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Volumn 18, Issue 2, 2009, Pages 434-439

Parallel screening and optimization of protein constructs for structural studies

Author keywords

Automated expression; High throughput; Isotope labeling; NMR; Structural biology; Structural genomics

Indexed keywords

ARTICLE; HIGH THROUGHPUT SCREENING; ISOTOPE LABELING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; STRUCTURAL GENOMICS; X RAY CRYSTALLOGRAPHY;

EID: 59949104320     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.46     Document Type: Article
Times cited : (7)

References (23)
  • 1
    • 3543148406 scopus 로고    scopus 로고
    • Expression screening, protein purification and NMR analysis of human protein domains for structural genomics
    • Folkers GE, van Buuren BN, Kaptein R (2004) Expression screening, protein purification and NMR analysis of human protein domains for structural genomics. J Struct Funct Genomics 5:119-131.
    • (2004) J Struct Funct Genomics , vol.5 , pp. 119-131
    • Folkers, G.E.1    van Buuren, B.N.2    Kaptein, R.3
  • 2
    • 0030042552 scopus 로고    scopus 로고
    • Rapid screening for structural integrity of expressed proteins by heteronu- clear NMR spectroscopy
    • Gronenborn AM, Clore GM (1996) Rapid screening for structural integrity of expressed proteins by heteronu- clear NMR spectroscopy. Protein Sci 5:174-177.
    • (1996) Protein Sci , vol.5 , pp. 174-177
    • Gronenborn, A.M.1    Clore, G.M.2
  • 4
    • 0038024376 scopus 로고    scopus 로고
    • Screening methods to determine biophysical properties of proteins in structural genomics
    • Woestenenk EA, Hammarstrom M, Hard T, Berglund H (2003) Screening methods to determine biophysical properties of proteins in structural genomics. Anal Bio- chem 318:71-79.
    • (2003) Anal Bio- chem , vol.318 , pp. 71-79
    • Woestenenk, E.A.1    Hammarstrom, M.2    Hard, T.3    Berglund, H.4
  • 5
    • 0037349452 scopus 로고    scopus 로고
    • Structural proteomics: Toward high-throughput structural biology as a tool in functional genomics
    • Yee A, Pardee K, Christendat D, Savchenko A, Edwards AM, Arrowsmith CH (2003) Structural proteomics: toward high-throughput structural biology as a tool in functional genomics. Acc Chem Res 36:183-189.
    • (2003) Acc Chem Res , vol.36 , pp. 183-189
    • Yee, A.1    Pardee, K.2    Christendat, D.3    Savchenko, A.4    Edwards, A.M.5    Arrowsmith, C.H.6
  • 7
    • 16244385882 scopus 로고    scopus 로고
    • identification and optimization of protein domains for NMR studies
    • Card PB, Gardner KH (2005) identification and optimization of protein domains for NMR studies. Methods Enzymol 394:3-16.
    • (2005) Methods Enzymol , vol.394 , pp. 3-16
    • Card, P.B.1    Gardner, K.H.2
  • 9
    • 20444393525 scopus 로고    scopus 로고
    • Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
    • Schanda P, Brutscher B (2005) Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds. J Am Chem Soc 127:8014-8015.
    • (2005) J Am Chem Soc , vol.127 , pp. 8014-8015
    • Schanda, P.1    Brutscher, B.2
  • 11
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromo- lecules in solution
    • Pervushin K, Riek R, Wider G, Wuthrich K (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromo- lecules in solution. Proc Natl Acad Sci USA 94:12366-12371.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 12
    • 0042510932 scopus 로고    scopus 로고
    • Refolding out of guanidine hydrochloride is an effective approach for high-throughput structural studies of small proteins
    • Maxwell KL, Bona D, Liu C, Arrowsmith CH, Edwards AM (2003) Refolding out of guanidine hydrochloride is an effective approach for high-throughput structural studies of small proteins. Protein Sci 12:2073-2080.
    • (2003) Protein Sci , vol.12 , pp. 2073-2080
    • Maxwell, K.L.1    Bona, D.2    Liu, C.3    Arrowsmith, C.H.4    Edwards, A.M.5
  • 13
    • 0742323351 scopus 로고    scopus 로고
    • The Arabi- dopsis double-stranded RNA-binding protein HYL1 plays a role in micro RNA-mediated gene regulation
    • Han MH, Goud S, Song L, Fedoroff N (2004) The Arabi- dopsis double-stranded RNA-binding protein HYL1 plays a role in micro RNA-mediated gene regulation. Proc Natl Acad Sci USA 101:1093-1098.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1093-1098
    • Han, M.H.1    Goud, S.2    Song, L.3    Fedoroff, N.4
  • 14
    • 1542350745 scopus 로고    scopus 로고
    • The nuclear dsRNA binding protein HYL1 is required for microRNA accumulation and plant development, but not posttranscriptional transgene silencing
    • Vazquez F, Gasciolli V, Crete P, Vaucheret H (2004) The nuclear dsRNA binding protein HYL1 is required for microRNA accumulation and plant development, but not posttranscriptional transgene silencing. Curr Biol 14:351.
    • (2004) Curr Biol , vol.14 , pp. 351
    • Vazquez, F.1    Gasciolli, V.2    Crete, P.3    Vaucheret, H.4
  • 15
    • 34247339143 scopus 로고    scopus 로고
    • The N- terminal double-stranded RNA binding domains of Arabi- dopsis HYPONASTIC LEAVES1 are sufficient for pre- microRNA processing
    • Wu F, Yu L, Cao W, Mao Y, Liu Z, He Y (2007) The N- terminal double-stranded RNA binding domains of Arabi- dopsis HYPONASTIC LEAVES1 are sufficient for pre- microRNA processing. Plant Cell 19:914-925.
    • (2007) Plant Cell , vol.19 , pp. 914-925
    • Wu, F.1    Yu, L.2    Cao, W.3    Mao, Y.4    Liu, Z.5    He, Y.6
  • 16
    • 13844311014 scopus 로고    scopus 로고
    • NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline
    • Page R, Peti W, Wilson IA, Stevens RC, Wuthrich K (2005) NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline. Proc Natl Acad Sci USA 102: 1901-1905.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 1901-1905
    • Page, R.1    Peti, W.2    Wilson, I.A.3    Stevens, R.C.4    Wuthrich, K.5
  • 17
    • 28444480251 scopus 로고    scopus 로고
    • Snyder DA, Chen Y, Denissova NG, Acton T, Aramini JM, Ciano M, Karlin R, Liu J, Manor P, Rajan PA, Rossi P, Swapna GV, Xiao R, Rost B, Hunt J, Montelione GT (2005) Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination. J Am Chem Soc 127:1650516511.
    • Snyder DA, Chen Y, Denissova NG, Acton T, Aramini JM, Ciano M, Karlin R, Liu J, Manor P, Rajan PA, Rossi P, Swapna GV, Xiao R, Rost B, Hunt J, Montelione GT (2005) Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination. J Am Chem Soc 127:1650516511.
  • 18
    • 36749034218 scopus 로고    scopus 로고
    • Dong A, Xu X, Edwards AM, Chang C, Chruszcz M, Cuff M, Cymborowski M, Di Leo R, Egorova O, Evdokimova E, Filippova E, Gu J, Guthrie J, Ignatchenko A, Joachi- miak A, Klostermann N, Kim Y, Korniyenko Y, Minor W, Que Q, Savchenko A, Skarina T, Tan K, Yakunin A, Yee A, Yim V, Zhang R, Zheng H, Akutsu M, Arrowsmith C, Avvakumov GV, Bochkarev A, Dahlgren LG, Dhe-Paganon S, Dimov S, Dombrovski L, Finerty P, Jr, Flodin S, Flores A, Gräslund S, Hammerström M, Herman MD, Hong BS, Hui R, Johansson I, Liu Y, Nilsson M, Nedyal- kova L, Nordlund P, Nyman T, Min J, Ouyang H, Park HW, Qi C, Rabeh W, Shen L, Shen Y, Sukumard D, Tem- pel W, Tong Y, Tresagues L, Vedadi M, Walker JR, Wei- gelt J, Welin M, Wu H, Xiao T, Zeng H, Zhu H (2007) In situ proteolysis for protein crystallization and structure determination. Nat Methods 4:1019-1021
    • Dong A, Xu X, Edwards AM, Chang C, Chruszcz M, Cuff M, Cymborowski M, Di Leo R, Egorova O, Evdokimova E, Filippova E, Gu J, Guthrie J, Ignatchenko A, Joachi- miak A, Klostermann N, Kim Y, Korniyenko Y, Minor W, Que Q, Savchenko A, Skarina T, Tan K, Yakunin A, Yee A, Yim V, Zhang R, Zheng H, Akutsu M, Arrowsmith C, Avvakumov GV, Bochkarev A, Dahlgren LG, Dhe-Paganon S, Dimov S, Dombrovski L, Finerty P, Jr, Flodin S, Flores A, Gräslund S, Hammerström M, Herman MD, Hong BS, Hui R, Johansson I, Liu Y, Nilsson M, Nedyal- kova L, Nordlund P, Nyman T, Min J, Ouyang H, Park HW, Qi C, Rabeh W, Shen L, Shen Y, Sukumard D, Tem- pel W, Tong Y, Tresagues L, Vedadi M, Walker JR, Wei- gelt J, Welin M, Wu H, Xiao T, Zeng H, Zhu H (2007) In situ proteolysis for protein crystallization and structure determination. Nat Methods 4:1019-1021.
  • 20
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heter- onuclear correlation spectra of proteins within a few seconds
    • Schanda P, Kupce E, Brutscher B (2005) SOFAST-HMQC experiments for recording two-dimensional heter- onuclear correlation spectra of proteins within a few seconds. J Biomol NMR 33:199-211.
    • (2005) J Biomol NMR , vol.33 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3
  • 22
    • 0000596240 scopus 로고
    • Maximum entropy reconstruction of complex (phase-sensitive) spectra
    • Hoch JC, Stern AS, Donoho DL, Johnstone IM (1990) Maximum entropy reconstruction of complex (phase-sensitive) spectra. J Magn Reson 86:236-246.
    • (1990) J Magn Reson , vol.86 , pp. 236-246
    • Hoch, J.C.1    Stern, A.S.2    Donoho, D.L.3    Johnstone, I.M.4
  • 23
    • 34548486475 scopus 로고    scopus 로고
    • Automatic maximum entropy spectral reconstruction in NMR
    • Mobli M, Maciejewski MW, Gryk MR, Hoch JC (2007) Automatic maximum entropy spectral reconstruction in NMR. J Biomol NMR 39:133-139.
    • (2007) J Biomol NMR , vol.39 , pp. 133-139
    • Mobli, M.1    Maciejewski, M.W.2    Gryk, M.R.3    Hoch, J.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.