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Volumn 55, Issue 5, 2012, Pages 404-414

Cellular and organellar membrane-associated proteins in haloarchaea: Perspectives on the physiological significance and biotechnological applications

Author keywords

biotechnology; halophilic archaea; membrane proteins; physiology

Indexed keywords

ARCHAEAL PROTEIN;

EID: 84861713420     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-012-4321-z     Document Type: Review
Times cited : (19)

References (135)
  • 1
    • 77953672648 scopus 로고    scopus 로고
    • Translation of Henrich Klebahn's' Damaging agents of the klippfish-a contribution to the knowledge of the salt-loving organisms
    • DasSarma P, Klebahn G, Klebahn H. Translation of Henrich Klebahn's' Damaging agents of the klippfish-a contribution to the knowledge of the salt-loving organisms'. Saline Systems, 2010, 6: 7.
    • (2010) Saline Systems , vol.6 , pp. 7
    • Dassarma, P.1    Klebahn, G.2    Klebahn, H.3
  • 3
    • 33645103946 scopus 로고    scopus 로고
    • From genomes to function: haloarchaea as model organisms
    • Soppa J. From genomes to function: haloarchaea as model organisms. Microbiol-Sgm, 2006, 152: 585-590.
    • (2006) Microbiol-Sgm , vol.152 , pp. 585-590
    • Soppa, J.1
  • 4
    • 0026587424 scopus 로고
    • Crystalline bacterial cell-surface layers
    • Messner P, Sleytr U B. Crystalline bacterial cell-surface layers. Adv Microb Physiol, 1992, 33: 213-275.
    • (1992) Adv Microb Physiol , vol.33 , pp. 213-275
    • Messner, P.1    Sleytr, U.B.2
  • 5
    • 0033022073 scopus 로고    scopus 로고
    • Bioenergetic aspects of halophilism
    • Oren A. Bioenergetic aspects of halophilism. Microbiol Mol Biol Rev, 1999, 63: 334-348.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 334-348
    • Oren, A.1
  • 7
    • 33745218504 scopus 로고    scopus 로고
    • Protein secretion in the Archaea: multiple paths towards a unique cell surface
    • Albers S V, Szabó Z, Driessen A J M. Protein secretion in the Archaea: multiple paths towards a unique cell surface. Nat Rev Microbiol, 2006, 4: 537-547.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 537-547
    • Albers, S.V.1    Szabó, Z.2    Driessen, A.J.M.3
  • 8
    • 50049087513 scopus 로고    scopus 로고
    • Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane Distinct translocases and mechanisms
    • Natale P, Brüser T, Driessen A J M. Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane Distinct translocases and mechanisms. BBA-Biomembranes, 2008, 1778: 1735-1756.
    • (2008) BBA-Biomembranes , vol.1778 , pp. 1735-1756
    • Natale, P.1    Brüser, T.2    Driessen, A.J.M.3
  • 10
    • 0000562142 scopus 로고    scopus 로고
    • Bacteriorhodopsin as a photochromic retinal protein for optical memories
    • Hampp N. Bacteriorhodopsin as a photochromic retinal protein for optical memories. Chem Rev, 2000, 100: 1755-1776.
    • (2000) Chem Rev , vol.100 , pp. 1755-1776
    • Hampp, N.1
  • 11
    • 0022484888 scopus 로고
    • Halorhodopsin: a light-driven chloride ion pump
    • Lanyi J K. Halorhodopsin: a light-driven chloride ion pump. Annu Rev Biophys Biophys Chem, 1986, 15: 11-28.
    • (1986) Annu Rev Biophys Biophys Chem , vol.15 , pp. 11-28
    • Lanyi, J.K.1
  • 13
    • 0030814406 scopus 로고    scopus 로고
    • Genetic analysis of the gas vesicle gene cluster in haloarchaea
    • DasSarma S, Arora P. Genetic analysis of the gas vesicle gene cluster in haloarchaea. Fems Microbiol Lett, 1997, 153: 1-10.
    • (1997) Fems Microbiol Lett , vol.153 , pp. 1-10
    • Dassarma, S.1    Arora, P.2
  • 14
    • 84863229520 scopus 로고    scopus 로고
    • Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei
    • Cai S, Cai L, Liu H, et al. Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei. Appl Environ Microbiol, 2012, 78: 1946-1952.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1946-1952
    • Cai, S.1    Cai, L.2    Liu, H.3
  • 15
    • 44949083652 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthase in Haloferax mediterranei
    • Lu Q H, Han J, Zhou L G, et al. Genetic and biochemical characterization of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate) synthase in Haloferax mediterranei. J Bacteriol, 2008, 190: 4173-4180.
    • (2008) J Bacteriol , vol.190 , pp. 4173-4180
    • Lu, Q.H.1    Han, J.2    Zhou, L.G.3
  • 16
    • 35148828068 scopus 로고    scopus 로고
    • Hm, genes, required for biosynthesis of poly(3-hydroxybutyrate) in the extremely halophilic Archaeon Haloarcula marismortui
    • Hm, genes, required for biosynthesis of poly(3-hydroxybutyrate) in the extremely halophilic Archaeon Haloarcula marismortui. Appl Environ Microb, 2007, 73: 6058-6065.
    • (2007) Appl Environ Microb , vol.73 , pp. 6058-6065
    • Han, J.1    Lu, Q.2    Zhou, L.3
  • 17
    • 65549156552 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes)
    • Jendrossek D. Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes). J Bacteriol, 2009, 191: 3195-3202.
    • (2009) J Bacteriol , vol.191 , pp. 3195-3202
    • Jendrossek, D.1
  • 18
    • 0026467758 scopus 로고
    • Structural features of archaebacterial cell envelopes
    • Baumeister W, Lembcke G. Structural features of archaebacterial cell envelopes. J Bioenerg Biomembr, 1992, 24: 567-575.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 567-575
    • Baumeister, W.1    Lembcke, G.2
  • 19
    • 0024523934 scopus 로고
    • Principles of organization in eubacterial and archaebacterial surface-proteins
    • Baumeister W, Wildhaber I, Phipps B M. Principles of organization in eubacterial and archaebacterial surface-proteins. Can J Microbiol, 1989, 35: 215-227.
    • (1989) Can J Microbiol , vol.35 , pp. 215-227
    • Baumeister, W.1    Wildhaber, I.2    Phipps, B.M.3
  • 20
    • 0008599779 scopus 로고
    • Flagella, gas vacuoles and cell-wall structure in Halobacterium halobium: an electron microscope study
    • Houwink A L. Flagella, gas vacuoles and cell-wall structure in Halobacterium halobium: an electron microscope study. J Gen Microbiol, 1956, 15: 146-150.
    • (1956) J Gen Microbiol , vol.15 , pp. 146-150
    • Houwink, A.L.1
  • 21
    • 28244438390 scopus 로고    scopus 로고
    • Recent advances in structural research on ether lipids from archaea including comparative and physiological aspects
    • Koga Y, Morii H. Recent advances in structural research on ether lipids from archaea including comparative and physiological aspects. Biosci Biotech Bioch, 2005, 69: 2019-2034.
    • (2005) Biosci Biotech Bioch , vol.69 , pp. 2019-2034
    • Koga, Y.1    Morii, H.2
  • 22
    • 0017304039 scopus 로고
    • Formation of lipid-linked sugar compounds in Halobacterium salinarium-presumed intermediates in glycoprotein synthesis
    • Mescher M F, Hansen U, Strominger J L. Formation of lipid-linked sugar compounds in Halobacterium salinarium-presumed intermediates in glycoprotein synthesis. J Biol Chem, 1976, 251: 7289-7294.
    • (1976) J Biol Chem , vol.251 , pp. 7289-7294
    • Mescher, M.F.1    Hansen, U.2    Strominger, J.L.3
  • 23
    • 0008954109 scopus 로고
    • Sulfation of a repetitive saccharide in halobacterial cell-wall glycoprotein occurrence of a sulfated lipid-linked precursor
    • Wieland F, Lechner J, Bernhardt G, et al. Sulfation of a repetitive saccharide in halobacterial cell-wall glycoprotein occurrence of a sulfated lipid-linked precursor. Febs Lett, 1981, 132: 319-323.
    • (1981) Febs Lett , vol.132 , pp. 319-323
    • Wieland, F.1    Lechner, J.2    Bernhardt, G.3
  • 24
    • 0031061543 scopus 로고    scopus 로고
    • Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1
    • Wakai H, Nakamura S, Kawasaki H, et al. Cloning and sequencing of the gene encoding the cell surface glycoprotein of Haloarcula japonica strain TR-1. Extremophiles, 1997, 1: 29-35.
    • (1997) Extremophiles , vol.1 , pp. 29-35
    • Wakai, H.1    Nakamura, S.2    Kawasaki, H.3
  • 25
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper M, Berg E, Mengele R, et al. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J Bacteriol, 1990, 172: 7111-7118.
    • (1990) J Bacteriol , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3
  • 26
    • 0023655597 scopus 로고
    • The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria
    • Lechner J, Sumper M. The primary structure of a procaryotic glycoprotein. Cloning and sequencing of the cell surface glycoprotein gene of halobacteria. J Biol Chem, 1987, 262: 9724-9729.
    • (1987) J Biol Chem , vol.262 , pp. 9724-9729
    • Lechner, J.1    Sumper, M.2
  • 27
    • 0037459217 scopus 로고    scopus 로고
    • Unique amino acid composition of proteins in halophilic bacteria
    • Fukuchi S, Yoshimune K, Wakayama M, et al. Unique amino acid composition of proteins in halophilic bacteria. J Mol Biol, 2003, 327: 347-357.
    • (2003) J Mol Biol , vol.327 , pp. 347-357
    • Fukuchi, S.1    Yoshimune, K.2    Wakayama, M.3
  • 28
  • 29
    • 12944270421 scopus 로고    scopus 로고
    • Genome sequence of Halobacterium species NRC-1
    • Ng W V, Kennedy S P, Mahairas G G, et al. Genome sequence of Halobacterium species NRC-1. Proc Natl Acad Sci USA, 2000, 97: 12176-12181.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12176-12181
    • Ng, W.V.1    Kennedy, S.P.2    Mahairas, G.G.3
  • 30
    • 0017066835 scopus 로고
    • Chemical characterization of the regularly arranged surface layers of Clostridium thermosaccharolyticum and Clostridium thermohydrosulfuricum
    • Sleytr U B, Thorne K J. Chemical characterization of the regularly arranged surface layers of Clostridium thermosaccharolyticum and Clostridium thermohydrosulfuricum. J Bacteriol, 1976, 126: 377-383.
    • (1976) J Bacteriol , vol.126 , pp. 377-383
    • Sleytr, U.B.1    Thorne, K.J.2
  • 31
    • 43449108260 scopus 로고    scopus 로고
    • Sweet to the extreme: protein glycosylation in Archaea
    • Yurist-Doutsch S, Chaban B, VanDyke D J, et al. Sweet to the extreme: protein glycosylation in Archaea. Mol Microbiol, 2008, 68: 1079-1084.
    • (2008) Mol Microbiol , vol.68 , pp. 1079-1084
    • Yurist-Doutsch, S.1    Chaban, B.2    Vandyke, D.J.3
  • 32
    • 36248931035 scopus 로고    scopus 로고
    • Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
    • Abu-Qarn M, Yurist-Doutsch S, Giordano A, et al. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. J Mol Biol, 2007, 374: 1224-1236.
    • (2007) J Mol Biol , vol.374 , pp. 1224-1236
    • Abu-Qarn, M.1    Yurist-Doutsch, S.2    Giordano, A.3
  • 33
    • 42549147096 scopus 로고    scopus 로고
    • Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein
    • Abu-Qarn M, Giordano A, Battaglia F, et al. Identification of AglE, a second glycosyltransferase involved in N glycosylation of the Haloferax volcanii S-layer glycoprotein. J Bacteriol, 2008, 190: 3140-3146.
    • (2008) J Bacteriol , vol.190 , pp. 3140-3146
    • Abu-Qarn, M.1    Giordano, A.2    Battaglia, F.3
  • 34
    • 57349184123 scopus 로고    scopus 로고
    • Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii
    • Plavner N, Eichler J. Defining the topology of the N-glycosylation pathway in the halophilic archaeon Haloferax volcanii. J Bacteriol, 2008, 190: 8045-8052.
    • (2008) J Bacteriol , vol.190 , pp. 8045-8052
    • Plavner, N.1    Eichler, J.2
  • 35
    • 49249084955 scopus 로고    scopus 로고
    • aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein
    • Yurist-Doutsch S, Abu-Qarn M, Battaglia F, et al. aglF, aglG and aglI, novel members of a gene island involved in the N-glycosylation of the Haloferax volcanii S-layer glycoprotein. Mol Microbiol, 2008, 69: 1234-1245.
    • (2008) Mol Microbiol , vol.69 , pp. 1234-1245
    • Yurist-Doutsch, S.1    Abu-Qarn, M.2    Battaglia, F.3
  • 36
    • 0346252352 scopus 로고    scopus 로고
    • Facing extremes: archaeal surface-layer (glyco)proteins
    • Eichler J. Facing extremes: archaeal surface-layer (glyco)proteins. Microbiology, 2003, 149: 3347-3351.
    • (2003) Microbiology , vol.149 , pp. 3347-3351
    • Eichler, J.1
  • 37
    • 0026662396 scopus 로고
    • Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles
    • Mengele R, Sumper M. Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles. J Biol Chem, 1992, 267: 8182-8185.
    • (1992) J Biol Chem , vol.267 , pp. 8182-8185
    • Mengele, R.1    Sumper, M.2
  • 38
    • 0032524340 scopus 로고    scopus 로고
    • Mechanosensitive ion channels of the archaeon Haloferax volcanii
    • Le Dain A C, Saint N, Kloda A, et al. Mechanosensitive ion channels of the archaeon Haloferax volcanii. J Biol Chem, 1998, 273: 12116-12119.
    • (1998) J Biol Chem , vol.273 , pp. 12116-12119
    • le Dain, A.C.1    Saint, N.2    Kloda, A.3
  • 39
    • 0029100910 scopus 로고
    • Purification and functional reconstitution of the recombinant large mechanosensitive ion-channel (Mscl) of Escherichia coli
    • Häse C C, Ledain A C, Martinac B. Purification and functional reconstitution of the recombinant large mechanosensitive ion-channel (Mscl) of Escherichia coli. J Biol Chem, 1995, 270: 18329-18334.
    • (1995) J Biol Chem , vol.270 , pp. 18329-18334
    • Häse, C.C.1    Ledain, A.C.2    Martinac, B.3
  • 40
    • 0026621245 scopus 로고
    • ABC transporters: from microorganisms to man
    • Higgins C F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol, 1992, 8: 67-113.
    • (1992) Annu Rev Cell Biol , vol.8 , pp. 67-113
    • Higgins, C.F.1
  • 42
    • 0345151823 scopus 로고    scopus 로고
    • Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii
    • Wanner C, Soppa J. Genetic identification of three ABC transporters as essential elements for nitrate respiration in Haloferax volcanii. Genetics, 1999, 152: 1417-1428.
    • (1999) Genetics , vol.152 , pp. 1417-1428
    • Wanner, C.1    Soppa, J.2
  • 43
    • 24344486795 scopus 로고    scopus 로고
    • ABC transporter for corrinoids in Halobacterium sp strain NRC-1
    • Woodson J D, Reynolds A A, Escalante-Semerena J C. ABC transporter for corrinoids in Halobacterium sp strain NRC-1. J Bacteriol, 2005, 187: 5901-5909.
    • (2005) J Bacteriol , vol.187 , pp. 5901-5909
    • Woodson, J.D.1    Reynolds, A.A.2    Escalante-Semerena, J.C.3
  • 44
    • 34548478838 scopus 로고    scopus 로고
    • The ABC of binding-protein-dependent transport in archaea
    • Lee S J, Böhm A, Krug M, et al. The ABC of binding-protein-dependent transport in archaea. Trends Microbiol, 2007, 15: 389-397.
    • (2007) Trends Microbiol , vol.15 , pp. 389-397
    • Lee, S.J.1    Böhm, A.2    Krug, M.3
  • 45
    • 33747334086 scopus 로고    scopus 로고
    • The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity
    • Bolhuis H, Palm P, Wende A, et al. The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity. BMC Genomics, 2006, 7: 169.
    • (2006) BMC Genomics , vol.7 , pp. 169
    • Bolhuis, H.1    Palm, P.2    Wende, A.3
  • 46
    • 29144518548 scopus 로고    scopus 로고
    • Comparative genomic analyses of the bacterial phosphotransferase system
    • Barabote R D, Saier M H Jr. Comparative genomic analyses of the bacterial phosphotransferase system. Microbiol Mol Biol Rev, 2005, 69: 608-634.
    • (2005) Microbiol Mol Biol Rev , vol.69 , pp. 608-634
    • Barabote, R.D.1    Saier Jr., M.H.2
  • 47
    • 41949089913 scopus 로고    scopus 로고
    • Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction
    • Anderson I, Rodriguez J, Susanti D, et al. Genome sequence of Thermofilum pendens reveals an exceptional loss of biosynthetic pathways without genome reduction. J Bacteriol, 2008, 190: 2957-2965.
    • (2008) J Bacteriol , vol.190 , pp. 2957-2965
    • Anderson, I.1    Rodriguez, J.2    Susanti, D.3
  • 48
    • 0036854430 scopus 로고    scopus 로고
    • Protein transport in the halophilic archaeon Halobacterium sp NRC-1:a major role for the twin-arginine translocation pathway?
    • Bolhuis A. Protein transport in the halophilic archaeon Halobacterium sp NRC-1: a major role for the twin-arginine translocation pathway? Microbiol-Sgm, 2002, 148: 3335-3346.
    • (2002) Microbiol-Sgm , vol.148 , pp. 3335-3346
    • Bolhuis, A.1
  • 49
    • 0038202125 scopus 로고    scopus 로고
    • The archaeal twin-arginine translocation pathway
    • Hutcheon G W, Bolhuis A. The archaeal twin-arginine translocation pathway. Biochem Soc T, 2003, 31: 686-689.
    • (2003) Biochem Soc T , vol.31 , pp. 686-689
    • Hutcheon, G.W.1    Bolhuis, A.2
  • 50
    • 36549088956 scopus 로고    scopus 로고
    • Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins
    • Gimenez M I, Dilks K, Pöhlschroder M. Haloferax volcanii twin-arginine translocation substates include secreted soluble, C-terminally anchored and lipoproteins. Mol Microbiol, 2007, 66: 1597-1606.
    • (2007) Mol Microbiol , vol.66 , pp. 1597-1606
    • Gimenez, M.I.1    Dilks, K.2    Pöhlschroder, M.3
  • 51
    • 15744405122 scopus 로고    scopus 로고
    • Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
    • Berks B C, Palmer T, Sargent F. Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. Curr Opin Microbiol, 2005, 8: 174-181.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 174-181
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 52
    • 0036038940 scopus 로고    scopus 로고
    • Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway
    • Rose R W, Brüser T, Kissinger J C, et al. Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway. Mol Microbiol, 2002, 45: 943-950.
    • (2002) Mol Microbiol , vol.45 , pp. 943-950
    • Rose, R.W.1    Brüser, T.2    Kissinger, J.C.3
  • 53
    • 37349115561 scopus 로고    scopus 로고
    • A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life
    • Widdick D A, Eijlander R T, van Dijl J M, et al. A facile reporter system for the experimental identification of twin-arginine translocation (Tat) signal peptides from all kingdoms of life. J Mol Biol, 2008, 375: 595-603.
    • (2008) J Mol Biol , vol.375 , pp. 595-603
    • Widdick, D.A.1    Eijlander, R.T.2    van Dijl, J.M.3
  • 54
    • 0141672034 scopus 로고    scopus 로고
    • The Tat protein translocation pathway and its role in microbial physiology
    • Berks B C, Palmer T, Sargent F. The Tat protein translocation pathway and its role in microbial physiology. Adv Microb Physiol, 2003, 47: 187-254.
    • (2003) Adv Microb Physiol , vol.47 , pp. 187-254
    • Berks, B.C.1    Palmer, T.2    Sargent, F.3
  • 55
    • 27844443566 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea
    • Dilks K, Giménez M I, Pöhlschroder M. Genetic and biochemical analysis of the twin-arginine translocation pathway in halophilic archaea. J Bacteriol, 2005, 187: 8104-8113.
    • (2005) J Bacteriol , vol.187 , pp. 8104-8113
    • Dilks, K.1    Giménez, M.I.2    Pöhlschroder, M.3
  • 56
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: moving folded proteins across membranes
    • Sargent F. The twin-arginine transport system: moving folded proteins across membranes. Biochem Soc Trans, 2007, 35: 835-847.
    • (2007) Biochem Soc Trans , vol.35 , pp. 835-847
    • Sargent, F.1
  • 57
    • 33645064518 scopus 로고    scopus 로고
    • The tatC gene cluster is essential for viability in halophilic archaea
    • Thomas J R, Bolhuis A. The tatC gene cluster is essential for viability in halophilic archaea. FEMS Microbiol Lett, 2006, 256: 44-49.
    • (2006) FEMS Microbiol Lett , vol.256 , pp. 44-49
    • Thomas, J.R.1    Bolhuis, A.2
  • 58
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: structures and functions from archaea to humans
    • Spudich J L, Yang C S, Jung K H, et al. Retinylidene proteins: structures and functions from archaea to humans. Annu Rev Cell Dev Biol, 2000, 16: 365-392.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 365-392
    • Spudich, J.L.1    Yang, C.S.2    Jung, K.H.3
  • 59
    • 0031747352 scopus 로고    scopus 로고
    • Variations on a molecular switch: transport and sensory signalling by archaeal rhodopsins
    • Spudich J L. Variations on a molecular switch: transport and sensory signalling by archaeal rhodopsins. Mol Microbiol, 1998, 28: 1051-1058.
    • (1998) Mol Microbiol , vol.28 , pp. 1051-1058
    • Spudich, J.L.1
  • 60
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt D, Stoeckenius W. Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol, 1971, 233: 149-152.
    • (1971) Nat New Biol , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 61
    • 0016842810 scopus 로고
    • Three-dimensional model of purple membrane obtained by electron microscopy
    • Henderson R, Unwin P N T. Three-dimensional model of purple membrane obtained by electron microscopy. Nature, 1975, 257: 28-32.
    • (1975) Nature , vol.257 , pp. 28-32
    • Henderson, R.1    Unwin, P.N.T.2
  • 62
    • 0037093403 scopus 로고    scopus 로고
    • From structure to mechanism: electron crystallographic studies of bacteriorhodopsin
    • Subramaniam S, Hirai T, Henderson R. From structure to mechanism: electron crystallographic studies of bacteriorhodopsin. Philos T Roy Soc A, 2002, 360: 859-874.
    • (2002) Philos T Roy Soc A , vol.360 , pp. 859-874
    • Subramaniam, S.1    Hirai, T.2    Henderson, R.3
  • 63
    • 0024278712 scopus 로고
    • Bacteriorhodopsin, a membrane protein that uses light to translocate protons
    • Khorana H G. Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J Biol Chem, 1988, 263: 7439-7442.
    • (1988) J Biol Chem , vol.263 , pp. 7439-7442
    • Khorana, H.G.1
  • 64
    • 0026023558 scopus 로고
    • Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmid
    • Krebs M P, Hauss T, Heyn M P, et al. Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmid. Proc Natl Acad Sci USA, 1991, 88: 859-863.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 859-863
    • Krebs, M.P.1    Hauss, T.2    Heyn, M.P.3
  • 65
    • 0035937192 scopus 로고    scopus 로고
    • brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum
    • Peck R F, Echavarri-Erasun C, Johnson E A, et al. brp and blh are required for synthesis of the retinal cofactor of bacteriorhodopsin in Halobacterium salinarum. J Biol Chem, 2001, 276: 5739-5744.
    • (2001) J Biol Chem , vol.276 , pp. 5739-5744
    • Peck, R.F.1    Echavarri-Erasun, C.2    Johnson, E.A.3
  • 67
    • 0020016635 scopus 로고
    • Bacteriorhodopsin and related pigments of halobacteria
    • Stoeckenius W, Bogomolni R A. Bacteriorhodopsin and related pigments of halobacteria. Annu Rev Biochem, 1982, 51: 587-616.
    • (1982) Annu Rev Biochem , vol.51 , pp. 587-616
    • Stoeckenius, W.1    Bogomolni, R.A.2
  • 68
    • 33745018088 scopus 로고    scopus 로고
    • Bacteriorhodopsin (bR) as an electronic conduction medium: Current transport through bR-containing monolayers
    • Jin Y D, Friedman N, Sheves M, et al. Bacteriorhodopsin (bR) as an electronic conduction medium: Current transport through bR-containing monolayers. Proc Natl Acad Sci USA, 2006, 103: 8601-8606.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8601-8606
    • Jin, Y.D.1    Friedman, N.2    Sheves, M.3
  • 69
    • 0035498344 scopus 로고    scopus 로고
    • X-ray crystallography of bacteriorhodopsin and its photointermediates: Insights into the mechanism of proton transport
    • Lanyi J K. X-ray crystallography of bacteriorhodopsin and its photointermediates: Insights into the mechanism of proton transport. Biochemistry(Moscow), 2001, 66: 1192-1196.
    • (2001) Biochemistry(Moscow) , vol.66 , pp. 1192-1196
    • Lanyi, J.K.1
  • 70
    • 84455178930 scopus 로고    scopus 로고
    • The microbial opsin family of optogenetic tools
    • Zhang F, Vierock J, Yizhar O, et al. The microbial opsin family of optogenetic tools. Cell, 2011, 147: 1446-1457.
    • (2011) Cell , vol.147 , pp. 1446-1457
    • Zhang, F.1    Vierock, J.2    Yizhar, O.3
  • 71
    • 69249135566 scopus 로고    scopus 로고
    • Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses
    • Hirai T, Subramaniam S. Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses. PLoS ONE, 2009, 4: e5769.
    • (2009) PLoS ONE , vol.4
    • Hirai, T.1    Subramaniam, S.2
  • 72
    • 0016723355 scopus 로고
    • Bacteriorhodopsin: a light-driven proton pump in Halobacterium halobium
    • Lozier R H, Bogomolni R A, Stoeckenius W. Bacteriorhodopsin: a light-driven proton pump in Halobacterium halobium. Biophys J, 1975, 15: 955-962.
    • (1975) Biophys J , vol.15 , pp. 955-962
    • Lozier, R.H.1    Bogomolni, R.A.2    Stoeckenius, W.3
  • 73
    • 0027526352 scopus 로고
    • Mechanism of light-dependent proton translocation by bacteriorhodopsin
    • Krebs M P, Khorana H G. Mechanism of light-dependent proton translocation by bacteriorhodopsin. J Bacteriol, 1993, 175: 1555-1560.
    • (1993) J Bacteriol , vol.175 , pp. 1555-1560
    • Krebs, M.P.1    Khorana, H.G.2
  • 74
    • 34547471963 scopus 로고    scopus 로고
    • Bacteriorhodopsin photocycle at cryogenic temperatures reveals distributed barriers of conformational substates
    • Dioumaev A K, Lanyi J K. Bacteriorhodopsin photocycle at cryogenic temperatures reveals distributed barriers of conformational substates. Proc Natl Acad Sci USA, 2007, 104: 9621-9626.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9621-9626
    • Dioumaev, A.K.1    Lanyi, J.K.2
  • 75
    • 0020479529 scopus 로고
    • Halorhodopsin is a light-driven chloride pump
    • Schobert B, Lanyi J K. Halorhodopsin is a light-driven chloride pump. J Biol Chem, 1982, 257: 306-313.
    • (1982) J Biol Chem , vol.257 , pp. 306-313
    • Schobert, B.1    Lanyi, J.K.2
  • 76
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 angstrom resolution
    • Kolbe M, Besir H, Essen L O, et al. Structure of the light-driven chloride pump halorhodopsin at 1. 8 angstrom resolution. Science, 2000, 288: 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3
  • 77
    • 0000948647 scopus 로고
    • The photocycle of the chloride pump halorhodopsin I: azidecatalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump
    • Hegemann P, Oesterhelt D, Steiner M. The photocycle of the chloride pump halorhodopsin I: azidecatalyzed deprotonation of the chromophore is a side reaction of photocycle intermediates inactivating the pump. EMBO J, 1985, 4: 2347-2350.
    • (1985) EMBO J , vol.4 , pp. 2347-2350
    • Hegemann, P.1    Oesterhelt, D.2    Steiner, M.3
  • 78
    • 0034712851 scopus 로고    scopus 로고
    • The three-dimensional structure of halorhodopsin to 5 angstrom by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure
    • Kunji E R S, von Gronau S, Oesterhelt D, et al. The three-dimensional structure of halorhodopsin to 5 angstrom by electron crystallography: A new unbending procedure for two-dimensional crystals by using a global reference structure. Proc Natl Acad Sci USA, 2000, 97: 4637-4642.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4637-4642
    • Kunji, E.R.S.1    von Gronau, S.2    Oesterhelt, D.3
  • 79
    • 0032961349 scopus 로고    scopus 로고
    • Halobacterial rhodopsins
    • Mukohata Y, Ihara K, Tamura T, et al. Halobacterial rhodopsins. J Biochem, 1999, 125: 649-657.
    • (1999) J Biochem , vol.125 , pp. 649-657
    • Mukohata, Y.1    Ihara, K.2    Tamura, T.3
  • 80
    • 0000373165 scopus 로고
    • Identification of a 3rd-rhodopsin-like pigment in phototactic Halobacterium halobium
    • Bogomolni R A, Spudich J L. Identification of a 3rd-rhodopsin-like pigment in phototactic Halobacterium halobium. Proc Natl Acad Sci-Biol, 1982, 79: 6250-6254.
    • (1982) Proc Natl Acad Sci-Biol , vol.79 , pp. 6250-6254
    • Bogomolni, R.A.1    Spudich, J.L.2
  • 81
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff W D, Jung K H, Spudich J L. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu Rev Bioph Biom, 1997, 26: 223-258.
    • (1997) Annu Rev Bioph Biom , vol.26 , pp. 223-258
    • Hoff, W.D.1    Jung, K.H.2    Spudich, J.L.3
  • 83
    • 0032874464 scopus 로고    scopus 로고
    • Proton circulation during the photocycle of sensory rhodopsin II
    • Sasaki J, Spudich J L. Proton circulation during the photocycle of sensory rhodopsin II. Biophys J, 1999, 77: 2145-2152.
    • (1999) Biophys J , vol.77 , pp. 2145-2152
    • Sasaki, J.1    Spudich, J.L.2
  • 84
    • 0025653013 scopus 로고
    • Photophysics and molecular electronic applications of the rhodopsins
    • Birge R R. Photophysics and molecular electronic applications of the rhodopsins. Annu Rev Phys Chem, 1990, 41: 683-733.
    • (1990) Annu Rev Phys Chem , vol.41 , pp. 683-733
    • Birge, R.R.1
  • 85
    • 0025950123 scopus 로고
    • Mechanism of activation of sensory rhodopsin I: evidence for a steric trigger
    • Yan B, Nakanishi K, Spudich J L. Mechanism of activation of sensory rhodopsin I: evidence for a steric trigger. Proc Natl Acad Sci USA, 1991, 88: 9412-9416.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9412-9416
    • Yan, B.1    Nakanishi, K.2    Spudich, J.L.3
  • 86
    • 23344432363 scopus 로고    scopus 로고
    • Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer
    • Bergo V B, Spudich E N, Rothschild K J, et al. Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer. J Biol Chem, 2005, 280: 28365-28369.
    • (2005) J Biol Chem , vol.280 , pp. 28365-28369
    • Bergo, V.B.1    Spudich, E.N.2    Rothschild, K.J.3
  • 88
    • 0033623952 scopus 로고    scopus 로고
    • Eight of fourteen gvp genes are sufficient for formation of gas vesicles in halophilic archaea
    • Offner S, Hofacker A, Wanner G, et al. Eight of fourteen gvp genes are sufficient for formation of gas vesicles in halophilic archaea. J Bacteriol, 2000, 182: 4328-4336.
    • (2000) J Bacteriol , vol.182 , pp. 4328-4336
    • Offner, S.1    Hofacker, A.2    Wanner, G.3
  • 89
    • 0027985167 scopus 로고
    • Wild-type gas vesicle formation requires at least ten genes in the gvp gene cluster of Halobacterium halobium plasmid pNRC100
    • DasSarma S, Arora P, Lin F, et al. Wild-type gas vesicle formation requires at least ten genes in the gvp gene cluster of Halobacterium halobium plasmid pNRC100. J Bacteriol, 1994, 176: 7646-7652.
    • (1994) J Bacteriol , vol.176 , pp. 7646-7652
    • Dassarma, S.1    Arora, P.2    Lin, F.3
  • 90
    • 77957340600 scopus 로고    scopus 로고
    • Solid-state NMR characterization of gas vesicle structure
    • Sivertsen A C, Bayro M J, Belenky M, et al. Solid-state NMR characterization of gas vesicle structure. Biophys J, 2010, 99: 1932-1939.
    • (2010) Biophys J , vol.99 , pp. 1932-1939
    • Sivertsen, A.C.1    Bayro, M.J.2    Belenky, M.3
  • 91
    • 79959562522 scopus 로고    scopus 로고
    • Structural model of the gas vesicle protein GvpA and analysis of GvpA mutants in vivo
    • Strunk T, Hamacher K, Hoffgaard F, et al. Structural model of the gas vesicle protein GvpA and analysis of GvpA mutants in vivo. Mol Microbiol, 2011, 81: 56-68.
    • (2011) Mol Microbiol , vol.81 , pp. 56-68
    • Strunk, T.1    Hamacher, K.2    Hoffgaard, F.3
  • 92
    • 0026542940 scopus 로고
    • Gas vesicles are strengthened by the outer-surface protein, GvpC
    • Hayes P K, Buchholz B, Walsby A E. Gas vesicles are strengthened by the outer-surface protein, GvpC. Arch Microbiol, 1992, 157: 229-234.
    • (1992) Arch Microbiol , vol.157 , pp. 229-234
    • Hayes, P.K.1    Buchholz, B.2    Walsby, A.E.3
  • 93
    • 0027408494 scopus 로고
    • The rightward gas vesicle operon in Halobacterium plasmid pNRC100: identification of the gvpA and gvpC gene products by use of antibody probes and genetic analysis of the region downstream of gvpC
    • Halladay J T, Jones J G, Lin F, et al. The rightward gas vesicle operon in Halobacterium plasmid pNRC100: identification of the gvpA and gvpC gene products by use of antibody probes and genetic analysis of the region downstream of gvpC. J Bacteriol, 1993, 175: 684-692.
    • (1993) J Bacteriol , vol.175 , pp. 684-692
    • Halladay, J.T.1    Jones, J.G.2    Lin, F.3
  • 94
    • 0027155201 scopus 로고
    • Analysis of gas vesicle gene expression in Haloferax mediterranei reveals that GvpA and GvpC are both gas vesicle structural proteins
    • Englert C, Pfeifer F. Analysis of gas vesicle gene expression in Haloferax mediterranei reveals that GvpA and GvpC are both gas vesicle structural proteins. J Biol Chem, 1993, 268: 9329-9336.
    • (1993) J Biol Chem , vol.268 , pp. 9329-9336
    • Englert, C.1    Pfeifer, F.2
  • 95
    • 0029966038 scopus 로고    scopus 로고
    • Functional studies of the gvpACNO operon of Halobacterium salinarium reveal that the GvpC protein shapes gas vesicles
    • Offner S, Wanner G, Pfeifer F. Functional studies of the gvpACNO operon of Halobacterium salinarium reveal that the GvpC protein shapes gas vesicles. J Bacteriol, 1996, 178: 2071-2078.
    • (1996) J Bacteriol , vol.178 , pp. 2071-2078
    • Offner, S.1    Wanner, G.2    Pfeifer, F.3
  • 96
    • 0028261412 scopus 로고
    • Gas vesicles
    • Walsby A E. Gas vesicles. Microbiol Rev, 1994, 58: 94-144.
    • (1994) Microbiol Rev , vol.58 , pp. 94-144
    • Walsby, A.E.1
  • 97
    • 2342660728 scopus 로고    scopus 로고
    • Complexity of gas vesicle biogenesis in Halobacterium sp. strain NRC-1: identification of five new proteins
    • Shukla H D, DasSarma S. Complexity of gas vesicle biogenesis in Halobacterium sp. strain NRC-1: identification of five new proteins. J Bacteriol, 2004, 186: 3182-3186.
    • (2004) J Bacteriol , vol.186 , pp. 3182-3186
    • Shukla, H.D.1    Dassarma, S.2
  • 98
    • 79952408606 scopus 로고    scopus 로고
    • New structural proteins of Halobacterium salinarum gas vesicle revealed by comparative proteomics analysis
    • Chu L J, Chen M C, Setter J, et al. New structural proteins of Halobacterium salinarum gas vesicle revealed by comparative proteomics analysis. J Proteome Res, 2011, 10: 1170-1178.
    • (2011) J Proteome Res , vol.10 , pp. 1170-1178
    • Chu, L.J.1    Chen, M.C.2    Setter, J.3
  • 99
    • 77949374617 scopus 로고    scopus 로고
    • Halopiger aswanensis sp. nov., a polymer-producing and extremely halophilic archaeon isolated from hypersaline soil
    • Hezayen F F, Gutiérrez M C, Steinbüchel A, et al. Halopiger aswanensis sp. nov., a polymer-producing and extremely halophilic archaeon isolated from hypersaline soil. Int J Syst Evol Microbiol, 2010, 60: 633-637.
    • (2010) Int J Syst Evol Microbiol , vol.60 , pp. 633-637
    • Hezayen, F.F.1    Gutiérrez, M.C.2    Steinbüchel, A.3
  • 100
    • 0025282845 scopus 로고
    • Effects of culture conditions on poly(beta-hydroxybutyric acid) production by Haloferax mediterranei
    • Lillo J G, Rodriguez-Valera F. Effects of culture conditions on poly(beta-hydroxybutyric acid) production by Haloferax mediterranei. Appl Environ Microbiol, 1990, 56: 2517-2521.
    • (1990) Appl Environ Microbiol , vol.56 , pp. 2517-2521
    • Lillo, J.G.1    Rodriguez-Valera, F.2
  • 101
    • 0033802118 scopus 로고    scopus 로고
    • Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor
    • Hezayen F F, Rehm B H A, Eberhardt R, et al. Polymer production by two newly isolated extremely halophilic archaea: application of a novel corrosion-resistant bioreactor. Appl Microbiol Biot, 2000, 54: 319-325.
    • (2000) Appl Microbiol Biot , vol.54 , pp. 319-325
    • Hezayen, F.F.1    Rehm, B.H.A.2    Eberhardt, R.3
  • 102
    • 0345688125 scopus 로고    scopus 로고
    • Polyester synthases: natural catalysts for plastics
    • Rehm B H. Polyester synthases: natural catalysts for plastics. Biochem J, 2003, 376: 15-33.
    • (2003) Biochem J , vol.376 , pp. 15-33
    • Rehm, B.H.1
  • 103
    • 0036667428 scopus 로고    scopus 로고
    • Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16
    • Pötter M, Madkour M H, Mayer F, et al. Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16. Microbiology, 2002, 148: 2413-2426.
    • (2002) Microbiology , vol.148 , pp. 2413-2426
    • Pötter, M.1    Madkour, M.H.2    Mayer, F.3
  • 104
    • 16344375052 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate) granule-associated proteins: impacts on poly(3-hydroxybutyrate) synthesis and degradation
    • Pötter M, Steinbüchel A. Poly(3-hydroxybutyrate) granule-associated proteins: impacts on poly(3-hydroxybutyrate) synthesis and degradation. Biomacromolecules, 2005, 6: 552-560.
    • (2005) Biomacromolecules , vol.6 , pp. 552-560
    • Pötter, M.1    Steinbüchel, A.2
  • 105
    • 0036136119 scopus 로고    scopus 로고
    • The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production
    • York G M, Stubbe J, Sinskey A J. The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production. J Bacteriol, 2002, 184: 59-66.
    • (2002) J Bacteriol , vol.184 , pp. 59-66
    • York, G.M.1    Stubbe, J.2    Sinskey, A.J.3
  • 107
    • 33846273815 scopus 로고    scopus 로고
    • S-layers as a tool kit for nanobiotechnological applications
    • Sleytr U B, Huber C, Ilk N, et al. S-layers as a tool kit for nanobiotechnological applications. FEMS Microbiol Lett, 2007, 267: 131-144.
    • (2007) FEMS Microbiol Lett , vol.267 , pp. 131-144
    • Sleytr, U.B.1    Huber, C.2    Ilk, N.3
  • 108
    • 33846006521 scopus 로고    scopus 로고
    • S-Layers as a basic building block in a molecular construction kit
    • Sleytr U B, Egelseer E M, Ilk N, et al. S-Layers as a basic building block in a molecular construction kit. FEBS J, 2007, 274: 323-334.
    • (2007) FEBS J , vol.274 , pp. 323-334
    • Sleytr, U.B.1    Egelseer, E.M.2    Ilk, N.3
  • 109
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: structure-function relationships and their biotechnological applications
    • Sleytr U B, Sára M. Bacterial and archaeal S-layer proteins: structure-function relationships and their biotechnological applications. Trends Biotechnol, 1997, 15: 20-26.
    • (1997) Trends Biotechnol , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sára, M.2
  • 110
    • 4444231397 scopus 로고    scopus 로고
    • Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology
    • Schäffer C, Messner P. Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology. Glycobiology, 2004, 14: 31R-42R.
    • (2004) Glycobiology , vol.14
    • Schäffer, C.1    Messner, P.2
  • 111
    • 69249206640 scopus 로고    scopus 로고
    • Composite S-layer lipid structures
    • Schuster B, Sleytr U B. Composite S-layer lipid structures. J Struct Biol, 2009, 168: 207-216.
    • (2009) J Struct Biol , vol.168 , pp. 207-216
    • Schuster, B.1    Sleytr, U.B.2
  • 112
    • 0000606175 scopus 로고    scopus 로고
    • Biomolecular electronics: Protein-based associative processors and volumetric memories
    • Birge R R, Gillespie N B, Izaguirre E W, et al. Biomolecular electronics: Protein-based associative processors and volumetric memories. J Phys Chem B, 1999, 103: 10746-10766.
    • (1999) J Phys Chem B , vol.103 , pp. 10746-10766
    • Birge, R.R.1    Gillespie, N.B.2    Izaguirre, E.W.3
  • 113
    • 0037177177 scopus 로고    scopus 로고
    • Volumetric optical memory based on bacteriorhodopsin
    • Stuart J A, Marcy D L, Wise K J, et al. Volumetric optical memory based on bacteriorhodopsin. Synthetic Met, 2002, 127: 3-15.
    • (2002) Synthetic Met , vol.127 , pp. 3-15
    • Stuart, J.A.1    Marcy, D.L.2    Wise, K.J.3
  • 114
    • 1042298973 scopus 로고    scopus 로고
    • Photoelectric response of polarization sensitive bacteriorhodopsin films
    • Li Q, Stuart J A, Birge R R, et al. Photoelectric response of polarization sensitive bacteriorhodopsin films. Biosens Bioelectron, 2004, 19: 869-874.
    • (2004) Biosens Bioelectron , vol.19 , pp. 869-874
    • Li, Q.1    Stuart, J.A.2    Birge, R.R.3
  • 115
    • 0029136828 scopus 로고
    • Protein-based computers
    • Birge R R. Protein-based computers. Sci Am, 1995, 272: 90-95.
    • (1995) Sci Am , vol.272 , pp. 90-95
    • Birge, R.R.1
  • 116
    • 77954882764 scopus 로고    scopus 로고
    • Sensory systems: Back into the light
    • doi: 10. 1038/nrn2893
    • Bodo C. Sensory systems: Back into the light. Nat Rev Neurosci, 2010, 11, doi: 10. 1038/nrn2893.
    • (2010) Nat Rev Neurosci , vol.11
    • Bodo, C.1
  • 117
    • 77954847711 scopus 로고    scopus 로고
    • Genetic reactivation of cone photoreceptors restores visual responses in retinitis pigmentosa
    • Busskamp V, Duebel J, Balya D, et al. Genetic reactivation of cone photoreceptors restores visual responses in retinitis pigmentosa. Science, 2010, 329: 413-417.
    • (2010) Science , vol.329 , pp. 413-417
    • Busskamp, V.1    Duebel, J.2    Balya, D.3
  • 118
    • 77954847056 scopus 로고    scopus 로고
    • Neuroscience. Seeing the light of day
    • Cepko C. Neuroscience. Seeing the light of day. Science, 2010, 329: 403-404.
    • (2010) Science , vol.329 , pp. 403-404
    • Cepko, C.1
  • 119
    • 0024802898 scopus 로고
    • Gas vesicle proteins
    • Walsby A E, Hayes P K. Gas vesicle proteins. Biochem J, 1989, 264: 313-322.
    • (1989) Biochem J , vol.264 , pp. 313-322
    • Walsby, A.E.1    Hayes, P.K.2
  • 120
    • 0035876714 scopus 로고    scopus 로고
    • Antigen presentation using novel particulate organelles from halophilic archaea
    • Stuart E S, Morshed F, Sremac M, et al. Antigen presentation using novel particulate organelles from halophilic archaea. J Biotechnol, 2001, 88: 119-128.
    • (2001) J Biotechnol , vol.88 , pp. 119-128
    • Stuart, E.S.1    Morshed, F.2    Sremac, M.3
  • 121
    • 7444250349 scopus 로고    scopus 로고
    • Cassette-based presentation of SIV epitopes with recombinant gas vesicles from halophilic archaea
    • Stuart E S, Morshed F, Sremac M, et al. Cassette-based presentation of SIV epitopes with recombinant gas vesicles from halophilic archaea. J Biotechnol, 2004, 114: 225-237.
    • (2004) J Biotechnol , vol.114 , pp. 225-237
    • Stuart, E.S.1    Morshed, F.2    Sremac, M.3
  • 122
    • 41249093449 scopus 로고    scopus 로고
    • Recombinant gas vesicles from Halobacterium sp. displaying SIV peptides demonstrate biotechnology potential as a pathogen peptide delivery vehicle
    • Sremac M, Stuart E S. Recombinant gas vesicles from Halobacterium sp. displaying SIV peptides demonstrate biotechnology potential as a pathogen peptide delivery vehicle. BMC Biotechnol, 2008, 8: 9.
    • (2008) BMC Biotechnol , vol.8 , pp. 9
    • Sremac, M.1    Stuart, E.S.2
  • 123
    • 22544467008 scopus 로고    scopus 로고
    • The application of polyhydroxyalkanoates as tissue engineering materials
    • Chen G Q, Wu Q. The application of polyhydroxyalkanoates as tissue engineering materials. Biomaterials, 2005, 26: 6565-6578.
    • (2005) Biomaterials , vol.26 , pp. 6565-6578
    • Chen, G.Q.1    Wu, Q.2
  • 124
    • 33748368301 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate (PHA)/inorganic phase composites for tissue engineering applications
    • Misra S K, Valappil S P, Roy I, et al. Polyhydroxyalkanoate (PHA)/inorganic phase composites for tissue engineering applications. Biomacromolecules, 2006, 7: 2249-2258.
    • (2006) Biomacromolecules , vol.7 , pp. 2249-2258
    • Misra, S.K.1    Valappil, S.P.2    Roy, I.3
  • 125
    • 0033996295 scopus 로고    scopus 로고
    • Fabrication of a trileaflet heart valve scaffold from a polyhydroxyalkanoate biopolyester for use in tissue engineering
    • Sodian R, Sperling J S, Martin D P, et al. Fabrication of a trileaflet heart valve scaffold from a polyhydroxyalkanoate biopolyester for use in tissue engineering. Tissue Eng, 2000, 6: 183-188.
    • (2000) Tissue Eng , vol.6 , pp. 183-188
    • Sodian, R.1    Sperling, J.S.2    Martin, D.P.3
  • 126
    • 0032967705 scopus 로고    scopus 로고
    • PHA applications: Addressing the price performance issue I. Tissue engineering
    • Williams S F, Martin D P, Horowitz D M, et al. PHA applications: Addressing the price performance issue I. Tissue engineering. Int J Biol Macromol, 1999, 25: 111-121.
    • (1999) Int J Biol Macromol , vol.25 , pp. 111-121
    • Williams, S.F.1    Martin, D.P.2    Horowitz, D.M.3
  • 127
    • 33644961915 scopus 로고    scopus 로고
    • In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase
    • Peters V, Rehm B H A. In vivo enzyme immobilization by use of engineered polyhydroxyalkanoate synthase. Appl Environ Microb, 2006, 72: 1777-1783.
    • (2006) Appl Environ Microb , vol.72 , pp. 1777-1783
    • Peters, V.1    Rehm, B.H.A.2
  • 128
    • 33751001776 scopus 로고    scopus 로고
    • Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification
    • Brockelbank J A, Peters V, Rehm B H A. Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification. Appl Environ Microb, 2006, 72: 7394-7397.
    • (2006) Appl Environ Microb , vol.72 , pp. 7394-7397
    • Brockelbank, J.A.1    Peters, V.2    Rehm, B.H.A.3
  • 129
    • 38949135957 scopus 로고    scopus 로고
    • In vivo production of scFv-Displaying biopolymer beads using a self-assembly-promoting fusion partner
    • Grage K, Rehm B H A. In vivo production of scFv-Displaying biopolymer beads using a self-assembly-promoting fusion partner. Bioconjugate Chem, 2008, 19: 254-262.
    • (2008) Bioconjugate Chem , vol.19 , pp. 254-262
    • Grage, K.1    Rehm, B.H.A.2
  • 130
    • 41549140412 scopus 로고    scopus 로고
    • Protein engineering of streptavidin for in vivo assembly of streptavidin beads
    • Peters V, Rehm B H A. Protein engineering of streptavidin for in vivo assembly of streptavidin beads. J Biotechnol, 2008, 134: 266-274.
    • (2008) J Biotechnol , vol.134 , pp. 266-274
    • Peters, V.1    Rehm, B.H.A.2
  • 131
    • 55249108919 scopus 로고    scopus 로고
    • Multifunctional inorganic-binding beads self-assembled inside engineered bacteria
    • Jahns A C, Haverkamp R G, Rehm B H A. Multifunctional inorganic-binding beads self-assembled inside engineered bacteria. Bioconjugate Chem, 2008, 19: 2072-2080.
    • (2008) Bioconjugate Chem , vol.19 , pp. 2072-2080
    • Jahns, A.C.1    Haverkamp, R.G.2    Rehm, B.H.A.3
  • 132
    • 28144460981 scopus 로고    scopus 로고
    • Inteins and affinity resin substitutes for protein purification and scale up
    • Banki M R, Wood D W. Inteins and affinity resin substitutes for protein purification and scale up. Microb Cell Fact, 2005, 4: 32.
    • (2005) Microb Cell Fact , vol.4 , pp. 32
    • Banki, M.R.1    Wood, D.W.2
  • 133
    • 0025226099 scopus 로고
    • Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates
    • Anderson A J, Dawes E A. Occurrence, metabolism, metabolic role, and industrial uses of bacterial polyhydroxyalkanoates. Microbiol Rev, 1990, 54: 450-472.
    • (1990) Microbiol Rev , vol.54 , pp. 450-472
    • Anderson, A.J.1    Dawes, E.A.2
  • 134
    • 24644468575 scopus 로고    scopus 로고
    • Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads
    • Lee S J, Park J P, Park T J, et al. Selective immobilization of fusion proteins on poly(hydroxyalkanoate) microbeads. Anal Chem, 2005, 77: 5755-5759.
    • (2005) Anal Chem , vol.77 , pp. 5755-5759
    • Lee, S.J.1    Park, J.P.2    Park, T.J.3
  • 135
    • 22444444258 scopus 로고    scopus 로고
    • Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
    • Banki M R, Gerngross T U, Wood D W. Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Sci, 2005, 14: 1387-1395.
    • (2005) Protein Sci , vol.14 , pp. 1387-1395
    • Banki, M.R.1    Gerngross, T.U.2    Wood, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.