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Volumn 10, Issue , 2009, Pages 425-

Genome-wide analysis of signal peptide functionality in Lactobacillus plantarum WCFS1

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; MESSENGER RNA; NUCLEASE; SIGNAL PEPTIDASE I; SIGNAL PEPTIDE;

EID: 70349728622     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-10-425     Document Type: Article
Times cited : (85)

References (67)
  • 1
    • 0031879986 scopus 로고    scopus 로고
    • The normal Lactobacillus flora of healthy human rectal and oral mucosa
    • 10.1046/j.1365-2672.1998.00480.x, 9721659
    • Ahrné S, Nobaek S, Jeppsson B, Adlerberth I, Wold AE, Molin G. The normal Lactobacillus flora of healthy human rectal and oral mucosa. J Appl Microbiol 1998, 85:88-94. 10.1046/j.1365-2672.1998.00480.x, 9721659.
    • (1998) J Appl Microbiol , vol.85 , pp. 88-94
    • Ahrné, S.1    Nobaek, S.2    Jeppsson, B.3    Adlerberth, I.4    Wold, A.E.5    Molin, G.6
  • 3
    • 22144493299 scopus 로고    scopus 로고
    • High-level, inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum using versatile expression vectors
    • 10.1099/mic.0.28084-0, 16000734
    • Sørvig E, Mathiesen G, Naterstad K, Eijsink VGH, Axelsson L. High-level, inducible gene expression in Lactobacillus sakei and Lactobacillus plantarum using versatile expression vectors. Microbiology 2005, 151:2439-2449. 10.1099/mic.0.28084-0, 16000734.
    • (2005) Microbiology , vol.151 , pp. 2439-2449
    • Sørvig, E.1    Mathiesen, G.2    Naterstad, K.3    Eijsink, V.G.H.4    Axelsson, L.5
  • 4
    • 0028265878 scopus 로고
    • Use of homologous expression-secretion signals and vector-free stable chromosomal integration in engineering of Lactobacillus plantarum for α-amylase and levanase expression
    • 201496, 8017927
    • Hols P, Ferain T, Garmyn D, Bernard N, Delcour J. Use of homologous expression-secretion signals and vector-free stable chromosomal integration in engineering of Lactobacillus plantarum for α-amylase and levanase expression. Appl Environ Microbiol 1994, 60:1401-1413. 201496, 8017927.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1401-1413
    • Hols, P.1    Ferain, T.2    Garmyn, D.3    Bernard, N.4    Delcour, J.5
  • 5
    • 0030816521 scopus 로고    scopus 로고
    • Efficient secretion of the model antigen M6-gp41E in Lactobacillus plantarum NCIMB 8826
    • 10.1099/00221287-143-8-2733, 9274026
    • Hols P, Slos P, Dutot P, Reymund J, Chabot P, Delplace B, Delcour J, Mercenier A. Efficient secretion of the model antigen M6-gp41E in Lactobacillus plantarum NCIMB 8826. Microbiology 1997, 143:2733-2741. 10.1099/00221287-143-8-2733, 9274026.
    • (1997) Microbiology , vol.143 , pp. 2733-2741
    • Hols, P.1    Slos, P.2    Dutot, P.3    Reymund, J.4    Chabot, P.5    Delplace, B.6    Delcour, J.7    Mercenier, A.8
  • 6
    • 0033781867 scopus 로고    scopus 로고
    • Adaptation of the nisin-controlled expression system in Lactobacillus plantarum: a tool to study in vivo biological effects
    • 10.1128/AEM.66.10.4427-4432.2000, 92320, 11010894
    • Pavan S, Hols P, Delcour J, Geoffroy MC, Grangette C, Kleerebezem M, Mercenier A. Adaptation of the nisin-controlled expression system in Lactobacillus plantarum: a tool to study in vivo biological effects. Appl Environ Microbiol 2000, 66:4427-4432. 10.1128/AEM.66.10.4427-4432.2000, 92320, 11010894.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4427-4432
    • Pavan, S.1    Hols, P.2    Delcour, J.3    Geoffroy, M.C.4    Grangette, C.5    Kleerebezem, M.6    Mercenier, A.7
  • 7
    • 33847202223 scopus 로고    scopus 로고
    • Cre-lox-based system for multiple gene deletions and selectable-marker removal in Lactobacillus plantarum
    • 10.1128/AEM.01473-06, 1828656, 17142375
    • Lambert JM, Bongers RS, Kleerebezem M. Cre-lox-based system for multiple gene deletions and selectable-marker removal in Lactobacillus plantarum. Appl Environ Microbiol 2007, 73:1126-1135. 10.1128/AEM.01473-06, 1828656, 17142375.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1126-1135
    • Lambert, J.M.1    Bongers, R.S.2    Kleerebezem, M.3
  • 8
    • 4344567816 scopus 로고    scopus 로고
    • Identification of Lactobacillus plantarum genes that are induced in the gastrointestinal tract of mice
    • 10.1128/JB.186.17.5721-5729.2004, 516819, 15317777
    • Bron PA, Grangette C, Mercenier A, de Vos WM, Kleerebezem M. Identification of Lactobacillus plantarum genes that are induced in the gastrointestinal tract of mice. J Bacteriol 2004, 186:5721-5729. 10.1128/JB.186.17.5721-5729.2004, 516819, 15317777.
    • (2004) J Bacteriol , vol.186 , pp. 5721-5729
    • Bron, P.A.1    Grangette, C.2    Mercenier, A.3    de Vos, W.M.4    Kleerebezem, M.5
  • 9
    • 33846152023 scopus 로고    scopus 로고
    • Spatial and temporal expression of Lactobacillus plantarum genes in the gastrointestinal tracts of mice
    • 10.1128/AEM.01475-06, 1797133, 17071785
    • Marco ML, Bongers RS, de Vos WM, Kleerebezem M. Spatial and temporal expression of Lactobacillus plantarum genes in the gastrointestinal tracts of mice. Appl Environ Microbiol 2007, 73:124-132. 10.1128/AEM.01475-06, 1797133, 17071785.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 124-132
    • Marco, M.L.1    Bongers, R.S.2    de Vos, W.M.3    Kleerebezem, M.4
  • 10
    • 33747452065 scopus 로고    scopus 로고
    • Lactobacillus plantarum - survival, functional and potential probiotic properties in the human intestinal tract
    • de Vries MC, Vaughan EE, Kleerebezem M, de Vos WM. Lactobacillus plantarum - survival, functional and potential probiotic properties in the human intestinal tract. International Dairy Journal 2006, 16:1018-1028.
    • (2006) International Dairy Journal , vol.16 , pp. 1018-1028
    • de Vries, M.C.1    Vaughan, E.E.2    Kleerebezem, M.3    de Vos, W.M.4
  • 12
    • 42349105761 scopus 로고    scopus 로고
    • Mucosal delivery of therapeutic and prophylactic molecules using lactic acid bacteria
    • 10.1038/nrmicro1840, 18345021
    • Wells JM, Mercenier A. Mucosal delivery of therapeutic and prophylactic molecules using lactic acid bacteria. Nat Rev Microbiol 2008, 6:349-362. 10.1038/nrmicro1840, 18345021.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 349-362
    • Wells, J.M.1    Mercenier, A.2
  • 13
    • 63149182823 scopus 로고    scopus 로고
    • Dendritic cell targeting of Bacillus anthracis protective antigen expressed by Lactobacillus acidophilus protects mice from lethal challenge
    • 10.1073/pnas.0900029106, 2647975,2647975, 19246373
    • Mohamadzadeh M, Duong T, Sandwick SJ, Hoover T, Klaenhammer TR. Dendritic cell targeting of Bacillus anthracis protective antigen expressed by Lactobacillus acidophilus protects mice from lethal challenge. Proc Natl Acad Sci USA 2009, 106:4331-4336. 10.1073/pnas.0900029106, 2647975,2647975, 19246373.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4331-4336
    • Mohamadzadeh, M.1    Duong, T.2    Sandwick, S.J.3    Hoover, T.4    Klaenhammer, T.R.5
  • 14
    • 35348908966 scopus 로고    scopus 로고
    • Bacterial protein secretion through the translocase nanomachine
    • 10.1038/nrmicro1771, 17938627
    • Papanikou E, Karamanou S, Economou A. Bacterial protein secretion through the translocase nanomachine. Nat Rev Microbiol 2007, 5:839-851. 10.1038/nrmicro1771, 17938627.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 839-851
    • Papanikou, E.1    Karamanou, S.2    Economou, A.3
  • 16
    • 0034891203 scopus 로고    scopus 로고
    • Translocation of proteins across the cell envelope of Gram-positive bacteria
    • 10.1016/S0168-6445(01)00062-6, 11524133
    • van Wely KHM, Swaving J, Freudl R, Driessen AJM. Translocation of proteins across the cell envelope of Gram-positive bacteria. FEMS Microbiol Rev 2001, 25:437-454. 10.1016/S0168-6445(01)00062-6, 11524133.
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 437-454
    • van Wely, K.H.M.1    Swaving, J.2    Freudl, R.3    Driessen, A.J.M.4
  • 17
    • 0025297583 scopus 로고
    • The signal peptide
    • 10.1007/BF01868635, 2197415
    • von Heijne G. The signal peptide. J Membr Biol 1990, 115:195-201. 10.1007/BF01868635, 2197415.
    • (1990) J Membr Biol , vol.115 , pp. 195-201
    • von Heijne, G.1
  • 18
    • 33750963625 scopus 로고    scopus 로고
    • The predicted secretome of Lactobacillus plantarum WCFS1 sheds light on interactions with its environment
    • 10.1099/mic.0.29217-0, 17074889
    • Boekhorst J, Wels M, Kleerebezem M, Siezen RJ. The predicted secretome of Lactobacillus plantarum WCFS1 sheds light on interactions with its environment. Microbiology 2006, 152:3175-3183. 10.1099/mic.0.29217-0, 17074889.
    • (2006) Microbiology , vol.152 , pp. 3175-3183
    • Boekhorst, J.1    Wels, M.2    Kleerebezem, M.3    Siezen, R.J.4
  • 19
    • 44849091539 scopus 로고    scopus 로고
    • Heterologous protein secretion by Lactobacillus plantarum using homologous signal peptides
    • 10.1111/j.1365-2672.2008.03734.x, 18298538
    • Mathiesen G, Sveen A, Piard JC, Axelsson L, Eijsink VGH. Heterologous protein secretion by Lactobacillus plantarum using homologous signal peptides. J Appl Microbiol 2008, 105:215-226. 10.1111/j.1365-2672.2008.03734.x, 18298538.
    • (2008) J Appl Microbiol , vol.105 , pp. 215-226
    • Mathiesen, G.1    Sveen, A.2    Piard, J.C.3    Axelsson, L.4    Eijsink, V.G.H.5
  • 20
    • 0031035974 scopus 로고    scopus 로고
    • High level heterologous protein production in Lactococcus and Lactobacillus using a new secretion system based on the Lactobacillus brevis S-layer signals
    • 10.1016/S0378-1119(96)00717-2, 9074504
    • Savijoki K, Kahala M, Palva A. High level heterologous protein production in Lactococcus and Lactobacillus using a new secretion system based on the Lactobacillus brevis S-layer signals. Gene 1997, 186:255-262. 10.1016/S0378-1119(96)00717-2, 9074504.
    • (1997) Gene , vol.186 , pp. 255-262
    • Savijoki, K.1    Kahala, M.2    Palva, A.3
  • 21
    • 0035464768 scopus 로고    scopus 로고
    • Signal peptide and propeptide optimization for heterologous protein secretion in Lactococcus lactis
    • 10.1128/AEM.67.9.4119-4127.2001, 93138, 11526014
    • Le Loir Y, Nouaille S, Commissaire J, Bretigny L, Gruss A, Langella P. Signal peptide and propeptide optimization for heterologous protein secretion in Lactococcus lactis. Appl Environ Microbiol 2001, 67:4119-4127. 10.1128/AEM.67.9.4119-4127.2001, 93138, 11526014.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4119-4127
    • Le Loir, Y.1    Nouaille, S.2    Commissaire, J.3    Bretigny, L.4    Gruss, A.5    Langella, P.6
  • 22
    • 33845519008 scopus 로고    scopus 로고
    • Constitutive delivery of bovine β-lactoglobulin to the digestive tracts of gnotobiotic mice by engineered Lactobacillus casei
    • 10.1128/AEM.01032-06, 1694238, 16997983
    • Hazebrouck S, Oozeer R, Adel-Patient K, Langella P, Rabot S, Wal JM, Corthier G. Constitutive delivery of bovine β-lactoglobulin to the digestive tracts of gnotobiotic mice by engineered Lactobacillus casei. Appl Environ Microbiol 2006, 72:7460-7467. 10.1128/AEM.01032-06, 1694238, 16997983.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7460-7467
    • Hazebrouck, S.1    Oozeer, R.2    Adel-Patient, K.3    Langella, P.4    Rabot, S.5    Wal, J.M.6    Corthier, G.7
  • 23
    • 33947226554 scopus 로고    scopus 로고
    • Heterologous production and secretion of Clostridium perfringens beta-toxoid in closely related Gram-positive hosts
    • 10.1016/j.jbiotec.2006.07.014, 16959352
    • Nijland R, Lindner C, van Hartskamp M, Hamoen LW, Kuipers OP. Heterologous production and secretion of Clostridium perfringens beta-toxoid in closely related Gram-positive hosts. J Biotechnol 2007, 127:361-372. 10.1016/j.jbiotec.2006.07.014, 16959352.
    • (2007) J Biotechnol , vol.127 , pp. 361-372
    • Nijland, R.1    Lindner, C.2    van Hartskamp, M.3    Hamoen, L.W.4    Kuipers, O.P.5
  • 24
    • 33847092924 scopus 로고    scopus 로고
    • Lactobacillus plantarum for oral peptide delivery
    • 10.1111/j.1399-302X.2007.00338.x, 17311639
    • Oh Y, Varmanen P, Han XY, Bennett G, Xu Z, Lu T, Palva A. Lactobacillus plantarum for oral peptide delivery. Oral Microbiol Immunol 2007, 22:140-144. 10.1111/j.1399-302X.2007.00338.x, 17311639.
    • (2007) Oral Microbiol Immunol , vol.22 , pp. 140-144
    • Oh, Y.1    Varmanen, P.2    Han, X.Y.3    Bennett, G.4    Xu, Z.5    Lu, T.6    Palva, A.7
  • 25
    • 0037820426 scopus 로고    scopus 로고
    • Biological containment of genetically modified Lactococcus lactis for intestinal delivery of human interleukin 10
    • 10.1038/nbt840, 12808464
    • Steidler L, Neirynck S, Huyghebaert N, Snoeck V, Vermeire A, Goddeeris B, Cox E, Remon JP, Remaut E. Biological containment of genetically modified Lactococcus lactis for intestinal delivery of human interleukin 10. Nat Biotechnol 2003, 21:785-789. 10.1038/nbt840, 12808464.
    • (2003) Nat Biotechnol , vol.21 , pp. 785-789
    • Steidler, L.1    Neirynck, S.2    Huyghebaert, N.3    Snoeck, V.4    Vermeire, A.5    Goddeeris, B.6    Cox, E.7    Remon, J.P.8    Remaut, E.9
  • 26
    • 0034971985 scopus 로고    scopus 로고
    • Design of a protein-targeting system for lactic acid bacteria
    • 10.1128/JB.183.14.4157-4166.2001, 95304, 11418555
    • Dieye Y, Usai S, Clier F, Gruss A, Piard JC. Design of a protein-targeting system for lactic acid bacteria. J Bacteriol 2001, 183:4157-4166. 10.1128/JB.183.14.4157-4166.2001, 95304, 11418555.
    • (2001) J Bacteriol , vol.183 , pp. 4157-4166
    • Dieye, Y.1    Usai, S.2    Clier, F.3    Gruss, A.4    Piard, J.C.5
  • 28
    • 17444425389 scopus 로고    scopus 로고
    • Cell-surface display of E7 antigen from human papillomavirus type-16 in Lactococcus lactis and in Lactobacillus plantarum using a new cell-wall anchor from lactobacilli
    • 10.1080/10611860400024219, 15823960
    • Cortes-Perez NG, Azevedo V, Alcocer-Gonzalez JM, Rodriguez-Padilla C, Tamez-Guerra RS, Corthier G, Gruss A, Langella P, Bermudez-Humaran LG. Cell-surface display of E7 antigen from human papillomavirus type-16 in Lactococcus lactis and in Lactobacillus plantarum using a new cell-wall anchor from lactobacilli. J Drug Target 2005, 13:89-98. 10.1080/10611860400024219, 15823960.
    • (2005) J Drug Target , vol.13 , pp. 89-98
    • Cortes-Perez, N.G.1    Azevedo, V.2    Alcocer-Gonzalez, J.M.3    Rodriguez-Padilla, C.4    Tamez-Guerra, R.S.5    Corthier, G.6    Gruss, A.7    Langella, P.8    Bermudez-Humaran, L.G.9
  • 29
    • 0037086567 scopus 로고    scopus 로고
    • Comparison of the immune responses induced by local immunizations with recombinant Lactobacillus plantarum producing tetanus toxin fragment C in different cellular locations
    • 10.1016/S0264-410X(02)00027-0, 11906764
    • Reveneau N, Geoffroy MC, Locht C, Chagnaud P, Mercenier A. Comparison of the immune responses induced by local immunizations with recombinant Lactobacillus plantarum producing tetanus toxin fragment C in different cellular locations. Vaccine 2002, 20:1769-1777. 10.1016/S0264-410X(02)00027-0, 11906764.
    • (2002) Vaccine , vol.20 , pp. 1769-1777
    • Reveneau, N.1    Geoffroy, M.C.2    Locht, C.3    Chagnaud, P.4    Mercenier, A.5
  • 30
    • 0034036084 scopus 로고    scopus 로고
    • Expression of Bacillus subtilis phytase in Lactobacillus plantarum 755
    • 10.1046/j.1472-765x.2000.00660.x, 10792656
    • Kerovuo J, Tynkkynen S. Expression of Bacillus subtilis phytase in Lactobacillus plantarum 755. Lett Appl Microbiol 2000, 30:325-329. 10.1046/j.1472-765x.2000.00660.x, 10792656.
    • (2000) Lett Appl Microbiol , vol.30 , pp. 325-329
    • Kerovuo, J.1    Tynkkynen, S.2
  • 31
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • 10.1016/j.jmb.2004.05.028, 15223320
    • Bendtsen JD, Nielsen H, von Heijne G, Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 2004, 340:783-795. 10.1016/j.jmb.2004.05.028, 15223320.
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 32
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • 10.1093/protein/10.1.1, 9051728
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 1997, 10:1-6. 10.1093/protein/10.1.1, 9051728.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 34
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: a sequence logo generator
    • 10.1101/gr.849004, 419797, 15173120
    • Crooks GE, Hon G, Chandonia JM, Brenner SE. WebLogo: a sequence logo generator. Genome Res 2004, 14:1188-1190. 10.1101/gr.849004, 419797, 15173120.
    • (2004) Genome Res , vol.14 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.M.3    Brenner, S.E.4
  • 35
    • 0031944982 scopus 로고    scopus 로고
    • A nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactis
    • 107105, 9537390
    • Le Loir Y, Gruss A, Ehrlich SD, Langella P. A nine-residue synthetic propeptide enhances secretion efficiency of heterologous proteins in Lactococcus lactis. J Bacteriol 1998, 180:1895-1903. 107105, 9537390.
    • (1998) J Bacteriol , vol.180 , pp. 1895-1903
    • Le Loir, Y.1    Gruss, A.2    Ehrlich, S.D.3    Langella, P.4
  • 36
    • 0026896713 scopus 로고
    • Ethanol tolerance and carbohydrate-metabolism in Lactobacilli
    • Gold RS, Meagher MM, Hutkins R, Conway T. Ethanol tolerance and carbohydrate-metabolism in Lactobacilli. J Ind Microbiol 1992, 10:45-54.
    • (1992) J Ind Microbiol , vol.10 , pp. 45-54
    • Gold, R.S.1    Meagher, M.M.2    Hutkins, R.3    Conway, T.4
  • 37
    • 0030724903 scopus 로고    scopus 로고
    • Molecular characterization of the alpha-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3' end structure with direct tandem repeats and suggests a common evolutionary origin
    • 10.1016/S0378-1119(97)00309-0, 9370276
    • Giraud E, Cuny G. Molecular characterization of the alpha-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3' end structure with direct tandem repeats and suggests a common evolutionary origin. Gene 1997, 198:149-157. 10.1016/S0378-1119(97)00309-0, 9370276.
    • (1997) Gene , vol.198 , pp. 149-157
    • Giraud, E.1    Cuny, G.2
  • 38
    • 0027769981 scopus 로고
    • Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis
    • Wang Z, Jones JD, Rizo J, Gierasch LM. Membrane-bound conformation of a signal peptide: a transferred nuclear Overhauser effect analysis. Biochemistry (Mosc) 1993, 32:13991-13999.
    • (1993) Biochemistry (Mosc) , vol.32 , pp. 13991-13999
    • Wang, Z.1    Jones, J.D.2    Rizo, J.3    Gierasch, L.M.4
  • 39
    • 0022475473 scopus 로고
    • Conformations of signal peptides induced by lipids suggest initial steps in protein export
    • 10.1126/science.2941862, 2941862
    • Briggs MS, Cornell DG, Dluhy RA, Gierasch LM. Conformations of signal peptides induced by lipids suggest initial steps in protein export. Science 1986, 233:206-208. 10.1126/science.2941862, 2941862.
    • (1986) Science , vol.233 , pp. 206-208
    • Briggs, M.S.1    Cornell, D.G.2    Dluhy, R.A.3    Gierasch, L.M.4
  • 40
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • 10.1006/jmbi.2000.4315, 11152613
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 2001, 305:567-580. 10.1006/jmbi.2000.4315, 11152613.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 42
    • 33748101074 scopus 로고    scopus 로고
    • Systematic screening of all signal peptides from Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria
    • 10.1016/j.jmb.2006.07.034, 16930615
    • Brockmeier U, Caspers M, Freudl R, Jockwer A, Noll T, Eggert T. Systematic screening of all signal peptides from Bacillus subtilis: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria. J Mol Biol 2006, 362:393-402. 10.1016/j.jmb.2006.07.034, 16930615.
    • (2006) J Mol Biol , vol.362 , pp. 393-402
    • Brockmeier, U.1    Caspers, M.2    Freudl, R.3    Jockwer, A.4    Noll, T.5    Eggert, T.6
  • 43
    • 0034663718 scopus 로고    scopus 로고
    • The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis
    • 10.1042/0264-6021:3500031, 1221221, 10926823
    • Stephenson K, Jensen CL, Jørgensen ST, Lakey JH, Harwood CR. The influence of secretory-protein charge on late stages of secretion from the Gram-positive bacterium Bacillus subtilis. Biochem J 2000, 350:31-39. 10.1042/0264-6021:3500031, 1221221, 10926823.
    • (2000) Biochem J , vol.350 , pp. 31-39
    • Stephenson, K.1    Jensen, C.L.2    Jørgensen, S.T.3    Lakey, J.H.4    Harwood, C.R.5
  • 44
    • 39049125071 scopus 로고    scopus 로고
    • Bacillus protein secretion: an unfolding story
    • Harwood CR, Cranenburgh R. Bacillus protein secretion: an unfolding story. Trends Microbiol 2008, 16:73-79.
    • (2008) Trends Microbiol , vol.16 , pp. 73-79
    • Harwood, C.R.1    Cranenburgh, R.2
  • 45
    • 33745683590 scopus 로고    scopus 로고
    • Proteomic dissection of potential signal recognition particle dependence in protein secretion by Bacillus subtilis
    • 10.1002/pmic.200500560, 16705751
    • Zanen G, Antelmann H, Meima R, Jongbloed JD, Kolkman M, Hecker M, van Dijl JM, Quax WJ. Proteomic dissection of potential signal recognition particle dependence in protein secretion by Bacillus subtilis. Proteomics 2006, 6:3636-3648. 10.1002/pmic.200500560, 16705751.
    • (2006) Proteomics , vol.6 , pp. 3636-3648
    • Zanen, G.1    Antelmann, H.2    Meima, R.3    Jongbloed, J.D.4    Kolkman, M.5    Hecker, M.6    van Dijl, J.M.7    Quax, W.J.8
  • 46
    • 39149119271 scopus 로고    scopus 로고
    • High-level secretion of a chimeric thermostable lichenase from Bacillus subtilis by screening of site-mutated signal peptides with structural alterations
    • 10.1007/s00284-007-9077-5, 18172721
    • Fu LL, Xu ZR, Shuai JB, Hu CX, Dai W, Li WF. High-level secretion of a chimeric thermostable lichenase from Bacillus subtilis by screening of site-mutated signal peptides with structural alterations. Curr Microbiol 2008, 56:287-292. 10.1007/s00284-007-9077-5, 18172721.
    • (2008) Curr Microbiol , vol.56 , pp. 287-292
    • Fu, L.L.1    Xu, Z.R.2    Shuai, J.B.3    Hu, C.X.4    Dai, W.5    Li, W.F.6
  • 48
    • 0041923882 scopus 로고    scopus 로고
    • Optimization of signal peptide SP310 for heterologous protein production in Lactococcus lactis
    • 10.1099/mic.0.26299-0, 12904559
    • Ravn P, Arnau J, Madsen SM, Vrang A, Israelsen H. Optimization of signal peptide SP310 for heterologous protein production in Lactococcus lactis. Microbiology 2003, 149:2193-2201. 10.1099/mic.0.26299-0, 12904559.
    • (2003) Microbiology , vol.149 , pp. 2193-2201
    • Ravn, P.1    Arnau, J.2    Madsen, S.M.3    Vrang, A.4    Israelsen, H.5
  • 49
    • 33747870454 scopus 로고    scopus 로고
    • Signal sequence directs localized secretion of bacterial surface proteins
    • 10.1038/nature05021, 16929299
    • Carlsson F, Stalhammar-Carlemalm M, Flardh K, Sandin C, Carlemalm E, Lindahl G. Signal sequence directs localized secretion of bacterial surface proteins. Nature 2006, 442:943-946. 10.1038/nature05021, 16929299.
    • (2006) Nature , vol.442 , pp. 943-946
    • Carlsson, F.1    Stalhammar-Carlemalm, M.2    Flardh, K.3    Sandin, C.4    Carlemalm, E.5    Lindahl, G.6
  • 50
    • 54349128596 scopus 로고    scopus 로고
    • Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus
    • 10.1038/emboj.2008.185, 18800056
    • DeDent A, Bae T, Missiakas DM, Schneewind O. Signal peptides direct surface proteins to two distinct envelope locations of Staphylococcus aureus. EMBO J 2008, 27:2656-2668. 10.1038/emboj.2008.185, 18800056.
    • (2008) EMBO J , vol.27 , pp. 2656-2668
    • DeDent, A.1    Bae, T.2    Missiakas, D.M.3    Schneewind, O.4
  • 51
    • 33748937555 scopus 로고    scopus 로고
    • The surprising complexity of signal sequences
    • 10.1016/j.tibs.2006.08.004, 16919958
    • Hegde RS, Bernstein HD. The surprising complexity of signal sequences. Trends Biochem Sci 2006, 31:563-571. 10.1016/j.tibs.2006.08.004, 16919958.
    • (2006) Trends Biochem Sci , vol.31 , pp. 563-571
    • Hegde, R.S.1    Bernstein, H.D.2
  • 52
    • 0025960282 scopus 로고
    • Effect of signal sequence alterations on export of levansucrase in Bacillus subtilis
    • 207184, 1898923
    • Borchert TV, Nagarajan V. Effect of signal sequence alterations on export of levansucrase in Bacillus subtilis. J Bacteriol 1991, 173:276-282. 207184, 1898923.
    • (1991) J Bacteriol , vol.173 , pp. 276-282
    • Borchert, T.V.1    Nagarajan, V.2
  • 53
    • 0026701330 scopus 로고
    • Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency
    • Hikita C, Mizushima S. Effects of total hydrophobicity and length of the hydrophobic domain of a signal peptide on in vitro translocation efficiency. J Biol Chem 1992, 267:4882-4888.
    • (1992) J Biol Chem , vol.267 , pp. 4882-4888
    • Hikita, C.1    Mizushima, S.2
  • 54
    • 42549137778 scopus 로고    scopus 로고
    • LocateP: genome-scale subcellular-location predictor for bacterial proteins
    • 10.1186/1471-2105-9-173, 2375117, 18371216
    • Zhou M, Boekhorst J, Francke C, Siezen RJ. LocateP: genome-scale subcellular-location predictor for bacterial proteins. BMC Bioinformatics 2008, 9:173. 10.1186/1471-2105-9-173, 2375117, 18371216.
    • (2008) BMC Bioinformatics , vol.9 , pp. 173
    • Zhou, M.1    Boekhorst, J.2    Francke, C.3    Siezen, R.J.4
  • 56
    • 34548231707 scopus 로고    scopus 로고
    • Production and secretion stress caused by overexpression of heterologous α-Amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis
    • 10.1128/AEM.00472-07, 1950988, 17586671
    • Lulko AT, Veening J-W, Buist G, Smits WK, Blom EJ, Beekman AC, Bron S, Kuipers OP. Production and secretion stress caused by overexpression of heterologous α-Amylase leads to inhibition of sporulation and a prolonged motile phase in Bacillus subtilis. Appl Environ Microbiol 2007, 73:5354-5362. 10.1128/AEM.00472-07, 1950988, 17586671.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 5354-5362
    • Lulko, A.T.1    Veening, J.-.W.2    Buist, G.3    Smits, W.K.4    Blom, E.J.5    Beekman, A.C.6    Bron, S.7    Kuipers, O.P.8
  • 57
    • 0029198457 scopus 로고
    • Transformation of Lactobacillus by electroporation
    • Aukrust TW, Brurberg MB, Nes IF. Transformation of Lactobacillus by electroporation. Methods Mol Biol 1995, 47:201-208.
    • (1995) Methods Mol Biol , vol.47 , pp. 201-208
    • Aukrust, T.W.1    Brurberg, M.B.2    Nes, I.F.3
  • 58
    • 0345170069 scopus 로고    scopus 로고
    • Construction of vectors for inducible gene expression in Lactobacillus sakei and L. plantarum
    • 10.1016/S0378-1097(03)00798-5, 14659551
    • Sørvig E, Grönqvist S, Naterstad K, Mathiesen G, Eijsink VGH, Axelsson L. Construction of vectors for inducible gene expression in Lactobacillus sakei and L. plantarum. FEMS Microbiol Lett 2003, 229:119-126. 10.1016/S0378-1097(03)00798-5, 14659551.
    • (2003) FEMS Microbiol Lett , vol.229 , pp. 119-126
    • Sørvig, E.1    Grönqvist, S.2    Naterstad, K.3    Mathiesen, G.4    Eijsink, V.G.H.5    Axelsson, L.6
  • 59
    • 0029989630 scopus 로고    scopus 로고
    • Induction of bacteriocin production in Lactobacillus sake by a secreted peptide
    • 177930, 8636023
    • Eijsink VGH, Brurberg MB, Middelhoven PH, Nes IF. Induction of bacteriocin production in Lactobacillus sake by a secreted peptide. J Bacteriol 1996, 178:2232-2237. 177930, 8636023.
    • (1996) J Bacteriol , vol.178 , pp. 2232-2237
    • Eijsink, V.G.H.1    Brurberg, M.B.2    Middelhoven, P.H.3    Nes, I.F.4
  • 60
    • 15644370483 scopus 로고
    • Extracellular nuclease from Staphylococcus aureus
    • New York: Harper & Row, Cantoni GL, David R
    • Heins JN, Taniuchi H, Anfinsen CB. Extracellular nuclease from Staphylococcus aureus. Procedures in nucleic acid research 1966, 79-84. New York: Harper & Row, Cantoni GL, David R.
    • (1966) Procedures in nucleic acid research , pp. 79-84
    • Heins, J.N.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 61
    • 0030956641 scopus 로고    scopus 로고
    • Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria
    • 179078, 9139932
    • Piard JC, Hautefort I, Fischetti VA, Ehrlich SD, Fons M, Gruss A. Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria. J Bacteriol 1997, 179:3068-3072. 179078, 9139932.
    • (1997) J Bacteriol , vol.179 , pp. 3068-3072
    • Piard, J.C.1    Hautefort, I.2    Fischetti, V.A.3    Ehrlich, S.D.4    Fons, M.5    Gruss, A.6
  • 62
    • 2142798560 scopus 로고    scopus 로고
    • Investigation of protein export in Bifidobacterium breve UCC2003
    • 10.1128/AEM.69.12.6994-7001.2003, 309956, 14660341
    • MacConaill LE, Fitzgerald GF, van Sinderen D. Investigation of protein export in Bifidobacterium breve UCC2003. Appl Environ Microbiol 2003, 69:6994-7001. 10.1128/AEM.69.12.6994-7001.2003, 309956, 14660341.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6994-7001
    • MacConaill, L.E.1    Fitzgerald, G.F.2    van Sinderen, D.3
  • 63
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • 10.1093/nar/29.9.e45, 55695, 11328886
    • Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 2001, 29:e45. 10.1093/nar/29.9.e45, 55695, 11328886.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 64
    • 11844274688 scopus 로고    scopus 로고
    • Determination of an internal control to apply reverse transcription quantitative PCR to study stress response in the lactic acid bacterium Oenococcus oeni
    • 10.1016/j.mimet.2004.10.010, 15649534
    • Desroche N, Beltramo C, Guzzo J. Determination of an internal control to apply reverse transcription quantitative PCR to study stress response in the lactic acid bacterium Oenococcus oeni. J Microbiol Methods 2005, 60:325-333. 10.1016/j.mimet.2004.10.010, 15649534.
    • (2005) J Microbiol Methods , vol.60 , pp. 325-333
    • Desroche, N.1    Beltramo, C.2    Guzzo, J.3
  • 65
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • 10.1093/nar/30.9.e36, 113859, 11972351
    • Pfaffl MW, Horgan GW, Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 2002, 30:e36. 10.1093/nar/30.9.e36, 113859, 11972351.
    • (2002) Nucleic Acids Res , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 67
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • 10.1016/0022-2836(82)90515-0, 7108955
    • Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982, 157:105-132. 10.1016/0022-2836(82)90515-0, 7108955.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


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