메뉴 건너뛰기




Volumn 22, Issue 4, 2013, Pages 425-433

Rapid expression screening of eukaryotic membrane proteins in Pichia pastoris

Author keywords

GFP; Membrane protein expression; Pichia pastoris; Structural genomics

Indexed keywords

AQUAPORIN 4; EUKARYOTIC MEMBRANE PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLETHANOLAMINE METHYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84878269745     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2223     Document Type: Article
Times cited : (24)

References (36)
  • 1
    • 0034808117 scopus 로고    scopus 로고
    • Comparing function and structure between entire proteomes
    • DOI 10.1110/ps.10101
    • Liu J, Rost B (2001) Comparing function and structure between entire proteomes. Protein Sci 10:1970-1979. (Pubitemid 32911216)
    • (2001) Protein Science , vol.10 , Issue.10 , pp. 1970-1979
    • Liu, J.1    Rost, B.2
  • 4
    • 11144234979 scopus 로고    scopus 로고
    • Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli
    • DOI 10.1110/ps.041022305
    • Korepanova A, Gao FP, Hua Y, Qin H, Nakamoto RK, Cross TA (2005) Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli. Protein Sci 14:148-158. (Pubitemid 40054126)
    • (2005) Protein Science , vol.14 , Issue.1 , pp. 148-158
    • Korepanova, A.1    Gao, F.P.2    Hua, Y.3    Qin, H.4    Nakamoto, R.K.5    Cross, T.A.6
  • 5
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate T, Michel JC, Birdsong WT, Gouaux E (2009) Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 460:592-598.
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 7
    • 79960918054 scopus 로고    scopus 로고
    • The crystal structure of GXGD membrane protease FlaK
    • Hu J, Xue Y, Lee S, Ha Y (2011) The crystal structure of GXGD membrane protease FlaK. Nature 475: 528-531.
    • (2011) Nature , vol.475 , pp. 528-531
    • Hu, J.1    Xue, Y.2    Lee, S.3    Ha, Y.4
  • 9
    • 79960918054 scopus 로고    scopus 로고
    • The crystal structure of GXGD membrane protease FlaK
    • Hu J, Xue Y, Lee S, Ha Y (2011) The crystal structure of GXGD membrane protease FlaK. Nature 475: 528-U130.
    • (2011) Nature , vol.475
    • Hu, J.1    Xue, Y.2    Lee, S.3    Ha, Y.4
  • 10
    • 0032545321 scopus 로고    scopus 로고
    • Structure of the MscL homolog from Mycobacterium tuberculosis: A gated mechanosensitive ion channel
    • DOI 10.1126/science.282.5397.2220
    • Chang G, Spencer RH, Lee AT, Barclay MT, Rees DC (1998) Structure of the MscL homolog from Mycobacterium tuberculosis: a gated mechanosensitive ion channel. Science 282:2220-2226. (Pubitemid 29004063)
    • (1998) Science , vol.282 , Issue.5397 , pp. 2220-2226
    • Chang, G.1    Spencer, R.H.2    Lee, A.T.3    Barclay, M.T.4    Rees, D.C.5
  • 11
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • DOI 10.1016/S0014-5793(01)02980-5, PII S0014579301029805
    • Drew DE, von Heijne G, Nordlund P, de Gier JWL (2001) Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli. FEBS Lett 507:220-224. (Pubitemid 33001546)
    • (2001) FEBS Letters , vol.507 , Issue.2 , pp. 220-224
    • Drew, D.E.1    Von Heijne, G.2    Nordlund, P.3    De Gier, J.-W.L.4
  • 13
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • Kawate T, Gouaux E (2006) Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14: 673-681.
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 14
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • DOI 10.1038/nprot.2008.44, PII NPROT.2008.44
    • Drew D, Newstead S, Sonoda Y, Kim H, von Heijne G, Iwata S (2008) GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat Protoc 3:784-798. (Pubitemid 351639023)
    • (2008) Nature Protocols , vol.3 , Issue.5 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    Von Heijne, G.5    Iwata, S.6
  • 16
    • 80054991427 scopus 로고    scopus 로고
    • Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT
    • Hu NJ, Iwata S, Cameron AD, Drew D (2011) Crystal structure of a bacterial homologue of the bile acid sodium symporter ASBT. Nature 478:408-411.
    • (2011) Nature , vol.478 , pp. 408-411
    • Hu, N.J.1    Iwata, S.2    Cameron, A.D.3    Drew, D.4
  • 20
    • 84856297467 scopus 로고    scopus 로고
    • Crystal structure of the human two-pore domain potassium channel K2P1
    • Miller AN, Long SB (2012) Crystal structure of the human two-pore domain potassium channel K2P1. Science 335:432-436.
    • (2012) Science , vol.335 , pp. 432-436
    • Miller, A.N.1    Long, S.B.2
  • 21
    • 23244456428 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1126/science.1116269
    • Long SB, Campbell EB, Mackinnon R (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309:897-903. (Pubitemid 41099919)
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 25
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh A, Larsson B, von Heijne G, Sonnhammer ELL (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305:567-580. (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 26
    • 43249110882 scopus 로고    scopus 로고
    • Phosphatidylcholine and choline homeostasis
    • Li Z, Vance DE (2008) Phosphatidylcholine and choline homeostasis. J Lipid Res 49:1187-1194.
    • (2008) J Lipid Res , vol.49 , pp. 1187-1194
    • Li, Z.1    Vance, D.E.2
  • 28
    • 79953064630 scopus 로고    scopus 로고
    • Impaired phosphatidylcholine biosynthesis reduces atherosclerosis and prevents lipotoxic cardiac dysfunction in ApoE-/- mice
    • Cole LK, Dolinsky VW, Dyck JR, Vance DE (2011) Impaired phosphatidylcholine biosynthesis reduces atherosclerosis and prevents lipotoxic cardiac dysfunction in ApoE-/- mice. Circ Res 108:686-694.
    • (2011) Circ Res , vol.108 , pp. 686-694
    • Cole, L.K.1    Dolinsky, V.W.2    Dyck, J.R.3    Vance, D.E.4
  • 30
    • 0345276579 scopus 로고    scopus 로고
    • Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: A member of the major facilitator superfamily
    • DOI 10.1110/ps.03276603
    • Lemieux MJ, Song J, Kim MJ, Huang Y, Villa A, Auer M, Li XD, Wang DN (2003) Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily. Protein Sci 12:2748-2756. (Pubitemid 37445099)
    • (2003) Protein Science , vol.12 , Issue.12 , pp. 2748-2756
    • Lemieux, M.J.1    Song, J.2    Kim, M.J.3    Huang, Y.4    Villa, A.5    Auer, M.6    Li, X.-D.7    Wang, D.-N.8
  • 32
    • 14744271884 scopus 로고
    • High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene
    • Clare JJ, Rayment FB, Ballantine SP, Sreekrishna K, Romanos MA (1991) High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene. Biotechnology 9:455-460.
    • (1991) Biotechnology , vol.9 , pp. 455-460
    • Clare, J.J.1    Rayment, F.B.2    Ballantine, S.P.3    Sreekrishna, K.4    Romanos, M.A.5
  • 33
    • 0442309687 scopus 로고    scopus 로고
    • Effects of Gene Dosage, Promoters, and Substrates on Unfolded Protein Stress of Recombinant Pichia pastoris
    • DOI 10.1002/bit.10904
    • Hohenblum H, Gasser B, Maurer M, Borth N, Mattanovich D (2004) Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol Bioeng 85:367-375. (Pubitemid 38186091)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.4 , pp. 367-375
    • Hohenblum, H.1    Gasser, B.2    Maurer, M.3    Borth, N.4    Mattanovich, D.5
  • 35
    • 77954040576 scopus 로고    scopus 로고
    • The HAC1 gene from Pichia pastoris: Characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins
    • Guerfal M, Ryckaert S, Jacobs PP, Ameloot P, Van Craenenbroeck K, Derycke R, Callewaert N (2010) The HAC1 gene from Pichia pastoris: characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins. Microb Cell Fact 9:49.
    • (2010) Microb Cell Fact , vol.9 , pp. 49
    • Guerfal, M.1    Ryckaert, S.2    Jacobs, P.P.3    Ameloot, P.4    Van Craenenbroeck, K.5    Derycke, R.6    Callewaert, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.