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Volumn 425, Issue 7, 2013, Pages 1127-1142

Domain swapping in the cytoplasmic domain of the escherichia coli rhomboid protease

Author keywords

enzyme kinetics; GlpG; intramembrane peptidase; intramembrane protease; x ray crystallography

Indexed keywords

MONOMER; PROTEINASE; RHOMBOID; UNCLASSIFIED DRUG;

EID: 84875223117     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.01.019     Document Type: Article
Times cited : (30)

References (61)
  • 1
    • 79951770323 scopus 로고    scopus 로고
    • Rhomboids: 7 years of a new protease family
    • M. Freeman Rhomboids: 7 years of a new protease family Semin. Cell Dev. Biol. 2008
    • (2008) Semin. Cell Dev. Biol.
    • Freeman, M.1
  • 2
    • 80054893675 scopus 로고    scopus 로고
    • The rhomboid protease family: A decade of progress on function and mechanism
    • S. Urban, and S.W. Dickey The rhomboid protease family: a decade of progress on function and mechanism Genome Biol. 12 2011 231
    • (2011) Genome Biol. , vol.12 , pp. 231
    • Urban, S.1    Dickey, S.W.2
  • 3
    • 0025060344 scopus 로고
    • Rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster
    • E. Bier, L.Y. Jan, and Y.N. Jan rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster Genes Dev. 4 1990 190 203
    • (1990) Genes Dev. , vol.4 , pp. 190-203
    • Bier, E.1    Jan, L.Y.2    Jan, Y.N.3
  • 4
    • 34249989074 scopus 로고    scopus 로고
    • The EGFR ligands Spitz and Keren act cooperatively in the Drosophila eye
    • K.E. Brown, M. Kerr, and M. Freeman The EGFR ligands Spitz and Keren act cooperatively in the Drosophila eye Dev. Biol. 307 2007 105 113
    • (2007) Dev. Biol. , vol.307 , pp. 105-113
    • Brown, K.E.1    Kerr, M.2    Freeman, M.3
  • 5
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • S. Cipolat, T. Rudka, D. Hartmann, V. Costa, L. Serneels, and K. Craessaerts Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling Cell 126 2006 163 175
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1    Rudka, T.2    Hartmann, D.3    Costa, V.4    Serneels, L.5    Craessaerts, K.6
  • 7
    • 58149397651 scopus 로고    scopus 로고
    • Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin
    • [discussion 173]
    • A.J. Whitworth, J.R. Lee, V.M. Ho, R. Flick, R. Chowdhury, and G.A. McQuibban Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin Dis. Model. Mech. 1 2008 168 174 [discussion 173]
    • (2008) Dis. Model. Mech. , vol.1 , pp. 168-174
    • Whitworth, A.J.1    Lee, J.R.2    Ho, V.M.3    Flick, R.4    Chowdhury, R.5    McQuibban, G.A.6
  • 8
    • 0033772264 scopus 로고    scopus 로고
    • OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
    • C. Alexander, M. Votruba, U.E. Pesch, D.L. Thiselton, S. Mayer, and A. Moore OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28 Nat. Genet. 26 2000 211 215
    • (2000) Nat. Genet. , vol.26 , pp. 211-215
    • Alexander, C.1    Votruba, M.2    Pesch, U.E.3    Thiselton, D.L.4    Mayer, S.5    Moore, A.6
  • 9
  • 10
    • 59349107213 scopus 로고    scopus 로고
    • The Leu262Val polymorphism of presenilin associated rhomboid like protein (PARL) is associated with earlier onset of type 2 diabetes and increased urinary microalbumin creatinine ratio in an Irish case-control population
    • M. Hatunic, M. Stapleton, E. Hand, C. DeLong, V.E. Crowley, and J.J. Nolan The Leu262Val polymorphism of presenilin associated rhomboid like protein (PARL) is associated with earlier onset of type 2 diabetes and increased urinary microalbumin creatinine ratio in an Irish case-control population Diabetes Res. Clin. Pract. 83 2009 316 319
    • (2009) Diabetes Res. Clin. Pract. , vol.83 , pp. 316-319
    • Hatunic, M.1    Stapleton, M.2    Hand, E.3    Delong, C.4    Crowley, V.E.5    Nolan, J.J.6
  • 11
    • 49849094826 scopus 로고    scopus 로고
    • Human rhomboid family-1 gene silencing causes apoptosis or autophagy to epithelial cancer cells and inhibits xenograft tumor growth
    • Z. Yan, H. Zou, F. Tian, J.R. Grandis, A.J. Mixson, P.Y. Lu, and L.Y. Li Human rhomboid family-1 gene silencing causes apoptosis or autophagy to epithelial cancer cells and inhibits xenograft tumor growth Mol. Cancer Ther. 7 2008 1355 1364
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1355-1364
    • Yan, Z.1    Zou, H.2    Tian, F.3    Grandis, J.R.4    Mixson, A.J.5    Lu, P.Y.6    Li, L.Y.7
  • 12
    • 59649109249 scopus 로고    scopus 로고
    • Human rhomboid family-1 gene RHBDF1 participates in GPCR-mediated transactivation of EGFR growth signals in head and neck squamous cancer cells
    • H. Zou, S.M. Thomas, Z.W. Yan, J.R. Grandis, A. Vogt, and L.Y. Li Human rhomboid family-1 gene RHBDF1 participates in GPCR-mediated transactivation of EGFR growth signals in head and neck squamous cancer cells FASEB J. 23 2009 425 432
    • (2009) FASEB J , vol.23 , pp. 425-432
    • Zou, H.1    Thomas, S.M.2    Yan, Z.W.3    Grandis, J.R.4    Vogt, A.5    Li, L.Y.6
  • 13
    • 15244360655 scopus 로고    scopus 로고
    • A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma
    • F. Brossier, T.J. Jewett, L.D. Sibley, and S. Urban A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma Proc. Natl Acad. Sci. USA 102 2005 4146 4151
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4146-4151
    • Brossier, F.1    Jewett, T.J.2    Sibley, L.D.3    Urban, S.4
  • 14
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • R.P. Baker, R. Wijetilaka, and S. Urban Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria PLoS Pathog. 2 2006 e113
    • (2006) PLoS Pathog. , vol.2 , pp. 113
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 15
    • 2642528789 scopus 로고    scopus 로고
    • Expression of a novel gene, gluP, is essential for normal Bacillus subtilis cell division and contributes to glucose export
    • L.R. Mesak, F.M. Mesak, and M.K. Dahl Expression of a novel gene, gluP, is essential for normal Bacillus subtilis cell division and contributes to glucose export BMC Microbiol. 4 2004 13
    • (2004) BMC Microbiol. , vol.4 , pp. 13
    • Mesak, L.R.1    Mesak, F.M.2    Dahl, M.K.3
  • 16
    • 33846541511 scopus 로고    scopus 로고
    • Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase
    • L.G. Stevenson, K. Strisovsky, K.M. Clemmer, S. Bhatt, M. Freeman, and P.N. Rather Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase Proc. Natl Acad. Sci. USA 104 2007 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
  • 17
    • 0037264371 scopus 로고    scopus 로고
    • The rhomboids: A nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers
    • E.V. Koonin, K.S. Makarova, I.B. Rogozin, L. Davidovic, M.C. Letellier, and L. Pellegrini The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers Genome Biol. 4 2003 R19
    • (2003) Genome Biol. , vol.4 , pp. 19
    • Koonin, E.V.1    Makarova, K.S.2    Rogozin, I.B.3    Davidovic, L.4    Letellier, M.C.5    Pellegrini, L.6
  • 18
    • 35948982252 scopus 로고    scopus 로고
    • Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
    • M.K. Lemberg, and M. Freeman Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases Genome Res. 17 2007 1634 1646
    • (2007) Genome Res. , vol.17 , pp. 1634-1646
    • Lemberg, M.K.1    Freeman, M.2
  • 19
    • 33846543356 scopus 로고    scopus 로고
    • The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
    • M.J. Lemieux, S.J. Fischer, M.M. Cherney, K.S. Bateman, and M.N. James The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis Proc. Natl Acad. Sci. USA 104 2007 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
  • 20
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Y. Wang, Y. Zhang, and Y. Ha Crystal structure of a rhomboid family intramembrane protease Nature 2006 1 5
    • (2006) Nature , pp. 1-5
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 21
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • A. Ben-Shem, D. Fass, and E. Bibi Structural basis for intramembrane proteolysis by rhomboid serine proteases Proc. Natl Acad. Sci. USA 104 2007 462 466
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 462-466
    • Ben-Shem, A.1    Fass, D.2    Bibi, E.3
  • 22
    • 33845365770 scopus 로고    scopus 로고
    • Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry
    • Z. Wu, N. Yan, L. Feng, A. Oberstein, H. Yan, and R.P. Baker Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry Nat. Struct. Mol. Biol. 13 2006 1084 1091
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1084-1091
    • Wu, Z.1    Yan, N.2    Feng, L.3    Oberstein, A.4    Yan, H.5    Baker, R.P.6
  • 23
    • 79952316125 scopus 로고    scopus 로고
    • Structure of rhomboid protease in a lipid environment
    • K.R. Vinothkumar Structure of rhomboid protease in a lipid environment J. Mol. Biol. 407 2011 232 247
    • (2011) J. Mol. Biol. , vol.407 , pp. 232-247
    • Vinothkumar, K.R.1
  • 24
    • 71149098713 scopus 로고    scopus 로고
    • Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain
    • A.R. Sherratt, M.V. Braganza, E. Nguyen, T. Ducat, and N.K. Goto Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain Biochim. Biophys. Acta 1788 2009 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
  • 25
    • 84867073516 scopus 로고    scopus 로고
    • Activity-based protein profiling of the E. coli GlpG rhomboid protein delineates the catalytic core
    • A.R. Sherratt, D.R. Blais, H. Ghasriani, J.P. Pezacki, and N.K. Goto Activity-based protein profiling of the E. coli GlpG rhomboid protein delineates the catalytic core Biochemistry 51 2012 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
  • 26
    • 13844306483 scopus 로고    scopus 로고
    • Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
    • S. Urban, and M.S. Wolfe Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity Proc. Natl Acad. Sci. USA 102 2005 1883 1888
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 1883-1888
    • Urban, S.1    Wolfe, M.S.2
  • 27
    • 14844300797 scopus 로고    scopus 로고
    • Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases
    • M.K. Lemberg, J. Menendez, A. Misik, M. Garcia, C.M. Koth, and M. Freeman Mechanism of intramembrane proteolysis investigated with purified rhomboid proteases EMBO J. 24 2005 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    Freeman, M.6
  • 28
    • 26644441432 scopus 로고    scopus 로고
    • Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane
    • S. Maegawa, K. Ito, and Y. Akiyama Proteolytic action of GlpG, a rhomboid protease in the Escherichia coli cytoplasmic membrane Biochemistry 44 2005 13543 13552
    • (2005) Biochemistry , vol.44 , pp. 13543-13552
    • Maegawa, S.1    Ito, K.2    Akiyama, Y.3
  • 29
    • 0037080869 scopus 로고    scopus 로고
    • Intracellular trafficking by Star regulates cleavage of the Drosophila EGF receptor ligand Spitz
    • R. Tsruya, A. Schlesinger, A. Reich, L. Gabay, A. Sapir, and B.Z. Shilo Intracellular trafficking by Star regulates cleavage of the Drosophila EGF receptor ligand Spitz Genes Dev. 16 2002 222 234
    • (2002) Genes Dev. , vol.16 , pp. 222-234
    • Tsruya, R.1    Schlesinger, A.2    Reich, A.3    Gabay, L.4    Sapir, A.5    Shilo, B.Z.6
  • 30
    • 5644244829 scopus 로고    scopus 로고
    • Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6
    • J. Shen, and R. Prywes Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6 J. Biol. Chem. 279 2004 43046 43051
    • (2004) J. Biol. Chem. , vol.279 , pp. 43046-43051
    • Shen, J.1    Prywes, R.2
  • 31
    • 73149105938 scopus 로고    scopus 로고
    • Cleavage of a multispanning membrane protein by an intramembrane serine protease
    • E. Erez, and E. Bibi Cleavage of a multispanning membrane protein by an intramembrane serine protease Biochemistry 48 2009 12314 12322
    • (2009) Biochemistry , vol.48 , pp. 12314-12322
    • Erez, E.1    Bibi, E.2
  • 32
    • 41849117736 scopus 로고    scopus 로고
    • Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii
    • L. Sheiner, T.J. Dowse, and D. Soldati-Favre Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii Traffic 9 2008 665 677
    • (2008) Traffic , vol.9 , pp. 665-677
    • Sheiner, L.1    Dowse, T.J.2    Soldati-Favre, D.3
  • 33
    • 1242288387 scopus 로고    scopus 로고
    • Diverse substrate recognition mechanisms for rhomboids; Thrombomodulin is cleaved by mammalian rhomboids
    • O. Lohi, S. Urban, and M. Freeman Diverse substrate recognition mechanisms for rhomboids; thrombomodulin is cleaved by mammalian rhomboids Curr. Biol. 14 2004 236 241
    • (2004) Curr. Biol. , vol.14 , pp. 236-241
    • Lohi, O.1    Urban, S.2    Freeman, M.3
  • 34
    • 80855138090 scopus 로고    scopus 로고
    • Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing
    • T.L. Cheng, Y.T. Wu, H.Y. Lin, F.C. Hsu, S.K. Liu, and B.I. Chang Functions of rhomboid family protease RHBDL2 and thrombomodulin in wound healing J. Invest. Dermatol. 131 2011 2486 2494
    • (2011) J. Invest. Dermatol. , vol.131 , pp. 2486-2494
    • Cheng, T.L.1    Wu, Y.T.2    Lin, H.Y.3    Hsu, F.C.4    Liu, S.K.5    Chang, B.I.6
  • 35
    • 84865389259 scopus 로고    scopus 로고
    • Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins
    • L. Fleig, N. Bergbold, P. Sahasrabudhe, B. Geiger, L. Kaltak, and M.K. Lemberg Ubiquitin-dependent intramembrane rhomboid protease promotes ERAD of membrane proteins Mol. Cell 47 2012 558 569
    • (2012) Mol. Cell , vol.47 , pp. 558-569
    • Fleig, L.1    Bergbold, N.2    Sahasrabudhe, P.3    Geiger, B.4    Kaltak, L.5    Lemberg, M.K.6
  • 36
    • 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
    • A. Del Rio, K. Dutta, J. Chavez, I. Ubarretxena-Belandia, and R. Ghose 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 2007 109 122
    • (2007) J. Mol. Biol. , vol.365 , pp. 109-122
    • Del Rio, A.1    Dutta, K.2    Chavez, J.3    Ubarretxena-Belandia, I.4    Ghose, R.5
  • 37
    • 84875226232 scopus 로고    scopus 로고
    • The catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate
    • Y. Xue, and Y. Ha The catalytic mechanism of rhomboid protease GlpG probed by 3,4-dichloroisocoumarin and diisopropyl fluorophosphonate J. Biol. Chem. 51 2012 3723 3731
    • (2012) J. Biol. Chem. , vol.51 , pp. 3723-3731
    • Xue, Y.1    Ha, Y.2
  • 38
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • M.J. Bennett, M.P. Schlunegger, and D. Eisenberg 3D domain swapping: a mechanism for oligomer assembly Protein Sci. 4 1995 2455 2468
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 39
    • 0036429022 scopus 로고    scopus 로고
    • The domain-swapped dimer of cyanovirin-N contains two sets of oligosaccharide binding sites in solution
    • L.G. Barrientos, and A.M. Gronenborn The domain-swapped dimer of cyanovirin-N contains two sets of oligosaccharide binding sites in solution Biochem. Biophys. Res. Commun. 298 2002 598 602
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 598-602
    • Barrientos, L.G.1    Gronenborn, A.M.2
  • 41
    • 0035826713 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues
    • F. Rousseau, J.W. Schymkowitz, H.R. Wilkinson, and L.S. Itzhaki Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues Proc. Natl Acad. Sci. USA 98 2001 5596 5601
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5596-5601
    • Rousseau, F.1    Schymkowitz, J.W.2    Wilkinson, H.R.3    Itzhaki, L.S.4
  • 42
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • M.W. MacArthur, and J.M. Thornton Influence of proline residues on protein conformation J. Mol. Biol. 218 1991 397 412
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • Macarthur, M.W.1    Thornton, J.M.2
  • 43
    • 0037137255 scopus 로고    scopus 로고
    • Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system
    • I. Porcelli, E. de Leeuw, R. Wallis, E. van den Brink-van der Laan, B. de Kruijff, and B.A. Wallace Characterization and membrane assembly of the TatA component of the Escherichia coli twin-arginine protein transport system Biochemistry 41 2002 13690 13697
    • (2002) Biochemistry , vol.41 , pp. 13690-13697
    • Porcelli, I.1    De Leeuw, E.2    Wallis, R.3    Van Den Brink-Van Der Laan, E.4    De Kruijff, B.5    Wallace, B.A.6
  • 44
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • K. Strisovsky, H.J. Sharpe, and M. Freeman Sequence-specific intramembrane proteolysis: identification of a recognition motif in rhomboid substrates Mol. Cell 36 2009 1048 1059
    • (2009) Mol. Cell , vol.36 , pp. 1048-1059
    • Strisovsky, K.1    Sharpe, H.J.2    Freeman, M.3
  • 45
    • 33646255954 scopus 로고    scopus 로고
    • Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii
    • K.M. Clemmer, G.M. Sturgill, A. Veenstra, and P.N. Rather Functional characterization of Escherichia coli GlpG and additional rhomboid proteins using an aarA mutant of Providencia stuartii J. Bacteriol. 188 2006 3415 3419
    • (2006) J. Bacteriol. , vol.188 , pp. 3415-3419
    • Clemmer, K.M.1    Sturgill, G.M.2    Veenstra, A.3    Rather, P.N.4
  • 47
    • 0036427425 scopus 로고    scopus 로고
    • Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain
    • M.J. Lemieux, R.A. Reithmeier, and D.N. Wang Importance of detergent and phospholipid in the crystallization of the human erythrocyte anion-exchanger membrane domain J. Struct. Biol. 137 2002 322 332
    • (2002) J. Struct. Biol. , vol.137 , pp. 322-332
    • Lemieux, M.J.1    Reithmeier, R.A.2    Wang, D.N.3
  • 48
    • 0035913906 scopus 로고    scopus 로고
    • Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila
    • J.R. Lee, S. Urban, C.F. Garvey, and M. Freeman Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila Cell 107 2001 161 171
    • (2001) Cell , vol.107 , pp. 161-171
    • Lee, J.R.1    Urban, S.2    Garvey, C.F.3    Freeman, M.4
  • 49
  • 51
    • 0035127031 scopus 로고    scopus 로고
    • A domain-swapped RNase A dimer with implications for amyloid formation
    • Y. Liu, G. Gotte, M. Libonati, and D. Eisenberg A domain-swapped RNase A dimer with implications for amyloid formation Nat. Struct. Biol. 8 2001 211 214
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 211-214
    • Liu, Y.1    Gotte, G.2    Libonati, M.3    Eisenberg, D.4
  • 53
    • 84863260540 scopus 로고    scopus 로고
    • Domain swapping proceeds via complete unfolding: A 19F- and 1H-NMR study of the Cyanovirin-N protein
    • L. Liu, I.J. Byeon, I. Bahar, and A.M. Gronenborn Domain swapping proceeds via complete unfolding: a 19F- and 1H-NMR study of the Cyanovirin-N protein J. Am. Chem. Soc. 134 2012 4229 4235
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 4229-4235
    • Liu, L.1    Byeon, I.J.2    Bahar, I.3    Gronenborn, A.M.4
  • 54
    • 84864751064 scopus 로고    scopus 로고
    • Multifaceted substrate capture scheme of a rhomboid protease
    • T. Reddy, and J.K. Rainey Multifaceted substrate capture scheme of a rhomboid protease J. Phys. Chem. B 116 2012 8942 8954
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8942-8954
    • Reddy, T.1    Rainey, J.K.2
  • 55
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity.
    • J.R. Casey, and R.A. Reithmeier Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266 1991 15726 15737
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.2
  • 56
    • 0035036495 scopus 로고    scopus 로고
    • Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase
    • C.P. Macol, H. Tsuruta, B. Stec, and E.R. Kantrowitz Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase Nat. Struct. Biol. 8 2001 423 426
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 423-426
    • Macol, C.P.1    Tsuruta, H.2    Stec, B.3    Kantrowitz, E.R.4
  • 57
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • M. Yamasaki, W. Li, D.J. Johnson, and J.A. Huntington Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization Nature 455 2008 1255 1258
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4


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