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Volumn 16, Issue 2, 2011, Pages 203-218

Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria

Author keywords

Cold adaptation; Extremophiles; Heat shock protein 90; High temperature protein G; HSP90; HTPG; Protein interactions; Psychrophiles

Indexed keywords

ALCOHOL DEHYDROGENASE; HEAT SHOCK PROTEIN 90; ISOCITRATE LYASE; MALATE DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; SUCCINYL COENZYME A SYNTHETASE;

EID: 79951672952     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-010-0233-7     Document Type: Article
Times cited : (34)

References (48)
  • 1
    • 1242291827 scopus 로고    scopus 로고
    • Direct Colorimetric Assay for Rapid Detection of Rifampin-Resistant Mycobacterium tuberculosis
    • DOI 10.1128/JCM.42.2.871-873.2004
    • G Abate A Aseffa A Selassie S Goshu B Fekade D WoldeMeskal H Miörner 2004 Direct colorimetric assay for rapid detection of rifampicin-resistant Mycobacterium tuberculosis J Clin Microbiol 42 871 873 10.1128/JCM.42.2.871-873. 2004 1:CAS:528:DC%2BD2cXit1Sku78%3D 10.1128/JCM.42.2.871-873.2004 14766876 (Pubitemid 38222685)
    • (2004) Journal of Clinical Microbiology , vol.42 , Issue.2 , pp. 871-873
    • Abate, G.1    Aseffa, A.2    Selassie, A.3    Goshu, S.4    Fekade, B.5    WoldeMeskal, D.6    Miorner, H.7
  • 2
    • 33646113855 scopus 로고    scopus 로고
    • Evolutionary dynamics of prokaryotic transcriptional regulatory networks
    • 10.1016/j.jmb.2006.02.019 10.1016/j.jmb.2006.02.019
    • MM Babu SA Teichmann L Aravind 2006 Evolutionary dynamics of prokaryotic transcriptional regulatory networks J Mol Biol 358 614 633 10.1016/j.jmb.2006. 02.019 10.1016/j.jmb.2006.02.019
    • (2006) J Mol Biol , vol.358 , pp. 614-633
    • Babu, M.M.1    Teichmann, S.A.2    Aravind, L.3
  • 3
    • 0024044382 scopus 로고
    • Ancient heat shock gene is dispensable
    • 1:CAS:528:DyaL1cXkvVOitbc%3D 3290192
    • JC Bardwell EA Craig 1988 Ancient heat shock gene is dispensable J Bacteriol 170 2977 2983 1:CAS:528:DyaL1cXkvVOitbc%3D 3290192
    • (1988) J Bacteriol , vol.170 , pp. 2977-2983
    • Bardwell, J.C.1    Craig, E.A.2
  • 6
    • 0037693813 scopus 로고    scopus 로고
    • Prokaryotic metabolic activity and community structure in antarctic continental shelf sediments
    • DOI 10.1128/AEM.69.5.2448-2462.2003
    • JP Bowman SA McCammon JA Gibson L Robertson PD Nichols 2003 Prokaryotic metabolic activity and community structure in Antarctic continental shelf sediments Appl Environ Microbiol 69 2448 2462 10.1128/AEM.69.5.2448-2462.2003 1:CAS:528:DC%2BD3sXjslOlsr8%3D 10.1128/AEM.69.5.2448-2462.2003 12732510 (Pubitemid 36560318)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.5 , pp. 2448-2462
    • Bowman, J.P.1    McCammon, S.A.2    Gibson, J.A.E.3    Robertson, L.4    Nichols, P.D.5
  • 8
    • 0242657566 scopus 로고    scopus 로고
    • Diversity and Structure of Bacterial Communities in Arctic versus Antarctic Pack Ice
    • DOI 10.1128/AEM.69.11.6610-6619.2003
    • R Brinkmeyer K Knittel J Jurgens H Weyland R Amann E Helmke 2003 Diversity and structure of bacterial communities in Arctic versus Antarctic pack ice Appl Environ Microbiol 9 6610 6619 10.1128/AEM.69.11.6610-6619.2003 10.1128/AEM.69.11.6610-6619.2003 (Pubitemid 37420197)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.11 , pp. 6610-6619
    • Brinkmeyer, R.1    Knittel, K.2    Jurgens, J.3    Weyland, H.4    Amann, R.5    Helmke, E.6
  • 9
    • 0017888519 scopus 로고
    • Effects of low temperature on in vivo and in vitro protein synthesis in Escherichia coli and Pseudomonas fluorescens
    • RJ Broeze CJ Solomon DH Pope 1978 Effects of low temperature on in vivo and in vitro protein synthesis in Escherichia coli and Pseudomonas fluorescens J Bacteriol 134 861 874 1:CAS:528:DyaE1cXkvVOjurk%3D 96102 (Pubitemid 8360896)
    • (1978) Journal of Bacteriology , vol.134 , Issue.3 , pp. 861-874
    • Broeze, R.J.1    Solomon, C.J.2    Pope, D.H.3
  • 10
    • 33746660802 scopus 로고    scopus 로고
    • Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
    • DOI 10.1186/1471-2164-7-156
    • B Chen D Zhong A Monteiro 2006 Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms BMC Genomics 7 156 10.1186/1471-2164-7-156 10.1186/1471-2164-7-156 16780600 (Pubitemid 44151610)
    • (2006) BMC Genomics , vol.7 , pp. 156
    • Chen, B.1    Zhong, D.2    Monteiro, A.3
  • 11
    • 1442314697 scopus 로고    scopus 로고
    • Antibodies reactive to heat shock protein 90 induce oligodendrocyte precursor cell death in culture. Implications for demyelination in multiple sclerosis
    • 10.1096/fj.03-0606fje 1:CAS:528:DC%2BD2cXht1GitL4%3D 14688203
    • C Cid JC Alvarez-Cermeno E Camafeita M Salinas A Alcazar 2004 Antibodies reactive to heat shock protein 90 induce oligodendrocyte precursor cell death in culture. Implications for demyelination in multiple sclerosis FASEB J 18 409 411 10.1096/fj.03-0606fje 1:CAS:528:DC%2BD2cXht1GitL4%3D 14688203
    • (2004) FASEB J , vol.18 , pp. 409-411
    • Cid, C.1    Alvarez-Cermeno, J.C.2    Camafeita, E.3    Salinas, M.4    Alcazar, A.5
  • 12
    • 33845865788 scopus 로고    scopus 로고
    • Detection of anti-heat shock protein 90 β (Hsp90β) antibodies in cerebrospinal fluid
    • DOI 10.1016/j.jim.2006.09.017, PII S0022175906002705
    • C Cid M Garcia-Villanueva M Salinas A Alcazar 2007 Detection of anti-heat shock protein 90 beta (Hsp90beta) antibodies in cerebrospinal fluid J Immunol Methods 318 153 157 10.1016/j.jim.2006.09.017 1:CAS:528:DC%2BD2sXisVKhsQ%3D%3D 10.1016/j.jim.2006.09.017 17112536 (Pubitemid 46026804)
    • (2007) Journal of Immunological Methods , vol.318 , Issue.1-2 , pp. 153-157
    • Cid, C.1    Garcia-Villanueva, M.2    Salinas, M.3    Alcazar, A.4
  • 13
    • 34748925236 scopus 로고    scopus 로고
    • Proteomic characterization of protein phosphatase 1 complexes in ischemia-reperfusion and ischemic tolerance
    • DOI 10.1002/pmic.200700214
    • C Cid L Garcia-Bonilla E Camafeita J Burda M Salinas A Alcazar 2007 Proteomic characterization of protein phosphatase one complexes in ischemia-reperfusion and ischemic tolerance Proteomics 7 3207 3218 bip.21292/pmic.200700214 1:CAS:528:DC%2BD2sXhtFSkt7zL 10.1002/pmic.200700214 17683050 (Pubitemid 47477962)
    • (2007) Proteomics , vol.7 , Issue.17 , pp. 3207-3218
    • Cid, C.1    Garcia-Bonilla, L.2    Camafeita, E.3    Burda, J.4    Salinas, M.5    Alcazar, A.6
  • 14
    • 77952334099 scopus 로고    scopus 로고
    • Proteomic analysis of the response of an acidophilic strain of Chlamydomonas sp. (Chlorophyta) to natural metal-rich water
    • bip.21292/pmic.200900592 10.1002/pmic.200900592
    • C Cid L Garcia-Descalzo V Casado-Lafuente R Amils A Aguilera 2010 Proteomic analysis of the response of an acidophilic strain of Chlamydomonas sp. (Chlorophyta) to natural metal-rich water Proteomics 10 1 11 bip.21292/pmic.200900592 10.1002/pmic.200900592
    • (2010) Proteomics , vol.10 , pp. 1-11
    • Cid, C.1    Garcia-Descalzo, L.2    Casado-Lafuente, V.3    Amils, R.4    Aguilera, A.5
  • 15
    • 29244479192 scopus 로고    scopus 로고
    • Degradation of crude oil by an arctic microbial consortium
    • DOI 10.1007/s00792-005-0463-2
    • U Deppe HH Richnow W Michaelis G Antranikian 2005 Degradation of crude oil by an arctic microbial consortium Extremophiles 9 461 470 10.1007/s00792-005-0463-2 10.1007/s00792-005-0463-2 15999222 (Pubitemid 41831054)
    • (2005) Extremophiles , vol.9 , Issue.6 , pp. 461-470
    • Deppe, U.1    Richnow, H.-H.2    Michaelis, W.3    Antranikian, G.4
  • 16
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • O Fayet T Ziegelhoffer C Georgopoulos 1989 The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures J Bacteriol 171 1379 1385 1:CAS:528:DyaL1MXhs1OjtL8%3D 2563997 (Pubitemid 19080775)
    • (1989) Journal of Bacteriology , vol.171 , Issue.3 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 18
    • 1642580810 scopus 로고    scopus 로고
    • Preferential translation of cold-shock mRNAs during cold adaptation
    • DOI 10.1261/rna.5164904
    • AM Giuliodori A Brandi CO Gualerzi CL Pon 2004 Preferential translation of cold-shock mRNAs during cold adaptation RNA 10 265 276 10.1261/rna.5164904 1:CAS:528:DC%2BD2cXpsVShsA%3D%3D 10.1261/rna.5164904 14730025 (Pubitemid 38129831)
    • (2004) RNA , vol.10 , Issue.2 , pp. 265-276
    • Giuliodori, A.M.1    Brandi, A.2    Gualerzi, C.O.3    Pon, C.L.4
  • 19
    • 34447537991 scopus 로고    scopus 로고
    • Cold-stress-induced de novo expression of infC and role of IF3 in cold-shock translational bias
    • DOI 10.1261/rna.455607
    • AM Giuliodori A Brandi M Giangrossi CO Gualerzi CL Pon 2007 Cold-stress-induced de novo expression of infC and role of IF3 in cold-shock translational bias RNA 13 1355 1365 10.1261/rna.455607 1:CAS:528: DC%2BD2sXos1Ghsbo%3D 10.1261/rna.455607 17592046 (Pubitemid 47080479)
    • (2007) RNA , vol.13 , Issue.8 , pp. 1355-1365
    • Giuliodori, A.M.1    Brandi, A.2    Giangrossi, M.3    Gualerzi, C.O.4    Pon, C.L.5
  • 20
    • 12144289622 scopus 로고    scopus 로고
    • Functional refolding of the Campylobacter jejuni MOMP (major outer membrane protein) porin by GroEL from the same species
    • DOI 10.1042/BJ20031239
    • F Goulhen E De JM Pages JM Bolla 2004 Functional refolding of the Campylobacter jejuni MOMP (major outer membrane protein) porin by GroEL from the same species Biochem J 378 851 856 10.1042/BJ20031239 1:CAS:528: DC%2BD2cXisVyktLo%3D 10.1042/BJ20031239 14662009 (Pubitemid 38406862)
    • (2004) Biochemical Journal , vol.378 , Issue.3 , pp. 851-856
    • Goulhen, F.1    De, E.2    Pages, J.-M.3    Bolla, J.-M.4
  • 21
    • 0017358326 scopus 로고
    • Effects of temperature on the macromolecular composition and fine structure of psychrophilic Arthrobacter species
    • AM Gounot TJ Novitsky DJ Kushner 1977 Effects of temperature on the macromolecular composition and find structure of psychrophilic Arthrobacter species Can J Microbiol 23 357 362 1:CAS:528:DyaE2sXltFCgu7w%3D 10.1139/m77-053 856424 (Pubitemid 8078254)
    • (1977) Canadian Journal of Microbiology , vol.23 , Issue.3 , pp. 357-362
    • Gounot, A.M.1    Novitsky, T.J.2    Kushner, D.J.3
  • 22
    • 0037040541 scopus 로고    scopus 로고
    • Protein folding. Molecular chaperones in the cytosol: From nascent chain to folded protein
    • DOI 10.1126/science.1068408
    • FU Hartl M Hayer-Hartl 2002 Molecular chaperones in the cytosol: from nascent chain to folded protein Science 295 1852 1858 10.1126/science.1068408 1:CAS:528:DC%2BD38XhvFClsL4%3D 10.1126/science.1068408 11884745 (Pubitemid 34214115)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 24
    • 0036549167 scopus 로고    scopus 로고
    • HtpG plays a role in cold acclimation in cyanobacteria
    • DOI 10.1007/s00284-001-0005-9
    • MM Hossain H Nakamoto 2002 HtpG plays a role in cold acclimation in cyanobacteria Curr Microbiol 44 291 296 10.1007/s00284-001-0005-9 1:CAS:528:DC%2BD38Xhs1yrurs%3D 10.1007/s00284-001-0005-9 11910501 (Pubitemid 36929652)
    • (2002) Current Microbiology , vol.44 , Issue.4 , pp. 291-296
    • Hossain, M.1    Nakamoto, H.2
  • 25
    • 0033547324 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the chaperonin GroEL
    • 10.1038/45977 1:CAS:528:DyaK1MXnsVeksrw%3D 10.1038/45977 10647006
    • WA Houry D Frishman C Eckerskorn F Lottspeich FU Hartl 1999 Identification of in vivo substrates of the chaperonin GroEL Nature 402 147 154 10.1038/45977 1:CAS:528:DyaK1MXnsVeksrw%3D 10.1038/45977 10647006
    • (1999) Nature , vol.402 , pp. 147-154
    • Houry, W.A.1    Frishman, D.2    Eckerskorn, C.3    Lottspeich, F.4    Hartl, F.U.5
  • 26
    • 0024713012 scopus 로고
    • Growth and activity of Shewanella putrefaciens isolated from spoiling fish
    • 10.1016/0168-1605(89)90037-8 1:STN:280:DyaK3czltFyrsw%3D%3D 10.1016/0168-1605(89)90037-8 2641275
    • BR Jorgensen HH Huss 1989 Growth and activity of Shewanella putrefaciens isolated from spoiling fish Int J Food Microbiol 9 51 62 10.1016/0168-1605(89) 90037-8 1:STN:280:DyaK3czltFyrsw%3D%3D 10.1016/0168-1605(89)90037-8 2641275
    • (1989) Int J Food Microbiol , vol.9 , pp. 51-62
    • Jorgensen, B.R.1    Huss, H.H.2
  • 28
    • 3442885854 scopus 로고    scopus 로고
    • Small heat shock proteins from extremophiles: A review
    • DOI 10.1007/s00792-003-0362-3
    • P Laksanalamai FT Robb 2004 Small heat shock proteins from extremophiles: a review Extremophiles 8 1 11 10.1007/s00792-003-0362-3 1:CAS:528: DC%2BD2cXos1erug%3D%3D 10.1007/s00792-003-0362-3 15064984 (Pubitemid 40882696)
    • (2004) Extremophiles , vol.8 , Issue.1 , pp. 1-11
    • Laksanalamai, P.1    Robb, F.T.2
  • 29
    • 0034117339 scopus 로고    scopus 로고
    • Characterization of heat-inducible expression and cloning of HtpG (Hsp90 homologue) of Porphyromonas gingivalis
    • DOI 10.1128/IAI.68.4.1980-1987.2000
    • DE Lopatin A Combs DG Sweier JC Fenno S Dhamija 2000 Characterization of heat-inducible expression and cloning of HtpG (Hsp90 homologue) of Porphyromonas gingivalis Infect Immun 68 1980 1987 1:CAS:528:DC%2BD3cXitFemtbc%3D 10.1128/IAI.68.4.1980-1987.2000 10722592 (Pubitemid 30164827)
    • (2000) Infection and Immunity , vol.68 , Issue.4 , pp. 1980-1987
    • Lopatin, D.E.1    Combs, A.2    Sweier, D.G.3    Fenno, J.C.4    Dhamija, S.5
  • 30
    • 7044222207 scopus 로고    scopus 로고
    • Dissimilatory Fe(III) and Mn(IV) reduction
    • DOI 10.1016/S0065-2911(04)49005-5, PII S0065291104490055
    • D Lovley DE Holmes KP Nevin 2004 Dissimilatory Fe (III) and Mn (IV) reduction Adv Microb Physiol 49 219 286 10.1016/S0065-2911(04)49005-5 1:CAS:528:DC%2BD2cXhtVaksrrE 10.1016/S0065-2911(04)49005-5 15518832 (Pubitemid 39424008)
    • (2004) Advances in Microbial Physiology , vol.49 , pp. 219-286
    • Lovley, D.R.1    Holmes, D.E.2    Nevin, K.P.3
  • 31
    • 33644863337 scopus 로고    scopus 로고
    • Genomic comparisons among gamma-proteobacteria
    • 10.1111/j.1462-2920.2005.00894.x 16423015
    • J Mrázek AM Spormann S Karlin 2006 Genomic comparisons among gamma-proteobacteria Environ Microbiol 8 273 288 10.1111/j.1462-2920.2005.00894. x 16423015
    • (2006) Environ Microbiol , vol.8 , pp. 273-288
    • Mrázek, J.1    Spormann, A.M.2    Karlin, S.3
  • 32
    • 18644375051 scopus 로고    scopus 로고
    • Distinctions in adenylate metabolism among organisms inhabiting temperature extremes
    • DOI 10.1007/s00792-004-0424-1
    • MJ Napolitano DH Shain 2005 Distinctions in adenylate metabolism among organisms inhabiting temperature extremes Extremophiles 9 93 98 10.1007/s00792-004-0424-1 1:CAS:528:DC%2BD2MXjtlKqtL0%3D 10.1007/s00792-004- 0424-1 15490283 (Pubitemid 40660348)
    • (2005) Extremophiles , vol.9 , Issue.2 , pp. 93-98
    • Napolitano, M.J.1    Shain, D.H.2
  • 33
    • 0141532929 scopus 로고    scopus 로고
    • Changes in Escherichia coli transcriptome during acclimatization at low temperature
    • DOI 10.1016/S0923-2508(03)00167-0
    • A Polissi W De Laurentis S Zangrossi F Briani V Longhi G Pesole G Deho 2003 Changes in Escherichia coli transcriptome during acclimatization at low temperature Res Microbiol 154 573 580 10.1016/S0923-2508(03)00167-0 1:CAS:528:DC%2BD3sXns12ks78%3D 10.1016/S0923-2508(03)00167-0 14527658 (Pubitemid 37177001)
    • (2003) Research in Microbiology , vol.154 , Issue.8 , pp. 573-580
    • Polissi, A.1    De Laurentis, W.2    Zangrossi, S.3    Briani, F.4    Longhi, V.5    Pesole, G.6    Deho, G.7
  • 34
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • DOI 10.1016/S0092-8674(00)80314-1
    • C Prodromou SM Roe R O'Brien JE Ladbury PW Piper LH Pearl 1997 Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone Cell 90 65 75 10.1016/S0092-8674(00)80314-1 1:CAS:528:DyaK2sXkslShtLc%3D 10.1016/S0092-8674(00)80314-1 9230303 (Pubitemid 28009419)
    • (1997) Cell , vol.90 , Issue.1 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 35
    • 0022386726 scopus 로고
    • Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species
    • DOI 10.1021/bi00344a042
    • RM Riehl WP Sullivan BT Vroman VJ Bauer GR Pearson DO Toft 1985 Immunological evidence that the nonhormone binding component of avian steroid receptors exists in a wide range of tissues and species Biochemistry 24 6586 6591 1:CAS:528:DyaL2MXlvFemtLs%3D 10.1021/bi00344a042 4084541 (Pubitemid 16207135)
    • (1985) Biochemistry , vol.24 , Issue.23 , pp. 6586-6591
    • Riehl, R.M.1    Sullivan, W.P.2    Vroman, B.T.3
  • 36
    • 0025528744 scopus 로고
    • Cold adaptation of microorganisms
    • 10.1098/rstb.1990.0034 1:CAS:528:DyaK3cXhslGgsrs%3D 10.1098/rstb.1990. 0034 1969649
    • NJ Russell 1990 Cold adaptation of microorganisms Philos Trans R Soc Lond B Biol Sci 326 595 608 10.1098/rstb.1990.0034 1:CAS:528:DyaK3cXhslGgsrs%3D 10.1098/rstb.1990.0034 1969649
    • (1990) Philos Trans R Soc Lond B Biol Sci , vol.326 , pp. 595-608
    • Russell, N.J.1
  • 37
    • 0037379626 scopus 로고    scopus 로고
    • Between genotype and phenotype: Protein chaperones and evolvability
    • DOI 10.1038/nrg1041
    • SL Rutherford 2003 Between genotype and phenotype: protein chaperones and evolvability Nat Rev Genet 4 263 274 10.1038/nrg1041 1:CAS:528: DC%2BD3sXisFWqsL4%3D 10.1038/nrg1041 12671657 (Pubitemid 36389531)
    • (2003) Nature Reviews Genetics , vol.4 , Issue.4 , pp. 263-274
    • Rutherford, S.L.1
  • 38
    • 0015080074 scopus 로고
    • The microbiology of fish and fishery products-a progress report
    • 1:STN:280:DyaE38%2Fit1GrtQ%3D%3D 4939266
    • JM Shewan 1971 The microbiology of fish and fishery products-a progress report J Appl Bacteriol 34 299 315 1:STN:280:DyaE38%2Fit1GrtQ%3D%3D 4939266
    • (1971) J Appl Bacteriol , vol.34 , pp. 299-315
    • Shewan, J.M.1
  • 39
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • CE Stebbins AA Russo C Schneider N Rosen FU Hartl NP Pavletich 1997 Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent Cell 89 239 250 10.1016/S0092-8674(00)80203-2 1:CAS:528:DyaK2sXislCitLo%3D 10.1016/S0092-8674(00)80203-2 9108479 (Pubitemid 27199896)
    • (1997) Cell , vol.89 , Issue.2 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 40
    • 31344476293 scopus 로고    scopus 로고
    • Low temperature-induced systems failure in Escherichia coli: Insights from rescue by cold-adapted chaperones
    • DOI 10.1002/pmic.200500031
    • M Strocchi M Ferrer KN Timmis PN Golyshin 2006 Low temperature-induced systems failure in Escherichia coli: insights from rescue by cold-adapted chaperones Proteomics 6 193 206 bip.21292/pmic.200500031 1:CAS:528: DC%2BD28XpsVSisQ%3D%3D 10.1002/pmic.200500031 16302275 (Pubitemid 43142945)
    • (2006) Proteomics , vol.6 , Issue.1 , pp. 193-206
    • Strocchi, M.1    Ferrer, M.2    Timmis, K.N.3    Golyshin, P.N.4
  • 41
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • K Tamura J Dudley M Nei S Kumar 2007 MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0 Mol Biol Evol 24 1596 1599 10.1093/molbev/msm092 1:CAS:528:DC%2BD2sXpsVGrsL8%3D 10.1093/molbev/msm092 17488738 (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 42
    • 0032840055 scopus 로고    scopus 로고
    • HtpG is essential for the thermal stress management in cyanobacteria
    • DOI 10.1016/S0014-5793(99)01134-5, PII S0014579399011345
    • N Tanaka H Nakamoto 1999 HtpG is essential for the thermal stress management in cyanobacteria FEBS Lett 458 117 123 10.1016/S0014-5793(99)01134-5 1:CAS:528:DyaK1MXlvVCgtr0%3D 10.1016/S0014-5793(99)01134-5 10481048 (Pubitemid 29428166)
    • (1999) FEBS Letters , vol.458 , Issue.2 , pp. 117-123
    • Tanaka, N.1    Nakamoto, H.2
  • 43
    • 0033045319 scopus 로고    scopus 로고
    • The Bacillus subtilis htpG gene is not involved in thermal stress management
    • DOI 10.1007/s004380051004
    • S Versteeg A Mogk W Schumann 1999 The Bacillus subtilis htpG gene is not involved in thermal stress management Mol Gen Genet 261 582 588 1:CAS:528:DyaK1MXjsFCmsLo%3D 10.1007/s004380051004 10323241 (Pubitemid 29185051)
    • (1999) Molecular and General Genetics , vol.261 , Issue.3 , pp. 582-588
    • Versteeg, S.1    Mogk, A.2    Schumann, W.3
  • 44
    • 0037224322 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis heat shock gene htpG is under positive control
    • DOI 10.1128/JB.185.2.466-474.2003
    • S Versteeg A Escher A Wende T Wiegert W Schumann 2003 Regulation of the Bacillus subtilis heat shock gene htpG is under positive control J Bacteriol 185 466 474 10.1128/JB.185.2.466-474.2003 1:CAS:528:DC%2BD3sXksl2lsA%3D%3D 10.1128/JB.185.2.466-474.2003 12511492 (Pubitemid 36070472)
    • (2003) Journal of Bacteriology , vol.185 , Issue.2 , pp. 466-474
    • Versteeg, S.1    Escher, A.2    Wende, A.3    Wiegert, T.4    Schumann, W.5
  • 45
    • 1642351870 scopus 로고    scopus 로고
    • Chaperone networks in bacteria: Analysis of protein homeostasis in minimal cells
    • DOI 10.1016/j.jsb.2003.11.006, PII S1047847703002533
    • P Wong WA Houry 2004 Chaperone networks in bacteria: analysis of protein homeostasis in minimal cells J Struct Biol 146 79 89 10.1016/j.jsb.2003.11.006 1:CAS:528:DC%2BD2cXisVSmtrc%3D 10.1016/j.jsb.2003.11.006 15037239 (Pubitemid 38369020)
    • (2004) Journal of Structural Biology , vol.146 , Issue.1-2 , pp. 79-89
    • Wong, P.1    Houry, W.A.2
  • 46
    • 21244474057 scopus 로고    scopus 로고
    • Gene structure and transcriptional regulation of dnaK and dnaJ genes from a psychrophilic bacterium, Colwellia maris
    • DOI 10.1007/s00792-004-0387-2
    • S Yamauchi H Okuyama Y Nishiyama H Hayashi 2004 Gene structure and transcriptional regulation of dnaK and dnaJ genes from a psychrophilic bacterium, Colwellia maris Extremophiles 8 283 290 10.1007/s00792-004-0387-2 1:CAS:528:DC%2BD2cXmsVChtbg%3D 10.1007/s00792-004-0387-2 15085417 (Pubitemid 40882689)
    • (2004) Extremophiles , vol.8 , Issue.4 , pp. 283-290
    • Yamauchi, S.1    Okuyama, H.2    Nishiyama, Y.3    Hayashi, H.4
  • 47
    • 20044382800 scopus 로고    scopus 로고
    • Navigating the chaperone network: An integrative map of physical and genetic interactions mediated by the hsp90 chaperone
    • DOI 10.1016/j.cell.2004.12.024
    • R Zhao M Davey YC Hsu P Kaplanek A Tong AB Parsons N Krogan G Cagney D Mai J Greenblatt C Boone A Emili WA Houry 2005 Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone Cell 120 715 727 10.1016/j.cell.2004.12.024 1:CAS:528: DC%2BD2MXis1yhtr8%3D 10.1016/j.cell.2004.12.024 15766533 (Pubitemid 40343082)
    • (2005) Cell , vol.120 , Issue.5 , pp. 715-727
    • Zhao, R.1    Davey, M.2    Hsu, Y.-C.3    Kaplanek, P.4    Tong, A.5    Parsons, A.B.6    Krogan, N.7    Cagney, G.8    Mai, D.9    Greenblatt, J.10    Boone, C.11    Emili, A.12    Houry, W.A.13
  • 48
    • 75149177573 scopus 로고    scopus 로고
    • Hsp90 and co-chaperones twist the functions of diverse client proteins
    • bip.21292/bip.21292 10.1002/bip.21292
    • A Zuehlke JL Johnson 2009 Hsp90 and co-chaperones twist the functions of diverse client proteins Biopolymers 93 211 217 bip.21292/bip.21292 10.1002/bip.21292
    • (2009) Biopolymers , vol.93 , pp. 211-217
    • Zuehlke, A.1    Johnson, J.L.2


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