메뉴 건너뛰기




Volumn 407, Issue 5, 2011, Pages 687-697

Insights into substrate gating in H. influenzae rhomboid

Author keywords

GlpG; intramembrane protease; protein crystallography; rhomboid protease; serine peptidase

Indexed keywords

BACTERIAL ENZYME; HELIX LOOP HELIX PROTEIN; RHOMBOID GLPG; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 79952738921     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.01.046     Document Type: Article
Times cited : (31)

References (48)
  • 1
    • 0035783060 scopus 로고    scopus 로고
    • The MEROPS database as a protease information system
    • Barrett, A. J., Rawlings, N. D. & O'Brien, E. A. (2001). The MEROPS database as a protease information system. J. Struct. Biol. 134, 95-102.
    • (2001) J. Struct. Biol. , vol.134 , pp. 95-102
    • Barrett, A.J.1    Rawlings, N.D.2    O'Brien, E.A.3
  • 2
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
    • Urban, S., Lee, J. R. & 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
  • 3
    • 0025060344 scopus 로고
    • Rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster
    • Bier, E., Jan, L. Y. & Jan, Y. N. (1990). Rhomboid, a gene required for dorsoventral axis establishment and peripheral nervous system development in Drosophila melanogaster. Genes Dev. 4, 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
    • Brown, K. E., Kerr, M. & Freeman, M. (2007). The EGFR ligands Spitz and Keren act cooperatively in the Drosophila eye. Dev. Biol. 307, 105-113.
    • (2007) Dev. Biol. , vol.307 , pp. 105-113
    • Brown, K.E.1    Kerr, M.2    Freeman, M.3
  • 5
    • 1542374120 scopus 로고    scopus 로고
    • Proteolysis within the membrane: Rhomboids revealed
    • Freeman, M. (2004). Proteolysis within the membrane: rhomboids revealed. Nat. Rev. Mol. Cell Biol. 5, 188-197.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 188-197
    • Freeman, M.1
  • 6
    • 0034234250 scopus 로고    scopus 로고
    • A family of rhomboid-like genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signaling
    • Wasserman, J. D., Urban, S. & Freeman, M. (2000). A family of rhomboid-like genes: Drosophila rhomboid-1 and roughoid/rhomboid-3 cooperate to activate EGF receptor signaling. Genes Dev. 14, 1651-1663. (Pubitemid 30460914)
    • (2000) Genes and Development , vol.14 , Issue.13 , pp. 1651-1663
    • Wasserman, J.D.1    Urban, S.2    Freeman, M.3
  • 7
    • 35948982252 scopus 로고    scopus 로고
    • Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases
    • Lemberg, M. K. & Freeman, M. (2007). Functional and evolutionary implications of enhanced genomic analysis of rhomboid intramembrane proteases. Genome Res. 17, 1634-1646.
    • (2007) Genome Res. , vol.17 , pp. 1634-1646
    • Lemberg, M.K.1    Freeman, M.2
  • 8
    • 33846541511 scopus 로고    scopus 로고
    • Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase
    • Stevenson, L. G., Strisovsky, K., Clemmer, K. M., Bhatt, S., Freeman, M. & Rather, P. N. (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
  • 9
    • 15244360655 scopus 로고    scopus 로고
    • A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma
    • Brossier, F., Jewett, T. J., Sibley, L. D. & Urban, S. (2005). A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Proc. Natl Acad. Sci. USA, 102, 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
  • 10
    • 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
  • 12
    • 0026459770 scopus 로고
    • Identifying targets of the rough homeobox gene of Drosophila: Evidence that rhomboid functions in eye development
    • Freeman, M., Kimmel, B. E. & Rubin, G. M. (1992). Identifying targets of the rough homeobox gene of Drosophila: evidence that rhomboid functions in eye development. Development, 116, 335-346.
    • (1992) Development , vol.116 , pp. 335-346
    • Freeman, M.1    Kimmel, B.E.2    Rubin, G.M.3
  • 13
    • 14044266249 scopus 로고    scopus 로고
    • EGF signal propagation during C. elegans vulval development mediated by ROM-1 rhomboid
    • Dutt, A., Canevascini, S., Froehli-Hoier, E. & Hajnal, A. (2004). EGF signal propagation during C. elegans vulval development mediated by ROM-1 rhomboid. PLoS Biol. 2, e334.
    • (2004) PLoS Biol. , vol.2
    • Dutt, A.1    Canevascini, S.2    Froehli-Hoier, E.3    Hajnal, A.4
  • 14
    • 0032563808 scopus 로고    scopus 로고
    • Multiple functions of the EGF receptor in Drosophila eye development
    • Dominguez, M., Wasserman, J. D. & Freeman, M. (1998). Multiple functions of the EGF receptor in Drosophila eye development. Curr. Biol. 8, 1039-1048.
    • (1998) Curr. Biol. , vol.8 , pp. 1039-1048
    • Dominguez, M.1    Wasserman, J.D.2    Freeman, M.3
  • 15
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K. et al. (2006). Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell, 126, 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
  • 16
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza, C., Cipolat, S., Martins de Brito, O., Micaroni, M., Beznoussenko, G. V., Rudka, T. et al. (2006). OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell, 126, 177-189.
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1    Cipolat, S.2    Martins De Brito, O.3    Micaroni, M.4    Beznoussenko, G.V.5    Rudka, T.6
  • 18
    • 20344378241 scopus 로고    scopus 로고
    • Molecular mechanisms of mitochondrial diabetes (MIDD)
    • Maassen, J. A., Janssen, G. M. & t Hart, L. M. (2005). Molecular mechanisms of mitochondrial diabetes (MIDD). Ann. Med. 37, 213-221.
    • (2005) Ann. Med. , vol.37 , pp. 213-221
    • Maassen, J.A.1    Janssen, G.M.2    T Hart, L.M.3
  • 19
    • 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
    • Hatunic, M., Stapleton, M., Hand, E., DeLong, C., Crowley, V. E. & Nolan, J. J. (2009). 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, 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
  • 20
    • 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
    • Whitworth, A. J., Lee, J. R., Ho, V. M., Flick, R., Chowdhury, R. & McQuibban, G. A. (2008). Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin. Dis. Models Mech. 1, 168-174; discussion, 173.
    • (2008) Dis. Models 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
  • 21
    • 0033772264 scopus 로고    scopus 로고
    • OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
    • Alexander, C., Votruba, M., Pesch, U. E., Thiselton, D. L., Mayer, S., Moore, A. et al. (2000). OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat. Genet. 26, 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
  • 22
    • 49849094826 scopus 로고    scopus 로고
    • Human rhomboid family-1 gene silencing causes apoptosis or autophagy to epithelial cancer cells and inhibits xenograft tumor growth
    • Yan, Z., Zou, H., Tian, F., Grandis, J. R., Mixson, A. J., Lu, P. Y. & Li, L. Y. (2008). Human rhomboid family-1 gene silencing causes apoptosis or autophagy to epithelial cancer cells and inhibits xenograft tumor growth. Mol. Cancer Ther. 7, 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
  • 23
    • 79952739755 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
    • Zou, H., Thomas, S. M., Yan, Z. W., Grandis, J. R., Vogt, A. & Li, L. Y. (2008). Human rhomboid family-1 gene RHBDF1 participates in GPCR-mediated transactivation of EGFR growth signals in head and neck squamous cancer cells. FASEB J.
    • (2008) FASEB J.
    • Zou, H.1    Thomas, S.M.2    Yan, Z.W.3    Grandis, J.R.4    Vogt, A.5    Li, L.Y.6
  • 24
    • 33846543356 scopus 로고    scopus 로고
    • The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis
    • Lemieux, M. J., Fischer, S. J., Cherney, M. M., Bateman, K. S. & James, M. N. (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
  • 25
    • 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
  • 26
    • 33846275257 scopus 로고    scopus 로고
    • Structural basis for intramembrane proteolysis by rhomboid serine proteases
    • Ben-Shem, A., Fass, D. & Bibi, E. (2007). Structural basis for intramembrane 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
  • 27
    • 33845365770 scopus 로고    scopus 로고
    • Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry
    • Wu, Z., Yan, N., Feng, L., Oberstein, A., Yan, H., Baker, R. P. et al. (2006). Structural analysis of a rhomboid family intramembrane protease reveals a gating mechanism for substrate entry. Nat. Struct. Mol. Biol. 13, 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
  • 28
    • 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, 1-5.
    • (2006) Nature , pp. 1-5
    • Wang, Y.1    Zhang, Y.2    Ha, Y.3
  • 29
    • 33646489776 scopus 로고    scopus 로고
    • Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates
    • Radisky, E. S., Lee, J. M., Lu, C. J. & Koshland, D. E., Jr. (2006). Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc. Natl Acad. Sci. USA, 103, 6835-6840.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6835-6840
    • Radisky, E.S.1    Lee, J.M.2    Lu, C.J.3    Koshland Jr., D.E.4
  • 30
    • 34347250499 scopus 로고    scopus 로고
    • Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate
    • Baker, R. P., Young, K., Feng, L., Shi, Y. & Urban, S. (2007). Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane 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
  • 32
    • 79952738760 scopus 로고    scopus 로고
    • Structural comparison of substrate entry gate for rhomboid intramembrane peptidases
    • in press
    • Lazareno-Saez, C., Brooks, C. & Lemieux, M. (2010). Structural comparison of substrate entry gate for rhomboid intramembrane peptidases. Biochem. Cell Biol, in press.
    • (2010) Biochem. Cell Biol
    • Lazareno-Saez, C.1    Brooks, C.2    Lemieux, M.3
  • 33
    • 0343819757 scopus 로고    scopus 로고
    • Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state
    • Li, Y. M., Lai, M. T., Xu, M., Huang, Q., DiMuzio-Mower, J., Sardana, M. K. et al. (2000). Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state. Proc. Natl Acad. Sci. USA, 97, 6138-6143.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6138-6143
    • Li, Y.M.1    Lai, M.T.2    Xu, M.3    Huang, Q.4    DiMuzio-Mower, J.5    Sardana, M.K.6
  • 34
    • 72149124813 scopus 로고    scopus 로고
    • Sequence-specific intramembrane proteolysis: Identification of a recognition motif in rhomboid substrates
    • Strisovsky, K., Sharpe, H. J. & 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
  • 35
    • 13844306483 scopus 로고    scopus 로고
    • Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity
    • Urban, S. & Wolfe, M. S. (2005). Reconstitution of intramembrane proteolysis 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
  • 36
    • 61549125968 scopus 로고    scopus 로고
    • Rhomboid protease dynamics and lipid interactions
    • Bondar, A. N., del Val, C. & 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
  • 37
    • 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
  • 38
    • 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. & 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
  • 39
    • 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. & 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
  • 40
    • 73149105938 scopus 로고    scopus 로고
    • Cleavage of a multispanning membrane protein by an intramembrane serine protease
    • Erez, E. & 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
  • 41
    • 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
  • 42
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal peptidase in complex with a beta- Lactam inhibitor
    • DOI 10.1038/24196
    • Paetzel, M., Dalbey, R. E. & Strynadka, N. C. (1998). Crystal structure of a bacterial signal peptidase in complex with a beta-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
  • 43
    • 10744225162 scopus 로고    scopus 로고
    • The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site
    • Botos, I., Melnikov, E. E., Cherry, S., Tropea, J. E., Khalatova, A. G., Rasulova, F. et al. (2004). The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site. J. Biol. Chem. 279, 8140-8148.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8140-8148
    • Botos, I.1    Melnikov, E.E.2    Cherry, S.3    Tropea, J.E.4    Khalatova, A.G.5    Rasulova, F.6
  • 45
    • 33745041491 scopus 로고    scopus 로고
    • Crystal structure of a novel viral protease with a serine/lysine catalytic dyad mechanism
    • Feldman, A. R., Lee, J., Delmas, B. & Paetzel, M. (2006). Crystal structure of a novel viral protease with a serine/lysine catalytic dyad mechanism. J. Mol. Biol. 358, 1378-1389.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1378-1389
    • Feldman, A.R.1    Lee, J.2    Delmas, B.3    Paetzel, M.4
  • 46
    • 0001109389 scopus 로고
    • Stereochemistry of reaction paths at carbonyl centers
    • Burgi, H. B. & Dunitz, J. D. (1974). Stereochemistry of reaction paths at carbonyl centers. Tetrahedron, 30, 1563-1572.
    • (1974) Tetrahedron , vol.30 , pp. 1563-1572
    • Burgi, H.B.1    Dunitz, J.D.2
  • 47
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. (1997). MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 48
    • 41849117736 scopus 로고    scopus 로고
    • Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii
    • DOI 10.1111/j.1600-0854.2008.00736.x
    • Sheiner, L., Dowse, T. J. & Soldati-Favre, D. (2008). Identification of trafficking determinants for polytopic rhomboid proteases in Toxoplasma gondii. Traffic, 9, 665-677. (Pubitemid 351494299)
    • (2008) Traffic , vol.9 , Issue.5 , pp. 665-677
    • Sheiner, L.1    Dowse, T.J.2    Soldati-Favre, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.