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Volumn 5, Issue , 2014, Pages

Crystal structure of listeriolysin O reveals molecular details of oligomerization and pore formation

Author keywords

[No Author keywords available]

Indexed keywords

LISTERIOLYSIN O; MITOGEN ACTIVATED PROTEIN KINASE 1; MONOMER; OLIGOMER; TRYPTOPHAN; BACTERIAL TOXIN; BIOPOLYMER; HEAT SHOCK PROTEIN; HEMOLYSIN; HLYA PROTEIN, LISTERIA MONOCYTOGENES;

EID: 84899053464     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4690     Document Type: Article
Times cited : (114)

References (59)
  • 1
    • 0042879872 scopus 로고    scopus 로고
    • Molecular features of the cytolytic pore-forming bacterial protein toxins
    • Alouf, J. E. Molecular features of the cytolytic pore-forming bacterial protein toxins. Folia. Microbiol. (Praha). 48, 5-16 (2003). (Pubitemid 37027631)
    • (2003) Folia Microbiologica , vol.48 , Issue.1 , pp. 5-16
    • Alouf, J.E.1
  • 2
    • 0034467504 scopus 로고    scopus 로고
    • Pore-forming bacterial protein toxins: An overview
    • Alouf, J. E. Pore-forming bacterial protein toxins: an overview. Curr. Top. Microbiol. Immunol. 257, 1-14 (2001).
    • (2001) Curr. Top. Microbiol. Immunol. , vol.257 , pp. 1-14
    • Alouf, J.E.1
  • 4
    • 0027526035 scopus 로고
    • The projection structure of Perfringolysin O (Clostridium perfringens θ-toxin)
    • DOI 10.1016/0014-5793(93)80050-5
    • Olofsson, A., Hebert, H. & Thelestam, M. The projection structure of perfringolysin O (Clostridium perfringens theta-toxin). FEBS Lett. 319, 125-127 (1993). (Pubitemid 23074283)
    • (1993) FEBS Letters , vol.319 , Issue.1-2 , pp. 125-127
    • Olofsson, A.1    Hebert, H.2    Thelestam, M.3
  • 6
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • DOI 10.1016/S0092-8674(00)81660-8
    • Shatursky, O. et al. The mechanism of membrane insertion for a cholesteroldependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99, 293-299 (1999). (Pubitemid 29519908)
    • (1999) Cell , vol.99 , Issue.3 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 7
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • DOI 10.1016/j.cell.2005.02.033
    • Tilley, S. J., Orlova, E. V., Gilbert, R. J., Andrew, P. W. & Saibil, H. R. Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121, 247-256 (2005). (Pubitemid 40546392)
    • (2005) Cell , vol.121 , Issue.2 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.J.C.3    Andrew, P.W.4    Saibil, H.R.5
  • 8
    • 44849103483 scopus 로고    scopus 로고
    • IFN-beta increases listeriolysin O-induced membrane permeabilization and death of macrophages
    • Zwaferink, H., Stockinger, S., Hazemi, P., Lemmens-Gruber, R. & Decker, T. IFN-beta increases listeriolysin O-induced membrane permeabilization and death of macrophages. J. Immunol. 180, 4116-4123 (2008).
    • (2008) J. Immunol. , vol.180 , pp. 4116-4123
    • Zwaferink, H.1    Stockinger, S.2    Hazemi, P.3    Lemmens-Gruber, R.4    Decker, T.5
  • 9
    • 0031912786 scopus 로고    scopus 로고
    • Listeria monocytogenes invasion of epithelial cells requires the MEK- 1/ERK-2 mitogen-activated protein kinase pathway
    • Tang, P., Sutherland, C. L., Gold, M. R. & Finlay, B. B. Listeria monocytogenes invasion of epithelial cells requires the MEK-1/ERK-2 mitogen-activated protein kinase pathway. Infect. Immun. 66, 1106-1112 (1998). (Pubitemid 28101153)
    • (1998) Infection and Immunity , vol.66 , Issue.3 , pp. 1106-1112
    • Tang, P.1    Sutherland, C.L.2    Gold, M.R.3    Finlay, B.B.4
  • 10
    • 76249108958 scopus 로고    scopus 로고
    • Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1beta, depending on listeriolysin O and NLRP3
    • Meixenberger, K. et al. Listeria monocytogenes-infected human peripheral blood mononuclear cells produce IL-1beta, depending on listeriolysin O and NLRP3. J. Immunol. 184, 922-930 (2010).
    • (2010) J. Immunol. , vol.184 , pp. 922-930
    • Meixenberger, K.1
  • 11
    • 77649163335 scopus 로고    scopus 로고
    • Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection
    • Meyer-Morse, N. et al. Listeriolysin O is necessary and sufficient to induce autophagy during Listeria monocytogenes infection. PLoS ONE 5, e8610 (2010).
    • (2010) PLoS ONE , vol.5
    • Meyer-Morse, N.1
  • 12
    • 83655190735 scopus 로고    scopus 로고
    • Listeriolysin O suppresses phospholipase C-mediated activation of the microbicidal NADPH oxidase to promote Listeria monocytogenes infection
    • Lam, G. Y. et al. Listeriolysin O suppresses phospholipase C-mediated activation of the microbicidal NADPH oxidase to promote Listeria monocytogenes infection. Cell. Host. Microbe. 10, 627-634 (2011).
    • (2011) Cell. Host. Microbe. , vol.10 , pp. 627-634
    • Lam, G.Y.1
  • 13
    • 77951535793 scopus 로고    scopus 로고
    • Listeria monocytogenes impairs SUMOylation for efficient infection
    • Ribet, D. et al. Listeria monocytogenes impairs SUMOylation for efficient infection. Nature 464, 1192-1195 (2010).
    • (2010) Nature , vol.464 , pp. 1192-1195
    • Ribet, D.1
  • 14
    • 79952749507 scopus 로고    scopus 로고
    • Listeria monocytogenes transiently alters mitochondrial dynamics during infection
    • Stavru, F., Bouillaud, F., Sartori, A., Ricquier, D. & Cossart, P. Listeria monocytogenes transiently alters mitochondrial dynamics during infection. Proc. Natl Acad. Sci. USA 108, 3612-3617 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 3612-3617
    • Stavru, F.1    Bouillaud, F.2    Sartori, A.3    Ricquier, D.4    Cossart, P.5
  • 16
    • 3042611531 scopus 로고    scopus 로고
    • Specificity of streptolysin O in cytolysinmediated translocation
    • Meehl, M. A. & Caparon, M. G. Specificity of streptolysin O in cytolysinmediated translocation. Mol. Microbiol. 52, 1665-1676 (2004).
    • (2004) Mol. Microbiol. , vol.52 , pp. 1665-1676
    • Meehl, M.A.1    Caparon, M.G.2
  • 18
    • 0034602312 scopus 로고    scopus 로고
    • A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity
    • Decatur, A. L. & Portnoy, D. A. A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity. Science 290, 992-995 (2000).
    • (2000) Science , vol.290 , pp. 992-995
    • Decatur, A.L.1    Portnoy, D.A.2
  • 19
    • 0344851711 scopus 로고    scopus 로고
    • Listeria monocytogenes Mutants That Fail to Compartmentalize Listerolysin O Activity Are Cytotoxic, Avirulent, and Unable to Evade Host Extracellular Defenses
    • DOI 10.1128/IAI.71.12.6754-6765.2003
    • Glomski, I. J., Decatur, A. L. & Portnoy, D. A. Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses. Infect. Immun. 71, 6754-6765 (2003). (Pubitemid 37475303)
    • (2003) Infection and Immunity , vol.71 , Issue.12 , pp. 6754-6765
    • Glomski, I.J.1    Decatur, A.L.2    Portnoy, D.A.3
  • 20
    • 33644819006 scopus 로고    scopus 로고
    • Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: Role of the PEST-like sequence
    • DOI 10.1111/j.1462-5822.2005.00631.x
    • Schnupf, P., Portnoy, D. A. & Decatur, A. L. Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: role of the PEST-like sequence. Cell. Microbiol. 8, 353-364 (2006). (Pubitemid 43356056)
    • (2006) Cellular Microbiology , vol.8 , Issue.2 , pp. 353-364
    • Schnupf, P.1    Portnoy, D.A.2    Decatur, A.L.3
  • 22
    • 83655192826 scopus 로고    scopus 로고
    • PH dependence of listeriolysin O aggregation and pore-forming ability
    • Bavdek, A. et al. pH dependence of listeriolysin O aggregation and pore-forming ability. FEBS J. 279, 126-141 (2012).
    • (2012) FEBS J. , vol.279 , pp. 126-141
    • Bavdek, A.1
  • 23
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • DOI 10.1128/IAI.73.10.6199-6209.2005
    • Tweten, R. K. Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect. Immun. 73, 6199-6209 (2005). (Pubitemid 41368781)
    • (2005) Infection and Immunity , vol.73 , Issue.10 , pp. 6199-6209
    • Tweten, R.K.1
  • 24
    • 84878787539 scopus 로고    scopus 로고
    • Listeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccines
    • Sun, R. & Liu, Y. Listeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccines. Hum. Vaccin. Immunother. 9, 1058-1068 (2013).
    • (2013) Hum. Vaccin. Immunother. , vol.9 , pp. 1058-1068
    • Sun, R.1    Liu, Y.2
  • 25
    • 78549267766 scopus 로고    scopus 로고
    • The structural basis for membrane binding and pore formation by lymphocyte perforin
    • Law, R. H. et al. The structural basis for membrane binding and pore formation by lymphocyte perforin. Nature 468, 447-451 (2010).
    • (2010) Nature , vol.468 , pp. 447-451
    • Law, R.H.1
  • 26
    • 84858967104 scopus 로고    scopus 로고
    • Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)
    • Aleshin, A. E. et al. Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). J. Biol. Chem. 287, 10210-10222 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 10210-10222
    • Aleshin, A.E.1
  • 27
    • 84861721290 scopus 로고    scopus 로고
    • Crystal structure of C5b-6 suggests structural basis for priming assembly of the membrane attack complex
    • Aleshin, A. E., DiScipio, R. G., Stec, B. & Liddington, R. C. Crystal structure of C5b-6 suggests structural basis for priming assembly of the membrane attack complex. J. Biol. Chem. 287, 19642-19652 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 19642-19652
    • Aleshin, A.E.1    Discipio, R.G.2    Stec, B.3    Liddington, R.C.4
  • 28
    • 79955953166 scopus 로고    scopus 로고
    • Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement
    • Lovelace, L. L., Cooper, C. L., Sodetz, J. M. & Lebioda, L. Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement. J. Biol. Chem. 286, 17585-17592 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 17585-17592
    • Lovelace, L.L.1    Cooper, C.L.2    Sodetz, J.M.3    Lebioda, L.4
  • 30
    • 84887313008 scopus 로고    scopus 로고
    • Crystallization and X-ray crystallographic analysis of the cholesterol-dependent cytolysin listeriolysin O from Listeria monocytogenes
    • Köster, S., Hudel, M., Chakraborty, T. & Yildiz, Ö. Crystallization and X-ray crystallographic analysis of the cholesterol-dependent cytolysin listeriolysin O from Listeria monocytogenes. Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 69, 1212-1215 (2013).
    • (2013) Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. , vol.69 , pp. 1212-1215
    • Köster, S.1    Hudel, M.2    Chakraborty, T.3    Yildiz, Ö.4
  • 31
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn, J., Feil, S. C., McKinstry, W. J., Tweten, R. K. & Parker, M. W. Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89, 685-692 (1997). (Pubitemid 27516171)
    • (1997) Cell , vol.89 , Issue.5 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 32
    • 67649743349 scopus 로고    scopus 로고
    • Cellular functions and X-ray structure of anthrolysin O, a cholesterol-dependent cytolysin secreted by Bacillus anthracis
    • Bourdeau, R. W. et al. Cellular functions and X-ray structure of anthrolysin O, a cholesterol-dependent cytolysin secreted by Bacillus anthracis. J. Biol. Chem. 284, 14645-14656 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 14645-14656
    • Bourdeau, R.W.1
  • 34
    • 79953148352 scopus 로고    scopus 로고
    • Crystal structure of cytotoxin protein suilysin from Streptococcus suis
    • Xu, L. et al. Crystal structure of cytotoxin protein suilysin from Streptococcus suis. Protein Cell 1, 96-105 (2010).
    • (2010) Protein Cell , vol.1 , pp. 96-105
    • Xu, L.1
  • 35
    • 84893639595 scopus 로고    scopus 로고
    • Structural studies of streptococcus pyogenes streptolysin o provide insights into the early steps of membrane penetration
    • Feil, S. C., Ascher, D. B., Kuiper, M. J., Tweten, R. K. & Parker, M. W. Structural Studies of Streptococcus pyogenes Streptolysin O Provide Insights into the Early Steps of Membrane Penetration. J. Mol. Biol. 426, 785-792 (2013).
    • (2013) J. Mol. Biol. , vol.426 , pp. 785-792
    • Feil, S.C.1    Ascher, D.B.2    Kuiper, M.J.3    Tweten, R.K.4    Parker, M.W.5
  • 36
    • 84878259928 scopus 로고    scopus 로고
    • Polyproline-II helix in proteins: Structure and functions
    • Adzhubei, A. A., Sternberg, M. J. & Makarov, A. A. Polyproline-II Helix in Proteins: Structure and Function. J. Mol. Biol. 425, 2100-2132 (2013).
    • (2013) J. Mol. Biol. , vol.425 , pp. 2100-2132
    • Adzhubei, A.A.1    Sternberg, M.J.2    Makarov, A.A.3
  • 38
    • 34447619164 scopus 로고    scopus 로고
    • 2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes
    • DOI 10.1111/j.1462-5822.2007.00932.x
    • Gekara, N. O. et al. The multiple mechanisms of Ca2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes. Cell. Microbiol. 9, 2008-2021 (2007). (Pubitemid 47087091)
    • (2007) Cellular Microbiology , vol.9 , Issue.8 , pp. 2008-2021
    • Gekara, N.O.1    Westphal, K.2    Ma, B.3    Rohde, M.4    Groebe, L.5    Weiss, S.6
  • 39
    • 1242343771 scopus 로고    scopus 로고
    • Calcium signalling during cell interactions with bacterial pathogens
    • DOI 10.1016/j.biolcel.2003.10.006, PII S0248490003001436
    • TranVan Nhieu, G., Clair, C., Grompone, G. & Sansonetti, P. Calcium signalling during cell interactions with bacterial pathogens. Biol. Cell. 96, 93-101 (2004). (Pubitemid 38240402)
    • (2004) Biology of the Cell , vol.96 , Issue.1 , pp. 93-101
    • TranVan Nhieu, G.1    Clair, C.2    Grompone, G.3    Sansonetti, P.4
  • 40
    • 67049154564 scopus 로고    scopus 로고
    • Listeriolysin O affects barrier function and induces chloride secretion in HT-29/B6 colon epithelial cells
    • Richter, J. F. et al. Listeriolysin O affects barrier function and induces chloride secretion in HT-29/B6 colon epithelial cells. Am. J. Physiol. Gastrointest. Liver. Physiol. 296, G1350-G1359 (2009).
    • (2009) Am. J. Physiol. Gastrointest. Liver. Physiol. , vol.296
    • Richter, J.F.1
  • 41
    • 0035830656 scopus 로고    scopus 로고
    • Streptolysin O: The C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization
    • DOI 10.1016/S0005-2736(00)00360-6, PII S0005273600003606
    • Weis, S. & Palmer, M. Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization. Biochim. Biophys. Acta. 1510, 292-299 (2001). (Pubitemid 32149904)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1510 , Issue.1-2 , pp. 292-299
    • Weis, S.1    Palmer, M.2
  • 42
    • 78649908803 scopus 로고    scopus 로고
    • Cholesterol microcrystals and cochleate cylinders: Attachment of pyolysin oligomers and domain 4
    • Harris, J. R. et al. Cholesterol microcrystals and cochleate cylinders: attachment of pyolysin oligomers and domain 4. J. Struct. Biol. 173, 38-45 (2011).
    • (2011) J. Struct. Biol. , vol.173 , pp. 38-45
    • Harris, J.R.1
  • 43
    • 84875762324 scopus 로고    scopus 로고
    • Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesteroldependent cytolysin
    • Pokrajac, L., Harris, J. R., Sarraf, N. & Palmer, M. Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesteroldependent cytolysin. Biochem. Cell Biol. 91, 59-66 (2013).
    • (2013) Biochem. Cell Biol. , vol.91 , pp. 59-66
    • Pokrajac, L.1    Harris, J.R.2    Sarraf, N.3    Palmer, M.4
  • 44
    • 85047686843 scopus 로고    scopus 로고
    • Development of a singlegene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes
    • Melton-Witt, J. A., McKay, S. L. & Portnoy, D. A. Development of a singlegene, signature-tag-based approach in combination with alanine mutagenesis to identify listeriolysin O residues critical for the in vivo survival of Listeria monocytogenes. Infect. Immun. 80, 2221-2230 (2012).
    • (2012) Infect. Immun. , vol.80 , pp. 2221-2230
    • Melton-Witt, J.A.1    McKay, S.L.2    Portnoy, D.A.3
  • 45
    • 0029126943 scopus 로고
    • Interaction of Listeria monocytogenes with mouse dendritic cells
    • Guzman, C. A. et al. Interaction of Listeria monocytogenes with mouse dendritic cells. Infect. Immun. 63, 3665-3673 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 3665-3673
    • Guzman, C.A.1
  • 46
    • 0043234285 scopus 로고    scopus 로고
    • Assembly and topography of the prepore complex in cholesterol-dependent cytolysins
    • DOI 10.1074/jbc.M303151200
    • Heuck, A. P., Tweten, R. K. & Johnson, A. E. Assembly and topography of the prepore complex in cholesterol-dependent cytolysins. J. Biol. Chem. 278, 31218-31225 (2003). (Pubitemid 36994638)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31218-31225
    • Heuck, A.P.1    Tweten, R.K.2    Johnson, A.E.3
  • 47
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • Hotze, E. M. et al. Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. J. Biol. Chem. 276, 8261-8268 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 8261-8268
    • Hotze, E.M.1
  • 49
    • 0028895031 scopus 로고
    • Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification
    • Darji, A. et al. Hyperexpression of listeriolysin in the nonpathogenic species Listeria innocua and high yield purification. J. Biotechnol. 43, 205-212 (1995).
    • (1995) J. Biotechnol. , vol.43 , pp. 205-212
    • Darji, A.1
  • 50
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 51
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. Solving structures of protein complexes by molecular replacement with Phaser. Acta. Crystallogr. D Biol. Crystallogr. 63, 32-41 (2007).
    • (2007) Acta. Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 52
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4, C
    • Collaborative Computational Project 4, C. The CCP4 suite: programs for protein crystallography. Acta. Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta. Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 53
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution, density modification, and model building
    • DOI 10.1107/S0909049503023938
    • Terwilliger, T. SOLVE and RESOLVE: automated structure solution, density modification and model building. J. Synchrotron. Radiat. 11, 49-52 (2004). (Pubitemid 40085632)
    • (2004) Journal of Synchrotron Radiation , vol.11 , Issue.1 , pp. 49-52
    • Terwilliger, T.1
  • 56
    • 49649085631 scopus 로고    scopus 로고
    • Automated structure solution with the PHENIX suite
    • Zwart, P. H. et al. Automated structure solution with the PHENIX suite. Methods. Mol. Biol. 426, 419-435 (2008).
    • (2008) Methods. Mol. Biol. , vol.426 , pp. 419-435
    • Zwart, P.H.1
  • 57
    • 33747593473 scopus 로고    scopus 로고
    • Use of PYMOL as a communications tool for molecular science
    • DeLano, W. L. Use of PYMOL as a communications tool for molecular science. Abstr. Pap. Am. Chem. S 228, U313-U314 (2004).
    • (2004) Abstr. Pap. Am. Chem. S , vol.228
    • Delano, W.L.1
  • 58
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J. et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 35, W522-W525 (2007).
    • (2007) Nucleic Acids Res. , vol.35
    • Dolinsky, T.J.1
  • 59
    • 0015740243 scopus 로고
    • Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes
    • Kant, J. A. & Steck, T. L. Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes. J. Biol. Chem. 248, 8457-8464 (1973).
    • (1973) J. Biol. Chem. , vol.248 , pp. 8457-8464
    • Kant, J.A.1    Steck, T.L.2


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