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Volumn 33, Issue 17, 2014, Pages 1896-1911

A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress

Author keywords

cryo electron microscopy; encapsulin; ferritin; HK97 fold; oxidative stress

Indexed keywords

BACTERIAL PROTEIN; CAPSID PROTEIN; ENCA PROTEIN; ENCAPSULIN NANOCOMPARTMENT; ENCB PROTEIN; ENCC PROTEIN; ENCD PROTEIN; FERRITIN; IRON; IRON BINDING PROTEIN; NANOCAGE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 84906825913     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201488566     Document Type: Article
Times cited : (135)

References (76)
  • 6
    • 77953807027 scopus 로고    scopus 로고
    • The Ferritin-like superfamily: Evolution of the biological iron storeman from a rubrerythrin-like ancestor
    • Andrews SC, (2010) The Ferritin-like superfamily: evolution of the biological iron storeman from a rubrerythrin-like ancestor. Biochim Biophys Acta 1800: 691-705
    • (2010) Biochim Biophys Acta , vol.1800 , pp. 691-705
    • Andrews, S.C.1
  • 7
    • 27744487093 scopus 로고    scopus 로고
    • Common ancestry of herpesviruses and tailed DNA bacteriophages
    • Baker ML, Jiang W, Rixon FJ, Chiu W, (2005) Common ancestry of herpesviruses and tailed DNA bacteriophages. J Virol 79: 14967-14970
    • (2005) J Virol , vol.79 , pp. 14967-14970
    • Baker, M.L.1    Jiang, W.2    Rixon, F.J.3    Chiu, W.4
  • 8
    • 0031257718 scopus 로고    scopus 로고
    • A method for establishing the handedness of biological macromolecules
    • Belnap DM, Olson NH, Baker TS, (1997) A method for establishing the handedness of biological macromolecules. J Struct Biol 120: 44-51
    • (1997) J Struct Biol , vol.120 , pp. 44-51
    • Belnap, D.M.1    Olson, N.H.2    Baker, T.S.3
  • 9
    • 0037282736 scopus 로고    scopus 로고
    • The variance of icosahedral virus models is a key indicator in the structure determination: A model-free reconstruction of viruses, suitable for refractory particles
    • Cantele F, Lanzavecchia S, Bellon PL, (2003) The variance of icosahedral virus models is a key indicator in the structure determination: a model-free reconstruction of viruses, suitable for refractory particles. J Struct Biol 141: 84-92
    • (2003) J Struct Biol , vol.141 , pp. 84-92
    • Cantele, F.1    Lanzavecchia, S.2    Bellon, P.L.3
  • 10
    • 23044510524 scopus 로고    scopus 로고
    • A resolution criterion for electron tomography based on cross-validation
    • Cardone G, Grünewald K, Steven AC, (2005) A resolution criterion for electron tomography based on cross-validation. J Struct Biol 151: 117-129
    • (2005) J Struct Biol , vol.151 , pp. 117-129
    • Cardone, G.1    Grünewald, K.2    Steven, A.C.3
  • 11
    • 84858240360 scopus 로고    scopus 로고
    • Procapsid assembly, maturation, nuclear exit: Dynamic steps in the production of infectious herpesvirions
    • Cardone G, Heymann JB, Cheng N, Trus BL, Steven AC, (2012) Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions. Adv Exp Med Biol 726: 423-439
    • (2012) Adv Exp Med Biol , vol.726 , pp. 423-439
    • Cardone, G.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Steven, A.C.5
  • 12
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project.
    • Collaborative Computational Project (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 15
    • 0028847173 scopus 로고
    • Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system
    • Conway JF, Duda RL, Cheng N, Hendrix RW, Steven AC, (1995) Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J Mol Biol 253: 86-99
    • (1995) J Mol Biol , vol.253 , pp. 86-99
    • Conway, J.F.1    Duda, R.L.2    Cheng, N.3    Hendrix, R.W.4    Steven, A.C.5
  • 17
    • 79959209134 scopus 로고    scopus 로고
    • Iron homeostasis and management of oxidative stress response in bacteria
    • Cornelis P, Wei Q, Andrews SC, Vinckx T, (2011) Iron homeostasis and management of oxidative stress response in bacteria. Metallomics 3: 540-549.
    • (2011) Metallomics , vol.3 , pp. 540-549
    • Cornelis, P.1    Wei, Q.2    Andrews, S.C.3    Vinckx, T.4
  • 18
    • 84871435690 scopus 로고    scopus 로고
    • Evolution of intracellular compartmentalization
    • Diekmann Y, Pereira-Leal JB, (2013) Evolution of intracellular compartmentalization. Biochem J 449: 319-331
    • (2013) Biochem J , vol.449 , pp. 319-331
    • Diekmann, Y.1    Pereira-Leal, J.B.2
  • 28
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P, (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275: 161-203
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 30
    • 84863242478 scopus 로고    scopus 로고
    • Bacteriophage HK97 capsid assembly and maturation
    • Hendrix RW, Johnson JE, (2012) Bacteriophage HK97 capsid assembly and maturation. Adv Exp Med Biol 726: 351-363
    • (2012) Adv Exp Med Biol , vol.726 , pp. 351-363
    • Hendrix, R.W.1    Johnson, J.E.2
  • 31
    • 0037406441 scopus 로고    scopus 로고
    • Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy
    • Heymann JB, Cheng N, Newcomb WW, Trus BL, Brown JC, Steven AC, (2003) Dynamics of herpes simplex virus capsid maturation visualized by time-lapse cryo-electron microscopy. Nat Struct Biol 10: 334-341
    • (2003) Nat Struct Biol , vol.10 , pp. 334-341
    • Heymann, J.B.1    Cheng, N.2    Newcomb, W.W.3    Trus, B.L.4    Brown, J.C.5    Steven, A.C.6
  • 32
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: Image processing and molecular modeling for electron microscopy
    • Heymann JB, Belnap DM, (2007) Bsoft: image processing and molecular modeling for electron microscopy. J Struct Biol 157: 3-18
    • (2007) J Struct Biol , vol.157 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 33
    • 0032438034 scopus 로고    scopus 로고
    • Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria
    • Hicks PM, Rinker KD, Baker JR, Kelly RM, (1998) Homomultimeric protease in the hyperthermophilic bacterium Thermotoga maritima has structural and amino acid sequence homology to bacteriocins in mesophilic bacteria. FEBS Lett 440: 393-398
    • (1998) FEBS Lett , vol.440 , pp. 393-398
    • Hicks, P.M.1    Rinker, K.D.2    Baker, J.R.3    Kelly, R.M.4
  • 34
    • 0018293841 scopus 로고
    • Genetics of gliding motility in Myxococcus xanthus (Myxobacterales): Two gene systems control movement
    • Hodgkin J, Kaiser D, (1979) Genetics of gliding motility in Myxococcus xanthus (Myxobacterales): two gene systems control movement. Mol Gen Genet 171: 177-191
    • (1979) Mol Gen Genet , vol.171 , pp. 177-191
    • Hodgkin, J.1    Kaiser, D.2
  • 35
    • 84883272572 scopus 로고    scopus 로고
    • Structure of the pseudorabies virus capsid: Comparison with herpes simplex virus type 1 and differential binding of essential minor proteins
    • Homa FL, Huffman JB, Toropova K, Lopez HR, Makhov AM, Conway JF, (2013) Structure of the pseudorabies virus capsid: comparison with herpes simplex virus type 1 and differential binding of essential minor proteins. J Mol Biol 425: 3415-3428
    • (2013) J Mol Biol , vol.425 , pp. 3415-3428
    • Homa, F.L.1    Huffman, J.B.2    Toropova, K.3    Lopez, H.R.4    Makhov, A.M.5    Conway, J.F.6
  • 36
    • 79953887810 scopus 로고    scopus 로고
    • The Prohead-I structure of bacteriophage HK97: Implications for scaffold-mediated control of particle assembly and maturation
    • Huang RK, Khayat R, Lee KK, Gertsman I, Duda RL, Hendrix RW, Johnson JE, (2011a) The Prohead-I structure of bacteriophage HK97: implications for scaffold-mediated control of particle assembly and maturation. J Mol Biol 408: 541-554
    • (2011) J Mol Biol , vol.408 , pp. 541-554
    • Huang, R.K.1    Khayat, R.2    Lee, K.K.3    Gertsman, I.4    Duda, R.L.5    Hendrix, R.W.6    Johnson, J.E.7
  • 38
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W, Chang J, Jakana J, Weigele P, King J, Chiu W, (2006) Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 439: 612-616
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 39
    • 0018536781 scopus 로고
    • Social gliding is correlated with the presence of pili in Myxococcus xanthus
    • Kaiser D, (1979) Social gliding is correlated with the presence of pili in Myxococcus xanthus. Proc Natl Acad Sci USA 76: 5952-5956
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 5952-5956
    • Kaiser, D.1
  • 41
    • 71549160364 scopus 로고    scopus 로고
    • Operon required for fruiting body development in Myxococcus xanthus
    • Kim D, Chung J, Hyun H, Lee C, Lee K, Cho K, (2009) Operon required for fruiting body development in Myxococcus xanthus. J Microbiol Biotechnol 19: 1288-1294
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 1288-1294
    • Kim, D.1    Chung, J.2    Hyun, H.3    Lee, C.4    Lee, K.5    Cho, K.6
  • 42
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • Kleywegt GJ, Brunger AT, (1996) Checking your imagination: applications of the free R value. Structure 4: 897-904
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brunger, A.T.2
  • 43
    • 0030498233 scopus 로고    scopus 로고
    • XdlMAPMAN and xdlDATAMAN - Programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets
    • Kleywegt GJ, Jones TA, (1996) xdlMAPMAN and xdlDATAMAN-programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets. Acta Crystallogr D Biol Crystallogr 52: 826-828
    • (1996) Acta Crystallogr D Biol Crystallogr , vol.52 , pp. 826-828
    • Kleywegt, G.J.1    Jones, T.A.2
  • 44
    • 84864020098 scopus 로고    scopus 로고
    • Myxococcus xanthus developmental cell fate production: Heterogeneous accumulation of developmental regulatory proteins and reexamination of the role of MazF in developmental lysis
    • Lee B, Holkenbrink C, Treuner-Lange A, Higgs PI, (2012a) Myxococcus xanthus developmental cell fate production: heterogeneous accumulation of developmental regulatory proteins and reexamination of the role of MazF in developmental lysis. J Bacteriol 194: 3058-3068
    • (2012) J Bacteriol , vol.194 , pp. 3058-3068
    • Lee, B.1    Holkenbrink, C.2    Treuner-Lange, A.3    Higgs, P.I.4
  • 45
    • 84859780045 scopus 로고    scopus 로고
    • Spatial organization of enzymes for metabolic engineering
    • Lee H, DeLoache WC, Dueber JE, (2012b) Spatial organization of enzymes for metabolic engineering. Metab Eng 14: 242-251
    • (2012) Metab Eng , vol.14 , pp. 242-251
    • Lee, H.1    Deloache, W.C.2    Dueber, J.E.3
  • 46
    • 2942558543 scopus 로고    scopus 로고
    • Ferritin reactions: Direct identification of the site for the diferric peroxide reaction intermediate
    • Liu X, Theil EC, (2004) Ferritin reactions: direct identification of the site for the diferric peroxide reaction intermediate. Proc Natl Acad Sci USA 101: 8557-8562
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8557-8562
    • Liu, X.1    Theil, E.C.2
  • 47
    • 77956258367 scopus 로고    scopus 로고
    • Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response
    • Lu LD, Sun Q, Fan XY, Zhong Y, Yao YF, Zhao GP, (2010) Mycobacterial MazG is a novel NTP pyrophosphohydrolase involved in oxidative stress response. J Biol Chem 285: 28076-28085
    • (2010) J Biol Chem , vol.285 , pp. 28076-28085
    • Lu, L.D.1    Sun, Q.2    Fan, X.Y.3    Zhong, Y.4    Yao, Y.F.5    Zhao, G.P.6
  • 48
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN, (2005) Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol 152: 36-51
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 49
    • 0000803940 scopus 로고
    • Ferritin: III the magnetic properties of ferritin and some other colloidal ferric compounds
    • Michaelis L, Coryell CD, Granick S, (1943) Ferritin: III. The magnetic properties of ferritin and some other colloidal ferric compounds. J Biol Chem 148: 463-480
    • (1943) J Biol Chem , vol.148 , pp. 463-480
    • Michaelis, L.1    Coryell, C.D.2    Granick, S.3
  • 50
    • 84869022036 scopus 로고    scopus 로고
    • Packaging accessory protein P7 and polymerase P2 have mutually occluding binding sites inside the bacteriophage φ6 procapsid
    • Nemecek D, Qiao J, Mindich L, Steven AC, Heymann JB, (2012) Packaging accessory protein P7 and polymerase P2 have mutually occluding binding sites inside the bacteriophage φ6 procapsid. J Virol 86: 11616-11624
    • (2012) J Virol , vol.86 , pp. 11616-11624
    • Nemecek, D.1    Qiao, J.2    Mindich, L.3    Steven, A.C.4    Heymann, J.B.5
  • 51
    • 77649128082 scopus 로고    scopus 로고
    • P22 coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical crosslinks
    • Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS, (2010) P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. Structure 18: 390-401
    • (2010) Structure , vol.18 , pp. 390-401
    • Parent, K.N.1    Khayat, R.2    Tu, L.H.3    Suhanovsky, M.M.4    Cortines, J.R.5    Teschke, C.M.6    Johnson, J.E.7    Baker, T.S.8
  • 53
    • 84876887523 scopus 로고    scopus 로고
    • Assembly in vitro of Rhodococcus jostii RHA1 encapsulin and peroxidase DypB to form a nanocompartment
    • Rahmanpour R, Bugg TD, (2013) Assembly in vitro of Rhodococcus jostii RHA1 encapsulin and peroxidase DypB to form a nanocompartment. FEBS J 280: 2097-2104
    • (2013) FEBS J , vol.280 , pp. 2097-2104
    • Rahmanpour, R.1    Bugg, T.D.2
  • 54
    • 0031813213 scopus 로고    scopus 로고
    • Identification and characterization of a 29-kilodalton protein from Mycobacterium tuberculosis culture filtrate recognized by mouse memory effector cells
    • Rosenkrands I, Rasmussen PB, Carnio M, Jacobsen S, Theisen M, Andersen P, (1998) Identification and characterization of a 29-kilodalton protein from Mycobacterium tuberculosis culture filtrate recognized by mouse memory effector cells. Infect Immun 66: 2728-2735
    • (1998) Infect Immun , vol.66 , pp. 2728-2735
    • Rosenkrands, I.1    Rasmussen, P.B.2    Carnio, M.3    Jacobsen, S.4    Theisen, M.5    Andersen, P.6
  • 55
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres SH, Chen S, (2012) Prevention of overfitting in cryo-EM structure determination. Nature Meth 9: 853-854
    • (2012) Nature Meth , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 56
    • 34247093347 scopus 로고    scopus 로고
    • Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils
    • Sen A, Baxa U, Simon MN, Wall JS, Sabate R, Saupe SJ, Steven AC, (2007) Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of stacked beta-solenoid model of HET-s prion fibrils. J Biol Chem 282: 5545-5550
    • (2007) J Biol Chem , vol.282 , pp. 5545-5550
    • Sen, A.1    Baxa, U.2    Simon, M.N.3    Wall, J.S.4    Sabate, R.5    Saupe, S.J.6    Steven, A.C.7
  • 57
    • 0033624219 scopus 로고    scopus 로고
    • The 1.9 A crystal structure of the "as isolated" rubrerythrin from Desulfovibrio vulgaris: Some surprising results
    • Sieker LC, Holmes M, Le Trong I, Turley S, Liu MY, LeGall J, Stenkamp RE, (2000) The 1.9 A crystal structure of the "as isolated" rubrerythrin from Desulfovibrio vulgaris: some surprising results. J Biol Inorg Chem 5: 505-513
    • (2000) J Biol Inorg Chem , vol.5 , pp. 505-513
    • Sieker, L.C.1    Holmes, M.2    Le Trong, I.3    Turley, S.4    Liu, M.Y.5    Legall, J.6    Stenkamp, R.E.7
  • 58
    • 78650903518 scopus 로고    scopus 로고
    • A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80alpha capsids
    • Spilman MS, Dearborn AD, Chang JR, Damle PK, Christie GE, Dokland T, (2011) A conformational switch involved in maturation of Staphylococcus aureus bacteriophage 80alpha capsids. J Mol Biol 405: 863-876
    • (2011) J Mol Biol , vol.405 , pp. 863-876
    • Spilman, M.S.1    Dearborn, A.D.2    Chang, J.R.3    Damle, P.K.4    Christie, G.E.5    Dokland, T.6
  • 59
    • 17044440108 scopus 로고    scopus 로고
    • Virus maturation: Dynamics and mechanism of a stabilizing structural transition that leads to infectivity
    • Steven AC, Heymann JB, Cheng N, Trus BL, Conway JF, (2005) Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity. Curr Opin Struct Biol 15: 227-236
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 227-236
    • Steven, A.C.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Conway, J.F.5
  • 61
    • 79953309867 scopus 로고    scopus 로고
    • Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry
    • Theil EC, (2011) Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry. Curr Opin Chem Biol 15: 304-311
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 304-311
    • Theil, E.C.1
  • 62
  • 63
    • 0028136474 scopus 로고
    • Mass analysis of biological macromolecular complexes by STEM
    • Thomas D, Schultz P, Steven AC, Wall JS, (1994) Mass analysis of biological macromolecular complexes by STEM. Biol Cell 80: 181-192
    • (1994) Biol Cell , vol.80 , pp. 181-192
    • Thomas, D.1    Schultz, P.2    Steven, A.C.3    Wall, J.S.4
  • 64
    • 42949089487 scopus 로고    scopus 로고
    • Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics
    • Trabuco LG, Villa E, Mitra K, Frank J, Schulten K, (2008) Flexible fitting of atomic structures into electron microscopy maps using molecular dynamics. Structure 16: 673-683
    • (2008) Structure , vol.16 , pp. 673-683
    • Trabuco, L.G.1    Villa, E.2    Mitra, K.3    Frank, J.4    Schulten, K.5
  • 65
    • 0030475588 scopus 로고    scopus 로고
    • Positive-negative KG cassettes for construction of multi-gene deletions using a single drug marker
    • Ueki T, Inouye S, Inouye M, (1996) Positive-negative KG cassettes for construction of multi-gene deletions using a single drug marker. Gene 183: 153-157
    • (1996) Gene , vol.183 , pp. 153-157
    • Ueki, T.1    Inouye, S.2    Inouye, M.3
  • 66
    • 0028075093 scopus 로고
    • Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens
    • Valdes-Stauber N, Scherer S, (1994) Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens. Appl Environ Microbiol 60: 3809-3814
    • (1994) Appl Environ Microbiol , vol.60 , pp. 3809-3814
    • Valdes-Stauber, N.1    Scherer, S.2
  • 69
    • 0017595257 scopus 로고
    • Developmentally induced autolysis during fruiting body formation by Myxococcus xanthus
    • Wireman JW, Dworkin M, (1977) Developmentally induced autolysis during fruiting body formation by Myxococcus xanthus. J Bacteriol 129: 798-802
    • (1977) J Bacteriol , vol.129 , pp. 798-802
    • Wireman, J.W.1    Dworkin, M.2
  • 70
    • 0030947960 scopus 로고    scopus 로고
    • A mycobacterial extracytoplasmic function sigma factor involved in survival following stress
    • Wu QL, Kong D, Lam K, Husson RN, (1997) A mycobacterial extracytoplasmic function sigma factor involved in survival following stress. J Bacteriol 179: 2922-2929
    • (1997) J Bacteriol , vol.179 , pp. 2922-2929
    • Wu, Q.L.1    Kong, D.2    Lam, K.3    Husson, R.N.4
  • 71
    • 33845348934 scopus 로고    scopus 로고
    • Ab initio random model method facilitates 3D reconstruction of icosahedral particles
    • Yan X, Dryden KA, Tang J, Baker TS, (2007) Ab initio random model method facilitates 3D reconstruction of icosahedral particles. J Struct Biol 157: 211-225
    • (2007) J Struct Biol , vol.157 , pp. 211-225
    • Yan, X.1    Dryden, K.A.2    Tang, J.3    Baker, T.S.4
  • 73
    • 79953080696 scopus 로고    scopus 로고
    • The protein shells of bacterial microcompartment organelles
    • Yeates TO, Thompson MC, Bobik TA, (2011) The protein shells of bacterial microcompartment organelles. Curr Opin Struct Biol 21: 223-231
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 223-231
    • Yeates, T.O.1    Thompson, M.C.2    Bobik, T.A.3
  • 74
    • 84864375724 scopus 로고    scopus 로고
    • Dps biomineralizing proteins: Multifunctional architects of nature
    • Zeth K, (2012) Dps biomineralizing proteins: multifunctional architects of nature. Biochem J 445: 297-311
    • (2012) Biochem J , vol.445 , pp. 297-311
    • Zeth, K.1
  • 75
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y, (2008) I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 9: 40
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 76
    • 35348833523 scopus 로고    scopus 로고
    • Chemosensory pathways, motility and development in Myxococcus xanthus
    • Zusman DR, Scott AE, Yang Z, Kirby JR, (2007) Chemosensory pathways, motility and development in Myxococcus xanthus. Nat Rev Microbiol 5: 862-872
    • (2007) Nat Rev Microbiol , vol.5 , pp. 862-872
    • Zusman, D.R.1    Scott, A.E.2    Yang, Z.3    Kirby, J.R.4


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