bibi E (2007) Structural basis for intramem-brane proteolysis by rhomboid serine proteases. Proc Natl Acad Sci USA 104: 462-466
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 6
    • 84987278622 scopus 로고
    • Structure and Substrate Specificity in the serine enzymes
    • Blow D (1974) Structure and Substrate Specificity in the serine enzymes. Isr J Chem 12: 483-494
    • (1974) Isr J Chem , vol.12 , pp. 483-494
    • Blow, D.1
  • 7
    • 0024571818 scopus 로고
    • Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors
    • Bode W, Meyer Jr E, Powers JC (1989) Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors. Biochemistry 28: 1951-1963
    • (1989) Biochemistry , vol.28 , pp. 1951-1963
    • Bode, W.1    Meyer Jr., E.2    Powers, J.C.3
  • 8
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • Bondar AN, del Val C, White SH (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
  • 10
    • 0034691249 scopus 로고    scopus 로고
    • Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type i signal peptidase
    • Carlos JL, Klenotic PA, Paetzel M, Strynadka NC, Dalbey RE (2000) Mutational evidence of transition state stabilization by serine 88 in Escherichia coli type I signal peptidase. Biochemistry 39: 7276-7283
    • (2000) Biochemistry , vol.39 , pp. 7276-7283
    • Carlos, J.L.1    Klenotic, P.A.2    Paetzel, M.3    Strynadka, N.C.4    Dalbey, R.E.5
  • 11
    • 0025048045 scopus 로고
    • The 2.2 Aresolution X-ray crystal structure of the complex of trypsin inhibited by 4-chloro-3-ethoxy-7-guanidinoisocoumarin: A proposed model of the thrombin-inhibitor complex
    • Chow MM, Meyer Jr EF, Bode W, Kam CM, Radhakrishnan R, Vijayalakshmi J, Powers JC (1990) The 2.2 Aresolution X-ray crystal structure of the complex of trypsin inhibited by 4-chloro-3-ethoxy-7-guanidinoisocoumarin: a proposed model of the thrombin-inhibitor complex. J Am Chem Soc 112: 7783-7789
    • (1990) J Am Chem Soc , vol.112 , pp. 7783-7789
    • Chow, M.M.1    Meyer Jr., E.F.2    Bode, W.3    Kam, C.M.4    Radhakrishnan, R.5    Vijayalakshmi, J.6    Powers, J.C.7
  • 15
    • 56749154097 scopus 로고    scopus 로고
    • Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration
    • Ekici OD, Paetzel M, Dalbey RE (2008) Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration. Protein Sci 17: 2023-2037
    • (2008) Protein Sci , vol.17 , pp. 2023-2037
    • Ekici, O.D.1    Paetzel, M.2    Dalbey, R.E.3
  • 16
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60 (Part 12, Part 1): 2126-2132
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 AND PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 17
    • 33644875355 scopus 로고    scopus 로고
    • Scaling and assessment of data quality
    • Evans P (2006) Scaling and assessment of data quality. Acta Crystallogr D Biol Crystallogr 62(Part 1): 72-82
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.PART 1 , pp. 72-82
    • Evans, P.1
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0022271601 scopus 로고
    • Reaction of serine proteases with substituted isocoumarins: Discovery of 3,4-dichloroisocou-marin, a new general mechanism based serine protease inhibitor
    • Harper JW, Hemmi K, Powers JC (1985) Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocou-marin, a new general mechanism based serine protease inhibitor. Biochemistry 24: 1831-1841
    • (1985) Biochemistry , vol.24 , pp. 1831-1841
    • Harper, J.W.1    Hemmi, K.2    Powers, J.C.3
  • 21
    • 36949069459 scopus 로고
    • Inhibition of chymotrypsin by diethyl p-nitrophenyl phosphate
    • Hartley BS, Kilby BA (1950) Inhibition of chymotrypsin by diethyl p-nitrophenyl phosphate. Nature 166: 784-785
    • (1950) Nature , vol.166 , pp. 784-785
    • Hartley, B.S.1    Kilby, B.A.2
  • 23
    • 0014945734 scopus 로고
    • Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzyme
    • Henderson R (1970) Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J Mol Biol 54: 341-354
    • (1970) J Mol Biol , vol.54 , pp. 341-354
    • Henderson, R.1
  • 24
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan M, Vogel F, Bornhovd C, Neupert W, Reichert AS (2003) Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J Biol Chem 278: 27781-27788
    • (2003) J Biol Chem , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 26
    • 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 EV, Makarova KS, Rogozin IB, Davidovic L, Letellier MC, 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
  • 27
    • 0035913906 scopus 로고    scopus 로고
    • Regulated intracel-lular ligand transport and proteolysis control EGF signal activation in Drosophila
    • Lee JR, Urban S, Garvey CF, Freeman M (2001) Regulated intracel-lular ligand transport and proteolysis control EGF signal activation in Drosophila. Cell 107: 161-171
    • (2001) Cell , vol.107 , pp. 161-171
    • Lee, J.R.1    Urban, S.2    Garvey, C.F.3    Freeman, M.4
  • 28
    • 35748982195 scopus 로고    scopus 로고
    • Cutting proteins within lipid bilayers: Rhomboid structure and mechanism
    • Freeman M
    • Lemberg MK, Freeman M (2007a) Cutting proteins within lipid bilayers: rhomboid structure and mechanism. Mol Cell 28: 930-940
    • (2007) Mol Cell , vol.28 , pp. 930-940
    • Lemberg, M.K.1
  • 29
    • 35948982252 scopus 로고    scopus 로고
    • Functional and evolutionary implications of enhanced genomic analysis of rhomboid intra-membrane proteases
    • Freeman M
    • Lemberg MK, Freeman M (2007b) Functional and evolutionary implications of enhanced genomic analysis of rhomboid intra-membrane proteases. Genome Res 17: 1634-1646
    • (2007) Genome Res , vol.17 , pp. 1634-1646
    • Lemberg, M.K.1
  • 30
    • 14844300797 scopus 로고    scopus 로고
    • Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
    • Freeman M
    • Lemberg MK, Menendez J, Misik A, Garcia M, Koth CM, Freeman M (2005) Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases. EMBO J 24: 464-472
    • (2005) EMBO J , vol.24 , pp. 464-472
    • Lemberg, M.K.1    Menendez, J.2    Misik, A.3    Garcia, M.4    Koth, C.M.5
  • 31
    • 33846543356 scopus 로고    scopus 로고
    • The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
    • Lemieux MJ, Fischer SJ, Cherney MM, Bateman KS, James MN (2007) The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis. Proc Natl Acad Sci USA 104: 750-754
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 750-754
    • Lemieux, M.J.1    Fischer, S.J.2    Cherney, M.M.3    Bateman, K.S.4    James, M.N.5
  • 32
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie AG (2006) The integration of macromolecular diffraction data. Acta Crystallogr D Biol Crystallogr 62(Part 1): 48-57
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.PART 1 , pp. 48-57
    • Leslie, A.G.1
  • 33
    • 1242288387 scopus 로고    scopus 로고
    • Diverse substrate recognition mechanisms for rhomboids; Thrombomodulin is cleaved by mammalian rhomboids
    • Lohi O, Urban S, Freeman M (2004) Diverse substrate recognition mechanisms for rhomboids; thrombomodulin is cleaved by mammalian rhomboids. Curr Biol 14: 236-241
    • (2004) Curr Biol , vol.14 , pp. 236-241
    • Lohi, O.1    Urban, S.2    Freeman, M.3
  • 34
    • 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
    • Maegawa S, Koide K, Ito K, 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
    • (2007) Mol Microbiol , vol.64 , pp. 435-447
    • Maegawa, S.1    Koide, K.2    Ito, K.3    Akiyama, Y.4
  • 36
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban GA, Saurya S, Freeman M (2003) Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423: 537-541
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 37
    • 0001522448 scopus 로고
    • Steresospecific reaction of 3-methoxy-4-chloro-7-aminoisocoumarin with crystalline porcine pancreatic elastase
    • Meyer Jr EF, Presta LG, Radhakrishnan R (1985) Steresospecific reaction of 3-methoxy-4-chloro-7-aminoisocoumarin with crystalline porcine pancreatic elastase. J Am Chem Soc 107: 4091-4093
    • (1985) J Am Chem Soc , vol.107 , pp. 4091-4093
    • Meyer Jr., E.F.1    Presta, L.G.2    Radhakrishnan, R.3
  • 38
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B, Walker JE (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J Mol Biol 260: 289-298
    • (1996) J Mol Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 39
    • 0014030459 scopus 로고
    • Structural specificity of alpha-chymotrypsin: Polypeptide substrates
    • Neil GL, Niemann C, Hein GE (1966) Structural specificity of alpha-chymotrypsin: polypeptide substrates. Nature 210: 903-907
    • (1966) Nature , vol.210 , pp. 903-907
    • Neil, G.L.1    Niemann, C.2    Hein, G.E.3
  • 41
    • 0037007235 scopus 로고    scopus 로고
    • Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii
    • Opitz C, Di Cristina M, Reiss M, Ruppert T, Crisanti A, Soldati D (2002) Intramembrane cleavage of microneme proteins at the surface of the apicomplexan parasite Toxoplasma gondii. EMBO J 21: 1577-1585
    • (2002) EMBO J , vol.21 , pp. 1577-1585
    • Opitz, C.1    Di Cristina, M.2    Reiss, M.3    Ruppert, T.4    Crisanti, A.5    Soldati, D.6
  • 42
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona JJ, Craik CS (1995) Structural basis of substrate specificity in the serine proteases. Protein Sci 4: 337-360
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 43
    • 27144523783 scopus 로고    scopus 로고
    • The catalytic triad of serine peptidases
    • Polgar L (2005) The catalytic triad of serine peptidases. Cell Mol Life Sci 62: 2161-2172
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2161-2172
    • Polgar, L.1
  • 44
    • 0033212804 scopus 로고    scopus 로고
    • The Rossmann Fourier autoindexing algorithm in MOSFLM
    • Powell HR (1999) The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr D Biol Crystallogr 55 (Part 10): 1690-1695
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , Issue.PART 10 , pp. 1690-1695
    • Powell, H.R.1
  • 45
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers JC, Asgian JL, Ekici OD, James KE (2002) Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem Rev 102: 4639-4750
    • (2002) Chem Rev , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 46
    • 0025265667 scopus 로고
    • Reaction of porcine pancreatic elastase with 7-substituted 3-alkoxy-4-chloroisocoumarins: Design of potent inhibitors using the crystal structure of the complex formed with 4-chloro-3-ethoxy-7-guani-dinoisocoumarin
    • Powers JC, Oleksyszyn J, Narasimhan SL, Kam CM (1990) Reaction of porcine pancreatic elastase with 7-substituted 3-alkoxy-4-chloroisocoumarins: design of potent inhibitors using the crystal structure of the complex formed with 4-chloro-3-ethoxy-7-guani-dinoisocoumarin. Biochemistry 29: 3108-3118
    • (1990) Biochemistry , vol.29 , pp. 3108-3118
    • Powers, J.C.1    Oleksyszyn, J.2    Narasimhan, S.L.3    Kam, C.M.4
  • 47
    • 0032561323 scopus 로고    scopus 로고
    • Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1
    • Rawson RB, Cheng D, Brown MS, Goldstein JL (1998) Isolation of cholesterol-requiring mutant Chinese hamster ovary cells with defects in cleavage of sterol regulatory element-binding proteins at site 1. J Biol Chem 273: 28261-28269
    • (1998) J Biol Chem , vol.273 , pp. 28261-28269
    • Rawson, R.B.1    Cheng, D.2    Brown, M.S.3    Goldstein, J.L.4
  • 48
    • 0015497445 scopus 로고
    • Subtilisin; A stereochemical mechanism involving transition-state stabilization
    • Robertus JD, Kraut J, Alden RA, Birktoft JJ (1972) Subtilisin; a stereochemical mechanism involving transition-state stabilization. Biochemistry 11 : 4293-4303
    • (1972) Biochemistry , vol.11 , pp. 4293-4303
    • Robertus, J.D.1    Kraut, J.2    Alden, R.A.3    Birktoft, J.J.4
  • 49
    • 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
    • Schafer A, Zick M, Kief J, Steger M, Heide H, Duvezin-Caubet S, Neupert W, Reichert AS (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
    • Schafer, 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
  • 50
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I, Berger A (1967) On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27: 157-162
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 51
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, van Aalten DM (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 60(Part 8): 1355-1363
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 8 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 52
    • 33846541511 scopus 로고    scopus 로고
    • Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase
    • Stevenson LG, Strisovsky K, Clemmer KM, Bhatt S, Freeman M, Rather PN (2007) Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase. Proc Natl Acad Sci USA 104: 1003-1008
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1003-1008
    • Stevenson, L.G.1    Strisovsky, K.2    Clemmer, K.M.3    Bhatt, S.4    Freeman, M.5    Rather, P.N.6
  • 53
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • Strisovsky K, Sharpe HJ, 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
  • 54
    • 33846490396 scopus 로고    scopus 로고
    • M-AAA protease-driven membrane dislocation allows intramem-brane cleavage by rhomboid in mitochondria
    • Tatsuta T, Augustin S, Nolden M, Friedrichs B, Langer T (2007) m-AAA protease-driven membrane dislocation allows intramem-brane cleavage by rhomboid in mitochondria. EMBO J 26: 325-335
    • (2007) EMBO J , vol.26 , pp. 325-335
    • Tatsuta, T.1    Augustin, S.2    Nolden, M.3    Friedrichs, B.4    Langer, T.5
  • 55
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography (1994) Acta Crystallogr D Biol Crystallogr 50(Part 5): 760-763
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , Issue.PART 5 , pp. 760-763
  • 56
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: Successes, failures and future prospects
    • Turk B (2006) Targeting proteases: successes, failures and future prospects. Nat Rev Drug Discov 5: 785-799
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 785-799
    • Turk, B.1
  • 57
    • 17244364283 scopus 로고    scopus 로고
    • Proteases universally recognize beta strands in their active sites
    • Tyndall JD, Nall T, Fairlie DP (2005) Proteases universally recognize beta strands in their active sites. Chem Rev 105: 973-999
    • (2005) Chem Rev , vol.105 , pp. 973-999
    • Tyndall, J.D.1    Nall, T.2    Fairlie, D.P.3
  • 58
    • 74349127184 scopus 로고    scopus 로고
    • Taking the plunge: Integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis
    • Urban S (2009) Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis. Biochem J 425: 501-512
    • (2009) Biochem J , vol.425 , pp. 501-512
    • Urban, S.1
  • 59
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • Urban S, 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
    • (2003) Mol Cell , vol.11 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 60
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
    • Urban S, Lee JR, Freeman M (2001) Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107 : 173-182
    • (2001) Cell , vol.107 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 61
    • 0037015265 scopus 로고    scopus 로고
    • Conservation of intramem-brane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids
    • Urban S, Schlieper D, Freeman M (2002) Conservation of intramem-brane proteolytic activity and substrate specificity in prokaryotic and eukaryotic rhomboids. Curr Biol 12: 1507-1512
    • (2002) Curr Biol , vol.12 , pp. 1507-1512
    • Urban, S.1    Schlieper, D.2    Freeman, M.3
  • 62
    • 13844306483 scopus 로고    scopus 로고
    • Reconstitution of intramembrane pro-teolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
    • Urban S, Wolfe MS (2005) Reconstitution of intramembrane pro-teolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc Natl Acad Sci USA 102: 1883-1888
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1883-1888
    • Urban, S.1    Wolfe, M.S.2
  • 63
    • 0025980157 scopus 로고
    • Structural study of porcine pancreatic elastase complexed with 7-amino-3-(2-bromoethoxy)-4-chloroisocoumarin as a nonreactivatable doubly covalent enzyme-inhibitor complex
    • Vijayalakshmi J, Meyer Jr EF, Kam CM, Powers JC (1991) Structural study of porcine pancreatic elastase complexed with 7-amino-3-(2-bromoethoxy)-4- chloroisocoumarin as a nonreactivatable doubly covalent enzyme-inhibitor complex. Biochemistry 30: 2175-2183
    • (1991) Biochemistry , vol.30 , pp. 2175-2183
    • Vijayalakshmi, J.1    Meyer Jr., E.F.2    Kam, C.M.3    Powers, J.C.4
  • 64
    • 33847793631 scopus 로고    scopus 로고
    • Open-cap conformation of intramembrane protease GlpG
    • Wang Y, Ha Y (2007) Open-cap conformation of intramembrane protease GlpG. Proc Natl Acad Sci USA 104: 2098-2102
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2098-2102
    • Wang, Y.1    Ha, Y.2
  • 65
    • 35748974498 scopus 로고    scopus 로고
    • The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG
    • Wang Y, Maegawa S, Akiyama Y, Ha Y (2007) The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG. J Mol Biol 374: 1104-1113
    • (2007) J Mol Biol , vol.374 , pp. 1104-1113
    • Wang, Y.1    Maegawa, S.2    Akiyama, Y.3    Ha, Y.4
  • 66
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang Y, Zhang Y, 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
  • 67
    • 0034234250 scopus 로고    scopus 로고
    • A family of rhomboidlike genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signaling
    • Wasserman JD, Urban S, Freeman M (2000) A family of rhomboidlike genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signaling. Genes Dev 14: 1651-1663
    • (2000) Genes Dev , vol.14 , pp. 1651-1663
    • Wasserman, J.D.1    Urban, S.2    Freeman, M.3
  • 68
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspar-tic protease
    • Weihofen A, Binns K, Lemberg MK, Ashman K, Martoglio B (2002) Identification of signal peptide peptidase, a presenilin-type aspar-tic protease. Science 296: 2215-2218
    • (2002) Science , vol.296 , pp. 2215-2218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 69
    • 4143084775 scopus 로고    scopus 로고
    • Intramembrane proteolysis: Theme and variations
    • Wolfe MS, Kopan R (2004) Intramembrane proteolysis: theme and variations. Science 305: 1119-1123
    • (2004) Science , vol.305 , pp. 1119-1123
    • Wolfe, M.S.1    Kopan, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.