메뉴 건너뛰기




Volumn 11, Issue 1, 2011, Pages

Molecular adaptation of a plant-bacterium outer membrane protease towards plague virulence factor Pla

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTATION; AMINO ACID; BACTERIUM; ENZYME ACTIVITY; GENE TRANSFER; INHIBITOR; LIFESTYLE; MEMBRANE; PATHOTYPE; VIRULENCE;

EID: 79751531758     PISSN: None     EISSN: 14712148     Source Type: Journal    
DOI: 10.1186/1471-2148-11-43     Document Type: Article
Times cited : (9)

References (52)
  • 3
    • 0033758756 scopus 로고    scopus 로고
    • Pathogenicity islands and the evolution of microbes
    • 10.1146/annurev.micro.54.1.641. 11018140
    • Pathogenicity islands and the evolution of microbes. J Hacker JB Kaper, Annual Review of Microbiology 2000 54 641 679 10.1146/annurev.micro.54.1.641 11018140
    • (2000) Annual Review of Microbiology , vol.54 , pp. 641-679
    • Hacker, J.1    Kaper, J.B.2
  • 4
    • 48149101623 scopus 로고    scopus 로고
    • Common themes and variations in serine protease autotransporters
    • 10.1016/j.tim.2008.05.003. 18595714
    • Common themes and variations in serine protease autotransporters. YT Yen M Kostakioti IR Henderson C Stathopoulos, Trends Microbiol 2008 16 8 370 379 10.1016/j.tim.2008.05.003 18595714
    • (2008) Trends Microbiol , vol.16 , Issue.8 , pp. 370-379
    • Yen, Y.T.1    Kostakioti, M.2    Henderson, I.R.3    Stathopoulos, C.4
  • 5
  • 6
    • 0033598784 scopus 로고    scopus 로고
    • Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis
    • 10.1073/pnas.96.24.14043. 10570195
    • Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis. M Achtman K Aurth G Morelli G Torrea A Guiyoule E Carniel, Proc Natl Acad Sci USA 1999 96 24 14043 14048 10.1073/pnas.96.24.14043 10570195
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.24 , pp. 14043-14048
    • Achtman, M.1    Aurth, K.2    Morelli, G.3    Torrea, G.4    Guiyoule, A.5    Carniel, E.6
  • 8
    • 0026488402 scopus 로고
    • A surface protease and the invasive character of plague
    • 10.1126/science.1439793. 1439793
    • A surface protease and the invasive character of plague. OA Sodeinde YV Subrahmanyam K Stark T Quan Y Bao JD Goguen, Science 1992 258 5084 1004 1007 10.1126/science.1439793 1439793
    • (1992) Science , vol.258 , Issue.5084 , pp. 1004-1007
    • Sodeinde, O.A.1    Subrahmanyam, Y.V.2    Stark, K.3    Quan, T.4    Bao, Y.5    Goguen, J.D.6
  • 9
    • 1342292545 scopus 로고    scopus 로고
    • The yersiniae - A model genus to study the rapid evolution of bacterial pathogens
    • 10.1038/nrmicro730. 15040180
    • The yersiniae - a model genus to study the rapid evolution of bacterial pathogens. BW Wren, Nat Rev Microbiol 2003 1 1 55 64 10.1038/nrmicro730 15040180
    • (2003) Nat Rev Microbiol , vol.1 , Issue.1 , pp. 55-64
    • Wren, B.W.1
  • 10
    • 33645788354 scopus 로고    scopus 로고
    • Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague
    • 10.1073/pnas.0509544103. 16567636
    • Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague. F Sebbane CO Jarrett D Gardner D Long BJ Hinnebusch, Proc Natl Acad Sci USA 2006 103 14 5526 5530 10.1073/pnas.0509544103 16567636
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.14 , pp. 5526-5530
    • Sebbane, F.1    Jarrett, C.O.2    Gardner, D.3    Long, D.4    Hinnebusch, B.J.5
  • 12
    • 33846645905 scopus 로고    scopus 로고
    • A plasminogen-activating protease specifically controls the development of primary pneumonic plague
    • DOI 10.1126/science.1137195
    • A plasminogen-activating protease specifically controls the development of primary pneumonic plague. WW Lathem PA Price VL Miller WE Goldman, Science 2007 315 5811 509 513 10.1126/science.1137195 17255510 (Pubitemid 46175753)
    • (2007) Science , vol.315 , Issue.5811 , pp. 509-513
    • Lathem, W.W.1    Price, P.A.2    Miller, V.L.3    Goldman, W.E.4
  • 14
    • 34548067653 scopus 로고    scopus 로고
    • Omptin proteins: An expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae (Review)
    • DOI 10.1080/09687680701443822, PII 779507806
    • Omptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae. V Hritonenko C Stathopoulos, Mol Membr Biol 2007 24 5-6 395 406 10.1080/09687680701443822 17710644 (Pubitemid 47290682)
    • (2007) Molecular Membrane Biology , vol.24 , Issue.5-6 , pp. 395-406
    • Hritonenko, V.1    Stathopoulos, C.2
  • 15
    • 63349105215 scopus 로고    scopus 로고
    • Breaking barriers - Attack on innate immune defences by omptin surface proteases of enterobacterial pathogens
    • 10.1177/1753425909102559. 19318417
    • Breaking barriers - attack on innate immune defences by omptin surface proteases of enterobacterial pathogens. J Haiko M Suomalainen T Ojala K Lähteenmäki TK Korhonen, Innate Immunity 2009 15 2 67 80 10.1177/1753425909102559 19318417
    • (2009) Innate Immunity , vol.15 , Issue.2 , pp. 67-80
    • Haiko, J.1    Suomalainen, M.2    Ojala, T.3    Lähteenmäki, K.4    Korhonen, T.K.5
  • 16
    • 77956520647 scopus 로고    scopus 로고
    • The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1
    • 10.1128/JB.00458-10. 20639337
    • The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1. J Haiko L Laakkonen K Juuti N Kalkkinen TK Korhonen, J Bacteriol 2010 192 4553 4561 10.1128/JB.00458-10 20639337
    • (2010) J Bacteriol , vol.192 , pp. 4553-4561
    • Haiko, J.1    Laakkonen, L.2    Juuti, K.3    Kalkkinen, N.4    Korhonen, T.K.5
  • 17
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease Ompt from Escherichia coli suggests a novel catalytic site
    • DOI 10.1093/emboj/20.18.5033
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. L Vandeputte-Rutten RA Kramer J Kroon N Dekker MR Egmond P Gros, EMBO J 2001 20 18 5033 5039 10.1093/emboj/20.18.5033 11566868 (Pubitemid 32910899)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 18
    • 77954630978 scopus 로고    scopus 로고
    • An active site water network in the plasminogen activator Pla from Yersinia pestis
    • 10.1016/j.str.2010.03.013. 20637417
    • An active site water network in the plasminogen activator Pla from Yersinia pestis. E Eren M Murphy J Goguen B van den Berg, Structure 2010 18 7 809 818 10.1016/j.str.2010.03.013 20637417
    • (2010) Structure , vol.18 , Issue.7 , pp. 809-818
    • Eren, E.1    Murphy, M.2    Goguen, J.3    Van Den Berg, B.4
  • 19
    • 0034968724 scopus 로고    scopus 로고
    • 2-antiplasmin in the surface protease Pla of Yersinia pestis
    • DOI 10.1046/j.1365-2958.2001.02451.x
    • Protein regions important for plasminogen activation and inactivation of alpha2-antiplasmin in the surface protease Pla of Yersinia pestis. M Kukkonen K Lähteenmäki M Suomalainen N Kalkkinen L Emödy H Lång TK Korhonen, Mol Microbiol 2001 40 5 1097 1111 10.1046/j.1365-2958.2001.02451.x 11401715 (Pubitemid 32574978)
    • (2001) Molecular Microbiology , vol.40 , Issue.5 , pp. 1097-1111
    • Kukkonen, M.1    Lahteenmaki, K.2    Suomalainen, M.3    Kalkkinen, N.4    Emody, L.5    Lang, H.6    Korhonen, T.K.7
  • 20
    • 0035852860 scopus 로고    scopus 로고
    • Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries
    • DOI 10.1021/bi0014195
    • Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries. N Dekker RC Cox RA Kramer MR Egmond, Biochemistry 2001 40 6 1694 1701 10.1021/bi0014195 11327829 (Pubitemid 32144039)
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1694-1701
    • Dekker, N.1    Cox, R.C.2    Kramer, R.A.3    Egmond, M.R.4
  • 21
    • 4344603667 scopus 로고    scopus 로고
    • Substrate specificity of the Escherichia coli outer membrane protease OmpT
    • DOI 10.1128/JB.186.17.5919-5925.2004
    • Substrate specificity of the Escherichia coli outer membrane protease OmpT. JD McCarter D Stephens K Shoemaker S Rosenberg JF Kirsch G Georgiou, J Bacteriol 2004 186 17 5919 5925 10.1128/JB.186.17.5919-5925.2004 15317797 (Pubitemid 39128665)
    • (2004) Journal of Bacteriology , vol.186 , Issue.17 , pp. 5919-5925
    • McCarter, J.D.1    Stephens, D.2    Shoemaker, K.3    Rosenberg, S.4    Kirsch, J.F.5    Georgiou, G.6
  • 22
    • 33846217757 scopus 로고    scopus 로고
    • Substrate specificity of the Escherichia coli outer membrane protease OmpP
    • DOI 10.1128/JB.01493-06
    • Substrate specificity of the Escherichia coli outer membrane protease OmpP. BY Hwang N Varadarajan H Li S Rodriguez BL Iverson G Georgiou, J Bacteriol 2007 189 2 522 530 10.1128/JB.01493-06 17085556 (Pubitemid 46106384)
    • (2007) Journal of Bacteriology , vol.189 , Issue.2 , pp. 522-530
    • Hwang, B.-Y.1    Varadarajan, N.2    Li, H.3    Rodriguez, S.4    Iverson, B.L.5    Georgiou, G.6
  • 23
    • 37549040498 scopus 로고    scopus 로고
    • Substrate specificity and screening of the integral membrane protease Pla
    • 10.1016/j.bmcl.2007.09.104. 17981463
    • Substrate specificity and screening of the integral membrane protease Pla. A Agarkov S Chauhan PJ Lory SR Gilbertson VL Motin, Bioorg Med Chem Lett 2008 18 1 427 431 10.1016/j.bmcl.2007.09.104 17981463
    • (2008) Bioorg Med Chem Lett , vol.18 , Issue.1 , pp. 427-431
    • Agarkov, A.1    Chauhan, S.2    Lory, P.J.3    Gilbertson, S.R.4    Motin, V.L.5
  • 24
    • 3142737933 scopus 로고    scopus 로고
    • The omptin family of enterobacterial surface proteases/adhesins: From housekeeping in Escherichia coli to systemic spread of Yersinia pestis
    • DOI 10.1016/j.ijmm.2004.01.003
    • The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis. M Kukkonen TK Korhonen, Int J Med Microbiol 2004 294 1 7 14 10.1016/j.ijmm.2004. 01.003 15293449 (Pubitemid 38915608)
    • (2004) International Journal of Medical Microbiology , vol.294 , Issue.1 , pp. 7-14
    • Kukkonen, M.1    Korhonen, T.K.2
  • 26
    • 67749127374 scopus 로고    scopus 로고
    • The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity
    • 10.1128/JB.00489-09. 19465664
    • The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity. J Haiko M Kukkonen JJ Ravantti B Westerlund-Wikström TK Korhonen, J Bacteriol 2009 191 15 4758 4766 10.1128/JB.00489-09 19465664
    • (2009) J Bacteriol , vol.191 , Issue.15 , pp. 4758-4766
    • Haiko, J.1    Kukkonen, M.2    Ravantti, J.J.3    Westerlund-Wikström, B.4    Korhonen, T.K.5
  • 27
    • 0031771558 scopus 로고    scopus 로고
    • Expression of plasminogen activator Pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix
    • Expression of plasminogen activator pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix. K Lähteenmäki R Virkola A Saren L Emödy TK Korhonen, Infect Immun 1998 66 12 5755 5762 9826351 (Pubitemid 28531831)
    • (1998) Infection and Immunity , vol.66 , Issue.12 , pp. 5755-5762
    • Lahteenmaki, K.1    Virkola, R.2    Saren, A.3    Emody, L.4    Korhonen, T.K.5
  • 28
    • 34250736946 scopus 로고    scopus 로고
    • Fibrin and fibrinolysis in infection and host defense
    • DOI 10.1111/j.1538-7836.2007.02519.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Fibrin and fibrinolysis in infection and host defense. JL Degen TH Bugge JD Goguen, J Thromb Haemost 2007 5 Suppl 1 24 31 10.1111/j.1538-7836.2007.02519. x 17635705 (Pubitemid 46958813)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 24-31
    • Degen, J.L.1    Bugge, T.H.2    Goguen, J.D.3
  • 29
    • 0033943626 scopus 로고    scopus 로고
    • Invasion of epithelial cells by Yersinia pestis: Evidence for a Y. pestis-specific invasin
    • DOI 10.1128/IAI.68.8.4523-4530.2000
    • Invasion of epithelial cells by Yersinia pestis: evidence for a Y. pestis-specific invasin. C Cowan HA Jones YH Kaya RD Perry SC Straley, Infect Immun 2000 68 8 4523 4530 10.1128/IAI.68.8.4523-4530.2000 10899851 (Pubitemid 30497719)
    • (2000) Infection and Immunity , vol.68 , Issue.8 , pp. 4523-4530
    • Cowan, C.1    Jones, H.A.2    Kaya, Y.H.3    Perry, R.D.4    Straley, S.C.5
  • 30
    • 0035943478 scopus 로고    scopus 로고
    • The Pla surface protease/adhesin of Yersinia pestis mediates bacterial invasion into human endothelial cells
    • DOI 10.1016/S0014-5793(01)02775-2, PII S0014579301027752
    • The Pla surface protease/adhesin of Yersinia pestis mediates bacterial invasion into human endothelial cells. K Lähteenmäki M Kukkonen TK Korhonen, FEBS Lett 2001 504 1-2 69 72 11522299 (Pubitemid 32777814)
    • (2001) FEBS Letters , vol.504 , Issue.1-2 , pp. 69-72
    • Lahteenmaki, K.1    Kukkonen, M.2    Korhonen, T.K.3
  • 31
    • 57649137960 scopus 로고    scopus 로고
    • Plasminogen activator Pla of Yersinia pestis utilizes murine DEC-205 (CD205) as a receptor to promote dissemination
    • 10.1074/jbc.M804646200. 18650418
    • Plasminogen activator Pla of Yersinia pestis utilizes murine DEC-205 (CD205) as a receptor to promote dissemination. SS Zhang GP Chae P Zhang SS Bartra GV Plano JD Klena M Skurnik BJ Hinnebusch T Chen, J Biol Chem 2008 283 46 31511 31521 10.1074/jbc.M804646200 18650418
    • (2008) J Biol Chem , vol.283 , Issue.46 , pp. 31511-31521
    • Zhang, S.S.1    Chae, G.P.2    Zhang, P.3    Bartra, S.S.4    Plano, G.V.5    Klena, J.D.6    Skurnik, M.7    Hinnebusch, B.J.8    Chen, T.9
  • 34
    • 14844325784 scopus 로고    scopus 로고
    • Robustness, evolvability, and neutrality
    • DOI 10.1016/j.febslet.2005.01.063, Systems Biology
    • Robustness, evolvability, and neutrality. A Wagner, FEBS Lett 2005 579 8 1772 1778 10.1016/j.febslet.2005.01.063 15763550 (Pubitemid 40342652)
    • (2005) FEBS Letters , vol.579 , Issue.8 , pp. 1772-1778
    • Wagner, A.1
  • 35
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • DOI 10.1046/j.1365-2958.2000.01983.x
    • Structure and function of bacterial outer membrane proteins: barrels in a nutshell. R Koebnik KP Locher P Van Gelder, Mol Microbiol 2000 37 2 239 253 10.1046/j.1365-2958.2000.01983.x 10931321 (Pubitemid 30481009)
    • (2000) Molecular Microbiology , vol.37 , Issue.2 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 36
    • 0033932639 scopus 로고    scopus 로고
    • Barrel membrane proteins
    • 10.1016/S0959-440X(00)00120-2. 10981633
    • -barrel membrane proteins. GE Schulz, Curr Opin Struct Biol 2000 10 4 443 447 10.1016/S0959-440X(00)00120-2 10981633
    • (2000) Curr Opin Struct Biol , vol.10 , Issue.4 , pp. 443-447
    • Schulz, G.E.1
  • 38
    • 42149152860 scopus 로고    scopus 로고
    • Capsular antigen fraction 1 and Pla modulate the susceptibility of Yersinia pestis to pulmonary antimicrobial peptides such as cathelicidin
    • DOI 10.1128/IAI.01197-07
    • Capsular antigen fraction 1 and Pla modulate the susceptibility of Yersinia pestis to pulmonary antimicrobial peptides such as cathelicidin. EM Galvn MA Lasaro DM Schifferli, Infect Immun 2008 76 4 1456 1464 18227173 (Pubitemid 351561989)
    • (2008) Infection and Immunity , vol.76 , Issue.4 , pp. 1456-1464
    • Galvan, E.M.1    Lasaro, M.A.S.2    Schifferli, D.M.3
  • 39
    • 77952709859 scopus 로고    scopus 로고
    • Temperature-induced changes in the lipopolysaccharide of Yersinia pestis affect plasminogen activation by the Pla surface protease
    • 10.1128/IAI.01329-09. 20368351
    • Temperature-induced changes in the lipopolysaccharide of Yersinia pestis affect plasminogen activation by the Pla surface protease. M Suomalainen LA Lobo K Brandenburg B Lindner R Virkola YA Knirel AP Anisimov O Holst TK Korhonen, Infect Immun 2010 78 6 2644 2652 10.1128/IAI.01329-09 20368351
    • (2010) Infect Immun , vol.78 , Issue.6 , pp. 2644-2652
    • Suomalainen, M.1    Lobo, L.A.2    Brandenburg, K.3    Lindner, B.4    Virkola, R.5    Knirel, Y.A.6    Anisimov, A.P.7    Holst, O.8    Korhonen, T.K.9
  • 40
    • 0031755765 scopus 로고    scopus 로고
    • Structure-function relationships in serpins: Current concepts and controversies
    • Structure-function relationships in serpins: current concepts and controversies. A Gils PJ Declerck, Thromb Haemost 1998 80 4 531 541 9798964 (Pubitemid 28479333)
    • (1998) Thrombosis and Haemostasis , vol.80 , Issue.4 , pp. 531-541
    • Gils, A.1    Declerck, P.J.2
  • 41
    • 15944400320 scopus 로고    scopus 로고
    • Antiprotease inactivation by Salmonella enterica released from infected macrophages
    • DOI 10.1111/j.1462-5822.2004.00483.x
    • Antiprotease inactivation by Salmonella enterica released from infected macrophages. K Lähteenmäki P Kyllönen L Partanen TK Korhonen, Cell Microbiol 2005 7 4 529 538 15760453 (Pubitemid 40439452)
    • (2005) Cellular Microbiology , vol.7 , Issue.4 , pp. 529-538
    • Lahteenmaki, K.1    Kyllonen, P.2    Partanen, L.3    Korhonen, T.K.4
  • 42
    • 0029994995 scopus 로고    scopus 로고
    • Periplasmic location of the pesticin immunity protein suggests inactivation of pesticin in the periplasm
    • Periplasmic location of the pesticin immunity protein suggests inactivation of pesticin in the periplasm. H Pilsl H Killmann K Hantke V Braun, J Bacteriol 1996 178 8 2431 2435 8636051 (Pubitemid 26124444)
    • (1996) Journal of Bacteriology , vol.178 , Issue.8 , pp. 2431-2435
    • Pilsl, H.1    Killmann, H.2    Hantke, K.3    Braun, V.4
  • 43
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • DOI 10.1046/j.1365-2958.2003.03629.x
    • Touch and go: Tying TonB to transport. K Postle RJ Kadner, Mol Microbiol 2003 49 4 869 882 10.1046/j.1365-2958.2003.03629.x 12890014 (Pubitemid 36981335)
    • (2003) Molecular Microbiology , vol.49 , Issue.4 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 44
    • 34248647893 scopus 로고    scopus 로고
    • TonB-dependent energy transduction between outer and cytoplasmic membranes
    • DOI 10.1007/s10534-006-9071-6, Biometals: function and transport in bacteria, fungi, and humans
    • TonB-dependent energy transduction between outer and cytoplasmic membranes. K Postle RA Larsen, Biometals 2007 20 3-4 453 465 10.1007/s10534-006-9071-6 17225934 (Pubitemid 46776585)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 453-465
    • Postle, K.1    Larsen, R.A.2
  • 45
    • 55549120907 scopus 로고    scopus 로고
    • Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • 10.1074/jbc.M802754200. 18641391
    • Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro. NK Burgess TP Dao AM Stanley KG Fleming, J Biol Chem 2008 283 39 26748 26758 10.1074/jbc.M802754200 18641391
    • (2008) J Biol Chem , vol.283 , Issue.39 , pp. 26748-26758
    • Burgess, N.K.1    Dao, T.P.2    Stanley, A.M.3    Fleming, K.G.4
  • 46
    • 0024213555 scopus 로고
    • Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma
    • DOI 10.1016/0014-5793(88)80999-2
    • Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma. B Wiman A Almquist O Sigurdardottir T Lindahl, FEBS Lett 1988 242 1 125 128 10.1016/0014-5793(88)80999-2 2462509 (Pubitemid 19012262)
    • (1988) FEBS Letters , vol.242 , Issue.1 , pp. 125-128
    • Wiman, B.1    Almquist, A.2    Sigurdardottir, O.3    Lindahl, T.4
  • 48
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • Comparative protein modelling by satisfaction of spatial restraints. A Sali TL Blundell, J Mol Biol 1993 234 3 779 815 10.1006/jmbi.1993.1626 8254673 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 49
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • DOI 10.1016/0263-7855(96)00018-5
    • VMD - Visual Molecular Dynamics. W Humphrey A Dalke K Schulten, J Molec Graphics 1996 14 33 38 10.1016/0263-7855(96)00018-5 (Pubitemid 26152973)
    • (1996) Journal of Molecular Graphics , vol.14 , Issue.1 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 51
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • ALSCRIPT: a tool to format multiple sequence alignments. GJ Barton, Protein Engineering 1993 6 1 37 40 10.1093/protein/6.1.37 8433969 (Pubitemid 23048938)
    • (1993) Protein Engineering , vol.6 , Issue.1 , pp. 37-40
    • Barton, G.J.1
  • 52
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • DOI 10.1002/prot.340230412
    • Knowledge-based protein secondary structure assignment. D Frishman P Argos, Proteins 1995 23 4 566 579 10.1002/prot.340230412 8749853 (Pubitemid 26009520)
    • (1995) Proteins: Structure, Function and Genetics , vol.23 , Issue.4 , pp. 566-579
    • Frishman, D.1    Argos, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.