Protein production and purification

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302

[6] Use of T7 RNA polymerase to direct expression of cloned genes

William Studier, F., Rosenberg, A. H., Dunn, J. J., & Dubendorff, J. W. (1990) · Methods in Enzymology · doi:10.1016/0076-6879(90)85008-c · Cited by 6,562

Protein production by auto-induction in high-density shaking cultures

Studier, F. W. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.01.016 · Cited by 5,931

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Guzman, L. M., Belin, D., Carson, M. J., & Beckwith, J. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.14.4121-4130.1995 · Cited by 4,935

The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

Niesen, F. H., Berglund, H., & Vedadi, M. (2007) · Nature Protocols · doi:10.1038/nprot.2007.321 · Cited by 2,408

Cell-free translation reconstituted with purified components

Shimizu, Y., Inoue, A., Tomari, Y., Suzuki, T., Yokogawa, T., Nishikawa, K., & Ueda, T. (2001) · Nature Biotechnology · doi:10.1038/90802 · Cited by 1,940

Intrinsic Disorder in Cell-signaling and Cancer-associated Proteins

Iakoucheva, L. M., Brown, C. J., Lawson, J. D., Obradović, Z., & Dunker, A. K. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00969-5 · Cited by 1,214

Ligation-independent cloning of PCR products (LIC-PCR)

Aslanidis, C., & de Jong, P. J. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.20.6069 · Cited by 1,204

DNA Cloning Using In Vitro Site-Specific Recombination

Hartley, J. L. (2000) · Genome Research · doi:10.1101/gr.143000 · Cited by 1,130

Production of human beta interferon in insect cells infected with a baculovirus expression vector.

Smith, G. E., Summers, M. D., & Fraser, M. J. (1983) · Molecular and Cellular Biology · doi:10.1128/mcb.3.12.2156 · Cited by 968

Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused

Kapust, R. B., & Waugh, D. S. (1999) · Protein Science · doi:10.1110/ps.8.8.1668 · Cited by 960

A time- and cost-efficient system for high-level protein production in mammalian cells

Aricescu, A. R., Lu, W., & Jones, E. Y. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906029799 · Cited by 762

3D-Jury: a simple approach to improve protein structure predictions

Ginalski, K., Elofsson, A., Fischer, D., & Rychlewski, L. (2003) · Bioinformatics · doi:10.1093/bioinformatics/btg124 · Cited by 719

The DISOPRED server for the prediction of protein disorder

Ward, J. J., McGuffin, L. J., Bryson, K., Buxton, B. F., & Jones, D. T. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth195 · Cited by 688

Immobilized metal ion affinity chromatography

Porath, J. (1992) · Protein Expression and Purification · doi:10.1016/1046-5928(92)90001-d · Cited by 644

RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins

Yang, Z. R., Thomson, R., McNeil, P., & Esnouf, R. M. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti534 · Cited by 644

Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins

Arnau, J., Lauritzen, C., Petersen, G. E., & Pedersen, J. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2005.12.002 · Cited by 629

DYNAMIC, STRUCTURAL, AND REGULATORY ASPECTS OF λ SITE-SPECIFIC RECOMBINATION

Landy, A. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.004405 · Cited by 612

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination

Vedadi, M., Niesen, F. H., Allali-Hassani, A., Fedorov, O. Y., Finerty, P. J., Wasney, G. A., Yeung, R., Arrowsmith, C., Ball, L. J., Berglund, H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605224103 · Cited by 589

Making the most of affinity tags

Waugh, D. S. (2005) · Trends in Biotechnology · doi:10.1016/j.tibtech.2005.03.012 · Cited by 565

Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor

Dubendorf, J. W., & Studier, F. W. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90856-2 · Cited by 468

Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline

Lesley, S. A., Kuhn, P., Godzik, A., Deacon, A. M., Mathews, I., Kreusch, A., Spraggon, G., Klock, H. E., McMullan, D., Shin, T., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142413399 · Cited by 377

Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli

Hammarström, M., Hellgren, N., van den Berg, S., Berglund, H., & Härd, T. (2002) · Protein Science · doi:10.1110/ps.22102 · Cited by 333

Preparation of Escherichia coli cell extract for highly productive cell-free protein expression

Kigawa, T., Yabuki, T., Matsuda, N., Matsuda, T., Nakajima, R., Tanaka, A., & Yokoyama, S. (2004) · Journal of Structural and Functional Genomics · doi:10.1023/b:jsfg.0000029204.57846.7d · Cited by 330

Overexpression of Trigger Factor Prevents Aggregation of Recombinant Proteins in Escherichia coli

Nishihara, K., Kanemori, M., Yanagi, H., & Yura, T. (2000) · Applied and Environmental Microbiology · doi:10.1128/aem.66.3.884-889.2000 · Cited by 304

Combining the polymerase incomplete primer extension method for cloning and mutagenesis with microscreening to accelerate structural genomics efforts

Klock, H. E., Koesema, E. J., Knuth, M. W., & Lesley, S. A. (2008) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.21786 · Cited by 284

The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures

Vera, A., González‐Montalbán, N., Arís, A., & Villaverde, A. (2007) · Biotechnology and Bioengineering · doi:10.1002/bit.21218 · Cited by 258

Protein expression systems for structural genomics and proteomics

Yokoyama, S. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00019-4 · Cited by 255

Strategies for protein coexpression in Escherichia coli

Tolia, N. H., & Joshua‐Tor, L. (2005) · Nature Methods · doi:10.1038/nmeth0106-55 · Cited by 246

His-tag impact on structure

Carson, M., Johnson, D. H., McDonald, H., Brouillette, C., & DeLucas, L. J. (2007) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906052024 · Cited by 240

A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing.

Carrington, J. C., & Dougherty, W. G. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.10.3391 · Cited by 235

Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography

Bolaños-García, V. M., & Davies, O. R. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.03.027 · Cited by 232

Real-time observation of trigger factor function on translating ribosomes

Kaiser, C. M., Chang, H.-C., Agashe, V. R., Lakshmipathy, S. K., Etchells, S. A., Hayer-Hartl, M., Hartl, F. U., & Barral, J. M. (2006) · Nature · doi:10.1038/nature05225 · Cited by 231

Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost

Peti, W., & Page, R. (2007) · Protein Expression and Purification · doi:10.1016/j.pep.2006.06.024 · Cited by 225

Vectors for co-expression of an unrestricted number of proteins

Scheich, C., Kümmel, D., Soumailakakis, D., Heinemann, U., & Büssow, K. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm067 · Cited by 209

Structure and Substrate Specificity of the Pim-1 Kinase

Bullock, A. N., Debreczeni, J. E., Amos, A. L., Knapp, S., & Turk, B. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510711200 · Cited by 206

Protein NMR spectroscopy in structural genomics.

Montelione, G. T., Zheng, D., Huang, Y. J., Gunsalus, K. C., & Szyperski, T. (2000) · Nature Structural Biology · doi:10.1038/80768 · Cited by 196

Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners

Nallamsetty, S., & Waugh, D. S. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2005.06.012 · Cited by 193

High‐throughput automated refolding screening of inclusion bodies

Vincentelli, R., Canaan, S., Campanacci, V., Valencia, C., Maurin, D., Frassinetti, F., Scappuccini‐Calvo, L., Bourne, Y., Cambillau, C., & Bignon, C. (2004) · Protein Science · doi:10.1110/ps.04806004 · Cited by 172

High-Throughput Proteomics: Protein Expression and Purification in the Postgenomic World

Lesley, S. A. (2001) · Protein Expression and Purification · doi:10.1006/prep.2001.1465 · Cited by 171

High throughput protein production for functional proteomics

Braun, P., & LaBaer, J. (2003) · Trends in Biotechnology · doi:10.1016/s0167-7799(03)00189-6 · Cited by 170

Crystal structure of the SOCS2–elongin C–elongin B complex defines a prototypical SOCS box ubiquitin ligase

Bullock, A. N., Debreczeni, J. E., Edwards, A. M., Sundström, M., & Knapp, S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601638103 · Cited by 170

Recombinant protein expression and solubility screening in Escherichia coli : a comparative study

Berrow, N. S., Büssow, K., Coutard, B., Diprose, J. M., Ekberg, M., Folkers, G. E., Levy, N., Lieu, V., Owens, R. J., Peleg, Y., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906031337 · Cited by 151

Fusion proteins in biotechnology

Uhlén, M., Forsberg, G., Moks, T., Hartmanis, M. G. N., & Nilsson, B. (1992) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(92)90164-e · Cited by 148

Co-expression of protein complexes in prokaryotic and eukaryotic hosts: experimental procedures, database tracking and case studies

Romier, C., Jelloul, M. B., Albeck, S., Buchwald, G., Busso, D., Celie, P. H. N., Christodoulou, E., Marco, V. D., van Gerwen, S., Knipscheer, P., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906031003 · Cited by 140

An efficient mammalian cell-free translation system supplemented with translation factors

Mikami, S., Masutani, M., Sonenberg, N., Yokoyama, S., & Imataka, H. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.09.021 · Cited by 133

Robotic cloning and protein production platform of the northeast structural genomics consortium

Acton, T. B., Gunsalus, K. C., Xiao, R., Ma, L. C., Aramini, J., Baran, M. C., Chiang, Y.-W., Climent, T., Cooper, B., Denissova, N. G., et al. (2005) · Methods in Enzymology · doi:10.1016/s0076-6879(05)94008-1 · Cited by 129

The use of systematic N- and C-terminal deletions to promote production and structural studies of recombinant proteins

Gräslund, S., Sagemark, J., Berglund, H., Dahlgren, L. G., Flores, A., Hammarström, M., Johansson, I., Kotenyova, T., Nilsson, M. E., Nordlund, P., et al. (2007) · Protein Expression and Purification · doi:10.1016/j.pep.2007.11.008 · Cited by 127

High-throughput screening for expression of heterologous proteins in the yeast Pichia pastoris

Boettner, M., Prinz, B., Holz, C., et al. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(02)00157-8 · Cited by 123

A generic protocol for the expression and purification of recombinant proteins in Escherichia coli using a combinatorial His6-maltose binding protein fusion tag

Nallamsetty, S., & Waugh, D. S. (2007) · Nature Protocols · doi:10.1038/nprot.2007.50 · Cited by 111

Facilities and Methods for the High-Throughput Crystal Structural Analysis of Human Proteins

Heinemann, U., Büssow, K., Müeller, U., et al. (2003) · Accounts of Chemical Research · doi:10.1021/ar010129t · Cited by 98

Eukaryotic expression: developments for structural proteomics

Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T.-C., Davis, S. J., Dubrovsky, A. L., Gustafsson, L., Hedfalk, K., Heinemann, U., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906029805 · Cited by 97

Generation of an AraC-araBAD Promoter-Regulated T7 Expression System

Wycuff, D. R., & Matthews, K. S. (2000) · Analytical Biochemistry · doi:10.1006/abio.1999.4385 · Cited by 91

The impact of protein characterization in structural proteomics

Geerlof, A., Brown, J., Coutard, B., Egloff, M. P., Enguita, F. J., Fogg, M. J., Gilbert, R. J. C., Groves, M. R., Haouz, A., Nettleship, J. E., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906030307 · Cited by 81

Investigation of protein refolding using a fractional factorial screen: A study of reagent effects and interactions

Willis, M. S., Hogan, J. K., Prabhakar, P., Liu, X., Tsai, K., Wei, Y., & Fox, T. (2005) · Protein Science · doi:10.1110/ps.051433205 · Cited by 74

The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins

Gileadi, O., Knapp, S., Lee, W. H., Marsden, B. D., Müller, S., Niesen, F., Kavanagh, K. L., Ball, L., von Delft, F., Doyle, D., et al. (2007) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-007-9027-2 · Cited by 64

An evaluation of in vitro protein–protein interaction techniques: Assessing contaminating background proteins

Howell, J., Winstone, T. M. L., Coorssen, J. R., & Turner, R. J. (2006) · PROTEOMICS · doi:10.1002/pmic.200500517 · Cited by 61

Structural genomics of human proteins – target selection and generation of a public catalogue of expression clones

Büssow, K., Scheich, C., Sievert, V., Harttig, U., Schultz, J., Simon, B., Peer Bork, B., Lehrach, H. R., & Heinemann, U. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-21 · Cited by 61

Implementation of semi-automated cloning and prokaryotic expression screening: the impact of SPINE

Alzari, P. M., Berglund, H., Berrow, N. S., Blagova, E. V., Busso, D., Cambillau, C., Campanacci, V., Christodoulou, E., Eiler, S., Fogg, M. J., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906029775 · Cited by 59

Crystal Structure of the Rac Activator, Asef, Reveals Its Autoinhibitory Mechanism

Murayama, K., Shirouzu, M., Kawasaki, Y., Kato-Murayama, M., Hanawa‐Suetsugu, K., Sakamoto, A., Katsura, Y., Suenaga, A., Toyama, M., Terada, T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600234200 · Cited by 57

Construct for High-Level Expression and Low Misincorporation of Lysine for Arginine During Expression of pET-Encoded Eukaryotic Proteins in Escherichia coli

You, J., Cohen, R. E., & Pickart, C. M. (1999) · BioTechniques · doi:10.2144/99275st01 · Cited by 55

Novel protein fold discovered in the PabI family of restriction enzymes

Miyazono, K., Watanabe, M., Kosiński, J., Ishikawa, K., Kamo, M., Sawasaki, T., Nagata, K., Bujnicki, J. M., Endo, Y., Tanokura, M., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm091 · Cited by 48

Structural proteomics of the SARS coronavirus: a model response to emerging infectious diseases

Bartlam, M. G., Xu, Y., & Rao, Z. (2007) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-007-9024-5 · Cited by 42

Cell-free synthesis of zinc-binding proteins

Matsuda, T., Kigawa, T., Koshiba, S., Inoue, M., Aoki, M., Yamasaki, K., Seki, M., Shinozaki, K., & Yokoyama, S. (2006) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-006-9012-1 · Cited by 39

High Throughput Protein Production and Crystallization at NYSGXRC

Sauder, M. J., Rutter, M. E., Bain, K. T., Rooney, I. A., Gheyi, T., Atwell, S., Thompson, D. A., Emtage, S., & Burley, S. K. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-058-8_37 · Cited by 35

First steps towards effective methods in exploiting high-throughput technologies for the determination of human protein structures of high biomedical value

Banci, L., Bertini, I., Cusack, S., de Jong, R. N., Heinemann, U., Jones, E. Y., Kozielski, F., Maskos, K., Messerschmidt, A., Owens, R. J., et al. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906029350 · Cited by 34

Scalable High-Throughput Micro-Expression Device for Recombinant Proteins

Page, R., Moy, K., Sims, E., Velasquez, J., McManus, B., Grittini, C., Clayton, T., & Stevens, R. C. (2004) · BioTechniques · doi:10.2144/04373bm05 · Cited by 30

Plant Transformation by Agrobacterium tumefaciens

Frenkiel‐Krispin, D., Wolf, S. G., Albeck, S., Unger, T., Peleg, Y., Jacobovitch, J., Michael, Y., Daube, S. S., Sharon, M., Robinson, C. V., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605270200 · Cited by 28

Structural Genomics of Minimal Organisms and Protein Fold Space

Kim, S., Shin, D. H., Liu, J., Oganesyan, V., Chen, S., Xu, Q. S., Kim, J.-S., Das, D., Schulze‐Gahmen, U., Holbrook, S. R., et al. (2005) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-005-2651-9 · Cited by 26

Genomics, Proteomics and Vaccines

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High-level production and optimization of monodispersity of 11β-hydroxysteroid dehydrogenase type 1

Elleby, B., Svensson, S., Wu, X., Stefansson, K., Nilsson, J., Hallén, D., Oppermann, U. C. T., & Abrahmsén, L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.05.003 · Cited by 21

Facilities and Methods for the High‐Throughput Crystal Structural Analysis of Human Proteins

Heinemann, U., Buessow, K., Müeller, U., & Umbach, P. (2003) · ChemInform · doi:10.1002/chin.200320290 · Cited by 12

Structural genomics efforts at the Chinese Academy of Sciences and Peking University

Gong, W. M., Liu, H. Y., Niu, L., et al. (2003) · Journal of Structural and Functional Genomics · doi:10.1023/a:1026152612590 · Cited by 10

Three-dimensional structure determination of proteins related to human health in their functional context at The Israel Structural Proteomics Center (ISPC)

Albeck, S., Burstein, Y., Dym, O., Jacobovitch, Y., Levi, N., Meged, R., Michael, Y., Peleg, Y., Prilusky, J., Schreiber, G., et al. (2005) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905023565 · Cited by 10

An evolutionarily conserved mechanism for controlling the efficiency of protein translation

Tuller, T., Carmi, A., Vestsigian, K., Navon, S., Dorfan, Y., Zaborske, J., Pan, T., Dahan, O., Furman, I., & Pilpel, Y. (2010) · Cell · doi:10.1016/j.cell.2010.03.031 · Cited by 874

New tools for recombinant protein production in Escherichia coli: A 5‐year update

Rosano, G. L., Morales, E. S., & Ceccarelli, E. A. (2019) · Protein Science · doi:10.1002/pro.3668 · Cited by 372

Cultivation strategies to enhance productivity of Pichia pastoris: A review

Looser, V., Bruhlmann, B., Bumbak, F., Stenger, C., Costa, M., Camattari, A., Fotiadis, D., & Kovar, K. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.05.008 · Cited by 350

High-throughput recombinant protein expression in Escherichia coli : current status and future perspectives

Jia, B., & Jeon, C. O. (2016) · Open Biology · doi:10.1098/rsob.160196 · Cited by 295

Strategies to Optimize Protein Expression in E. coli

Francis, D. M., & Page, R. (2010) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps0524s61 · Cited by 272