Multiple Post-translational Modifications Affect Heterologous Protein Synthesis

The PyMOL Molecular Graphics System

DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · see citing works

The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling

Arnold, K., Bordoli, L., Kopp, J., & Schwede, T. F. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti770 · Cited by 6,951 · see citing works

SWISS-MODEL: an automated protein homology-modeling server

Schwede, T. F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg520 · Cited by 5,592 · see citing works

Prediction of post‐translational glycosylation and phosphorylation of proteins from the amino acid sequence

Blom, N., Sicheritz‐Pontén, T., Gupta, R., Gammeltoft, S., & Brunak, S. (2004) · PROTEOMICS · doi:10.1002/pmic.200300771 · Cited by 2,076 · see citing works

Recombinant protein folding and misfolding in Escherichia coli

Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,488 · see citing works

Oxidative protein folding in eukaryotes

Tu, B. P., & Weissman, J. S. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200311055 · Cited by 1,041 · see citing works

Post-translational modifications in the context of therapeutic proteins

Walsh, G., & Jefferis, R. (2006) · Nature Biotechnology · doi:10.1038/nbt1252 · Cited by 1,007 · see citing works

PROSITE: a documented database using patterns and profiles as motif descriptors

Sigrist, C. J. A. (2002) · Briefings in Bioinformatics · doi:10.1093/bib/3.3.265 · Cited by 913 · cited 3× · see citing works

Insights into the Molecular Basis of Leukocyte Tethering and Rolling Revealed by Structures of P- and E-Selectin Bound to SLeX and PSGL-1

Somers, W. S., Tang, J. H., Shaw, G. D., & Camphausen, R. T. (2000) · Cell · doi:10.1016/s0092-8674(00)00138-0 · Cited by 738 · see citing works

Mechanisms and principles of N-linked protein glycosylation

Schwarz, F., & Aebi, M. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.005 · Cited by 695 · see citing works

Tyrosine phosphorylation: thirty years and counting

Hunter, T. R. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.01.028 · Cited by 655 · see citing works

Identification, analysis, and prediction of protein ubiquitination sites

Predrag Radivojac, A., Vacic, V., Haynes, C. A., Cocklin, R., Mohan, A., Heyen, J. W., Goebl, M. G., & Iakoucheva, L. M. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22555 · Cited by 577 · see citing works

SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins

Malakhov, M. P., Mattern, M. R., Malakhova, O. A., Drinker, M. S., Weeks, S. D., & Butt, T. R. (2004) · Journal of Structural and Functional Genomics · doi:10.1023/b:jsfg.0000029237.70316.52 · Cited by 541 · see citing works

CSS-Palm 2.0: an updated software for palmitoylation sites prediction

Ren, J., Wen, L., Gao, X., Jin, C., Xue, Y., & Yao, X. (2008) · Protein Engineering Design and Selection · doi:10.1093/protein/gzn039 · Cited by 536 · see citing works

Protein glycosylation in bacteria: sweeter than ever

Nothaft, H., & Szymanski, C. M. (2010) · Nature Reviews Microbiology · doi:10.1038/nrmicro2383 · Cited by 531 · see citing works

A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes

Madin, K., Sawasaki, T., Ogasawara, T., & Endo, Y. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.559 · Cited by 467 · see citing works

ScanProsite: a reference implementation of a PROSITE scanning tool.

Gattiker, A., Gasteiger, E., & Bairoch, A. (2002) · PubMed · Cited by 432 · see citing works

The Proteomics of N-terminal Methionine Cleavage

Frottin, F., Martinez, A., Peynot, P., Mitra, S., Holz, R. C., Giglione, C., & Meinnel, T. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600225-mcp200 · Cited by 385 · see citing works

A curated compendium of phosphorylation motifs

Amanchy, R., Periaswamy, B., Mathivanan, S., Reddy, R., Tattikota, S. G., & Pandey, A. (2007) · Nature Biotechnology · doi:10.1038/nbt0307-285 · Cited by 372 · see citing works

The Biology and Enzymology of Protein Tyrosine O-Sulfation

Moore, K. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r300008200 · Cited by 360 · see citing works

Protein Prenylation: a Mediator of Protein-Protein Interactions

Marshall, C. J. (1993) · Science · doi:10.1126/science.8456312 · Cited by 353 · see citing works

The past, present and future of cell-free protein synthesis

Katzen, F., Chang, G. A., & Kudlicki, W. A. (2005) · Trends in biotechnology · doi:10.1016/j.tibtech.2005.01.003 · Cited by 341 · see citing works

Structural genomics projects in Japan.

Yokoyama, S., Hirota, H., Kigawa, T., Yabuki, T., Shirouzu, M., Terada, T., Ito, Y., Matsuo, Y., Kuroda, Y., Nishimura, Y., et al. (2000) · Nature Structural Biology · doi:10.1038/80712 · Cited by 336 · see citing works

Genomic analysis of the eukaryotic protein kinase superfamily: a perspective.

Hanks, S. K. (2003) · Genome biology · doi:10.1186/gb-2003-4-5-111 · Cited by 328 · see citing works

Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of <i>Escherichia coli</i> proteins

Niwa, T., Ying, B.-W., Saito, K., Jin, W., Takada, S., Ueda, T., & Taguchi, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811922106 · Cited by 321 · see citing works

N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

Mitra, N., Sinha, S., Ramya, T. N. C., & Surolia, A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.003 · Cited by 302 · see citing works

An efficient system for high‐level expression and easy purification of authentic recombinant proteins

Catanzariti, A., Soboleva, T., Jans, D. A., Philip G. Board, & Baker, R. T. (2004) · Protein Science · doi:10.1110/ps.04618904 · Cited by 298 · see citing works

Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

Cockman, M. E., Lancaster, D. E., Stolze, I. P., Hewitson, K. S., McDonough, M. A., Coleman, M. L., Coles, C. H., Yu, X., Hay, R. T., Ley, S. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606877103 · Cited by 285 · see citing works

Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression

Dyson, M. R., Shadbolt, S. P., Vincent, K. J., Perera, R. L., & McCafferty, J. (2004) · BMC Biotechnology · doi:10.1186/1472-6750-4-32 · Cited by 272 · see citing works

Phosphoprotein Analysis Using Antibodies Broadly Reactive against Phosphorylated Motifs

Zhang, H., Zha, X., Tan, Y., Hornbeck, P. V., Mastrangelo, A. J., Alessi, D. R., Polakiewicz, R. D., & Comb, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206399200 · Cited by 271 · see citing works

Systematic study of protein sumoylation: Development of a site‐specific predictor of SUMOsp 2.0

Ren, J. M., Gao, X., Jin, C., Mei, Z., Wang, X., Shaw, A., Wen, L., Yao, X., & Xue, Y. (2009) · PROTEOMICS · doi:10.1002/pmic.200800646 · Cited by 262 · see citing works

Proteome-scale purification of human proteins from bacteria

Falter‐Braun, P., Hu, Y., Shen, B., Halleck, A., Koundinya, M., Harlow, E., & LaBaer, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042684199 · Cited by 261 · see citing works

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 · see citing works

SUMOsp: a web server for sumoylation site prediction

Xue, Y., Zhou, F., Fu, C., Xu, Y., & Yao, X. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl207 · Cited by 212 · see citing works

High-throughput cell-free systems for synthesis of functionally active proteins

Spirin, A. S. (2004) · Trends in biotechnology · doi:10.1016/j.tibtech.2004.08.012 · Cited by 201 · see citing works

Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems

Wacker, M., Feldman, M. F., Callewaert, N., Kowarik, M., Clarke, B. R., Pohl, N. L. B., Hernandez, M., Vinés, E. D., Valvano, M. A., Whitfield, C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509207103 · Cited by 195 · see citing works

Understanding the relationship between the primary structure of proteins and its propensity to be soluble on overexpression in <i>Escherichia coli</i>

Idicula‐Thomas, S., & Balaji, P. V. (2005) · Protein Science · doi:10.1110/ps.041009005 · Cited by 175 · see citing works

Extent of N‐terminal modifications in cytosolic proteins from eukaryotes

Martinez, A., Traverso, J. A., Valot, B., Ferro, M., Espagne, C., Ephritikhine, G., Zivy, M., Giglione, C., & Meinnel, T. (2008) · PROTEOMICS · doi:10.1002/pmic.200701191 · Cited by 158 · see citing works

Large‐scale prediction of disulphide bridges using kernel methods, two‐dimensional recursive neural networks, and weighted graph matching

Cheng, J. J., Saigo, H., & Baldi, P. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20787 · Cited by 155 · see citing works

NetAcet: prediction of N-terminal acetylation sites

Kiemer, L., Bendtsen, J. D., & Blom, N. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bti130 · Cited by 148 · see citing works

Efficient production of a bioactive, multiple disulfide‐bonded protein using modified extracts of Escherichia coli

Kim, D., & Swartz, J. R. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10865 · Cited by 145 · see citing works

Mining the Structural Genomics Pipeline: Identification of Protein Properties that Affect High-throughput Experimental Analysis

Goh, C.-S., Lan, N., Douglas, S. M., Wu, B., Echols, N., Smith, A. A., Milburn, D., Montelione, G. T., Zhao, H., & Gerstein, M. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.11.053 · Cited by 144 · see citing works

Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis

Saracco, S. A., Hansson, M. C., Scalf, M., Walker, J. M., Smith, L. M., & Vierstra, R. D. (2009) · The Plant Journal · doi:10.1111/j.1365-313x.2009.03862.x · Cited by 143 · see citing works

Quality and authenticity of heterologous proteins synthesized in yeast

Eckart, M. R., & Bussineau, C. M. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80056-5 · Cited by 133 · see citing works

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 128 · see citing works

The Swiss-3DImage collection and PDB-Browser on the World-Wide Web

Peitsch, M. C. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)88963-x · Cited by 127 · see citing works

Target selection for structural genomics.

Brenner, S. E. (2000) · Nature Structural Biology · doi:10.1038/80747 · Cited by 123 · see citing works

SPINE: an integrated tracking database and data mining approach for identifying feasible targets in high-throughput structural proteomics

Bertone, P. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.13.2884 · Cited by 120 · see citing works

Cell‐Free Protein Synthesis System Prepared from Insect Cells by Freeze‐Thawing

Ezure, T., Suzuki, T., Higashide, S., Shintani, E., Endo, K., Kobayashi, S., Shikata, M., Ito, M., Tanimizu, K., & Nishimura, O. (2006) · Biotechnology Progress · doi:10.1021/bp060110v · Cited by 114 · see citing works

Toward a framework for sulfoproteomics: Synthesis and characterization of sulfotyrosine‐containing peptides

Seibert, C., & Sakmar, T. P. (2007) · Biopolymers · doi:10.1002/bip.20821 · Cited by 107 · see citing works

A support vector machine-based method for predicting the propensity of a protein to be soluble or to form inclusion body on overexpression in Escherichia coli

Idicula‐Thomas, S., Kulkarni, A. J., Kulkarni, B. D., Valadi, J. K., & Balaji, P. V. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti810 · Cited by 104 · see citing works

CAAX-box protein, prenylation process and carcinogenesis.

Gao, J., Liao, J., & Yang, G. (2009) · PubMed Central · Cited by 103 · see citing works

Cell-free protein synthesis: applications in proteomics and biotechnology

He, M. (2008) · New Biotechnology · doi:10.1016/j.nbt.2008.08.004 · Cited by 79 · see citing works

Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs.

Kloog, Y., & Cox, A. (2004) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2004.04.004 · Cited by 74 · see citing works

Arginine 336 and Asparagine 333 of the Human Cholecystokinin-A Receptor Binding Site Interact with the Penultimate Aspartic Acid and the C-terminal Amide of Cholecystokinin

Gigoux, V., Escrieut, C., Fehrentz, J., Silvente‐Poirot, S., Maigret, B., Moroder, L., Gully, D., Martínez, J., Vaysse, N., & Fourmy, D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20457 · Cited by 74 · see citing works

A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins

Mikami, S., Kobayashi, T., Yokoyama, S., & Imataka, H. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.06.018 · Cited by 68 · see citing works

Parallel cloning, expression, purification and crystallization of human proteins for structural genomics

Ding, H., Ren, H. J., Chen, Q., Fang, G., Li, L.-F., Li, R., Wang, Z., Jia, X., Liang, Y., Meihao, H., et al. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016359 · Cited by 41 · see citing works

Structural function of C‐terminal amidation of endomorphin

In, Y., Minoura, K., Tomoo, K., Sasaki, Y., Lazarus, L. H., Okada, Y., & Ishida, T. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04919.x · Cited by 33 · see citing works

Cell-Free Protein Synthesis

Spirin, A. S. (2002) · Springer eBooks · doi:10.1007/978-3-642-59379-6_1 · Cited by 32 · see citing works

Categorical data analysis in experimental biology

Xu, B., Feng, X., & Burdine, R. D. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.08.018 · Cited by 32 · see citing works

Target Selection for Structural Genomics: An Overview

Marsden, R. L., & Orengo, C. A. (2008) · Methods in molecular biology · doi:10.1007/978-1-60327-058-8_1 · Cited by 29 · see citing works

Conformational Ensembles: The Role of Neuropeptide Structures in Receptor Binding

Edison, A. S., Espinoza, E., & Zachariah, C. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-15-06318.1999 · Cited by 29 · see citing works

Heterologous and Cell-Free Protein Expression Systems

Farrokhi, N., Hrmová, M., Burton, R. A., & Fincher, G. B. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-427-8_10 · Cited by 29 · see citing works

Protein prenylation: A new mode of host–pathogen interaction

Amaya, M., Baranova, A. V., & van Hoek, M. L. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.142 · Cited by 28 · see citing works

Comprehensive bioinformatics analysis of cell‐free protein synthesis: identification of multiple protein properties that correlate with successful expression

Kurotani, A., Takagi, T., Toyama, M., Shirouzu, M., Yokoyama, S., Fukami, Y., & Tokmakov, A. A. (2009) · The FASEB Journal · doi:10.1096/fj.09-139527 · Cited by 21 · see citing works

Thirty years and counting

Parkinson, L. (2013) · Australian Journal on Ageing · doi:10.1111/ajag.12110 · Cited by 19 · see citing works

[RIKEN structural genomics/proteomics initiative].

Yokoyama, S., Kigawa, T., Shirouzu, M., Miyano, M., & Kuramitsu, S. (2008) · PubMed · Cited by 12 · see citing works

Use of Reticulocyte Lysates for Mechanistic Studies of Eukaryotic Translation Initiation

Merrick, W. C., & Baus, D. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)29001-9 · Cited by 10 · see citing works

ProteoMix: an integrated and flexible system for interactively analyzing large numbers of protein sequences

Chikayama, E., Kurotani, A., Kuroda, Y., & Yokoyama, S. (2004) · Bioinformatics · doi:10.1093/bioinformatics/bth276 · Cited by 8 · see citing works

[Large-scale structural proteomics project at RIKEN: present and future].

Yokoyama, S. (2005) · PubMed · Cited by 3 · see citing works

Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter

Darling, A., & Uversky, V. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00158 · Cited by 236 · see citing works

Cell-free synthetic biology: Engineering in an open world

Lu, Y. (2017) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2017.02.003 · Cited by 167 · see citing works

Yeasts as probiotics: Mechanisms, outcomes, and future potential

Sen, S., & Mansell, T. J. (2020) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2020.103333 · Cited by 162 · see citing works

Synthetic Biology: Bottom-Up Assembly of Molecular Systems

Hirschi, S., Ward, T. R., Meier, W. P., Müller, D. J., & Fotiadis, D. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00339 · Cited by 149 · see citing works

GAPDH controls extracellular vesicle biogenesis and enhances the therapeutic potential of EV mediated siRNA delivery to the brain

Dar, G. H., Mendes, C. C., Kuan, W.-L., Speciale, A. A., Conceição, M., Görgens, A., Uliyakina, I., Lobo, M. J., Lim, W. F., EL Andaloussi, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27056-3 · Cited by 100 · see citing works

Sources, purification, immobilization and industrial applications of microbial lipases: An overview

Enespa, Chandra, P., & Singh, D. P. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2038076 · Cited by 67 · see citing works

A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins

Fatima, K., Naqvi, F., & Younas, H. (2021) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-021-00970-5 · Cited by 66 · see citing works

Versatile phenotype-activated cell sorting

Lee, J., Liu, Z., Suzuki, P., Ahrens, J. F., Lai, S., Lu, X., Guan, S. A., & St-Pierre, F. (2020) · Science Advances · doi:10.1126/sciadv.abb7438 · Cited by 65 · see citing works

Aptamer Technology: Adjunct Therapy for Malaria

Kamarudin, N. A. A. N., Mohammed, N., & Mustaffa, K. M. F. (2017) · Biomedicines · doi:10.3390/biomedicines5010001 · Cited by 54 · see citing works

Trends and prospects in dairy protein replacement in yogurt and cheese

Diaz-Bustamante, M. L., Keppler, J. K., Reyes, L. H., & Alvarez Solano, O. A. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e16974 · Cited by 48 · see citing works

Unstructural Biology of TRP Ion Channels: The Role of Intrinsically Disordered Regions in Channel Function and Regulation

Goretzki, B., Guhl, C., Tebbe, F., Harder, J.-M., & Hellmich, U. A. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166931 · Cited by 48 · see citing works

HBD-2 binds SARS-CoV-2 RBD and blocks viral entry: Strategy to combat COVID-19

Zhang, L., Ghosh, S. K., Basavarajappa, S. C., Chen, Y., Shrestha, P., Penfield, J., Brewer, A., Ramakrishnan, P., Buck, M., & Weinberg, A. (2022) · iScience · doi:10.1016/j.isci.2022.103856 · Cited by 43 · see citing works

Characterization of recombinant laccase from Trametes versicolor synthesized by Arxula adeninivorans and its application in the degradation of pharmaceuticals

Litwińska, K., Bischoff, F., Matthes, F., Bode, R., Rutten, T. L. M., & Kunze, G. (2019) · AMB Express · doi:10.1186/s13568-019-0832-3 · Cited by 38 · see citing works

3-Bromotetrazine: labelling of macromolecules via monosubstituted bifunctional s -tetrazines

Schnell, S. D., Hoff, L. V., Panchagnula, A., Wurzenberger, M. H. H., Klapötke, T. M., Sieber, S., Linden, A., & Gademann, K. (2020) · Chemical Science · doi:10.1039/c9sc06169j · Cited by 34 · see citing works

Harnessing Transient Expression Systems with Plant Viral Vectors for the Production of Biopharmaceuticals in Nicotiana benthamiana

Akher, S. A., Wang, K., Hall, K., Hunpatin, O. S., Shan, M., Zhang, Z.-L., & Guo, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26125510 · Cited by 29 · see citing works

The cell-free system: A new apparatus for affordable, sensitive, and portable healthcare

Copeland, C. E., Langlois, A., Kim, J., & Kwon, Y. (2021) · Biochemical Engineering Journal · doi:10.1016/j.bej.2021.108124 · Cited by 31 · see citing works

The Current Status and Future Applications of Hairy Root Cultures

Dhiman, N., Patial, V., & Bhattacharya, A. (2018) · Springer eBooks · doi:10.1007/978-981-13-0535-1_5 · Cited by 28 · see citing works

Chemical Protein Synthesis by Native Chemical Ligation and Variations Thereof

Wang, S., Thopate, Y. A., Zhou, Q., & Wang, P. (2019) · Chinese Journal of Chemistry · doi:10.1002/cjoc.201900246 · Cited by 27 · see citing works

Investigation of the impact of PTMs on the protein backbone conformation

Craveur, P., Narwani, T., Rebehmed, J., & de Brevern, A. G. (2019) · Amino Acids · doi:10.1007/s00726-019-02747-w · Cited by 26 · see citing works

Cortactin in Lung Cell Function and Disease

Bandela, M., Belvitch, P. G., Garcia, J. G. N., & Dudek, S. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094606 · Cited by 25 · see citing works

Studying macromolecular complex stoichiometries by peptide‐based mass spectrometry

Wohlgemuth, I., Lenz, C., & Urlaub, H. (2014) · PROTEOMICS · doi:10.1002/pmic.201400466 · Cited by 25 · see citing works

The Bioengineering of Insect Cell Lines for Biotherapeutics and Vaccine Production: An Updated Review

Sułek, M., & Szuster‐Ciesielska, A. (2025) · Vaccines · doi:10.3390/vaccines13060556 · Cited by 21 · see citing works

Steric pressure between glycosylated transmembrane proteins inhibits internalization by endocytosis

Gollapudi, S., Jamal, S., Kamatar, A., Yuan, F., Wang, L., Lafer, E. M., Belardi, B., & Stachowiak, J. C. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2215815120 · Cited by 19 · see citing works

Salmonella enterica and outer membrane vesicles are current and future options for cancer treatment

Jorge, G. P., Gontijo, M. T. P., & Brocchi, M. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1293351 · Cited by 19 · see citing works

Synergistic role of nucleotides and lipids for the self-assembly of Shs1 septin oligomers

Taveneau, C., Blanc, R., Pehau‐Arnaudet, G., Cicco, A. D., & Bertin, A. (2020) · Biochemical Journal · doi:10.1042/bcj20200199 · Cited by 18 · see citing works

Serological antibody testing in the COVID-19 pandemic: their molecular basis and applications

Jiang, J.-C., & Zhang, Y. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200744 · Cited by 18 · see citing works

Novel human cell expression method reveals the role and prevalence of posttranslational modification in nonmuscle tropomyosins

Carman, P. J., Barrie, K. R., & Domínguez, R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101154 · Cited by 18 · see citing works

Advances in RNAi-Assisted Strain Engineering in Saccharomyces cerevisiae

Chen, Y., Guo, E., Zhang, J., & Si, T. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00731 · Cited by 17 · see citing works

Trends and Applications of Omics Technologies to Functional Characterisation of Enzymes and Protein Metabolites Produced by Fungi

Ijoma, G., Heri, S., Matambo, T., & Tekere, M. (2021) · Journal of Fungi · doi:10.3390/jof7090700 · Cited by 13 · see citing works

Identification of juvenile hormone-induced posttranslational modifications of methoprene tolerant and Krüppel homolog 1 in the yellow fever mosquito, Aedes aegypti

Kim, K., Albishi, N. M., & Palli, S. R. (2021) · Journal of Proteomics · doi:10.1016/j.jprot.2021.104257 · Cited by 15 · see citing works

Molecular characterization of diverse defensins (γ-thionins) from Capsicum annuum flowers and their effects on the insect pest Helicoverpa armigera

Mulla, J. A., Kibe, A., Deore, D. D., Jadhav, A. R., & Tamhane, V. A. (2021) · Plant Gene · doi:10.1016/j.plgene.2021.100284 · Cited by 15 · see citing works

The GTP-bound and Sumoylated Form of the rab17 Small Molecular Weight GTPase Selectively Binds Syntaxin 2 in Polarized Hepatic WIF-B Cells

Striz, A., & Tuma, P. L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.723353 · Cited by 15 · see citing works

Enhancing Protein Solubility via Glycosylation: From Chemical Synthesis to Machine Learning Predictions

Ma, B., Chen, H., Gong, J., Liu, W., Wei, X., Zhang, Y., Li, X., Li, M., Wang, Y., Shang, S., et al. (2024) · Biomacromolecules · doi:10.1021/acs.biomac.4c00134 · Cited by 13 · see citing works

Amino acid sequence encodes protein abundance shaped by protein stability at reduced synthesis cost

(2024) · doi:10.1002/pro.5239 · Cited by 12 · see citing works

Content of intrinsic disorder influences the outcome of cell-free protein synthesis

Tokmakov, A. A., Kurotani, A., Ikeda, M., Terazawa, Y., Shirouzu, M., Стефанов, В. Е., Sakurai, T., & Yokoyama, S. (2015) · Scientific Reports · doi:10.1038/srep14079 · Cited by 12 · see citing works

Optimization, characterization, comparison of self-assembly VLP of capsid protein L1 in yeast and reverse vaccinology design against human papillomavirus type 52

Firdaus, M. E. R., Mustopa, A. Z., Ekawati, N., Chairunnisa, S., Arifah, R. K., Hertati, A., Irawan, S., Prastyowati, A., Kusumawati, A., & Nurfatwa, M. (2023) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-023-00514-9 · Cited by 12 · see citing works

Reductive site-selective atypical C , Z -type/N2-C2 cleavage allows C-terminal protein amidation

Mollner, T. A., Giltrap, A. M., Zeng, Y., Demyanenko, Y., Buchanan, C. J., Oehlrich, D., Baldwin, A. J., Anthony, D. C., Mohammed, S., & Davis, B. G. (2022) · Science Advances · doi:10.1126/sciadv.abl8675 · Cited by 11 · see citing works

Structural biology workflow for the expression and characterization of functional human sodium glucose transporter type 1 in Pichia pastoris

Suades, A., Alcaraz, A., Cruz, E., Álvarez-Marimon, E., Whitelegge, J. P., Manyosa, J., Cladera, J., & Perálvarez‐Marín, A. (2019) · Scientific Reports · doi:10.1038/s41598-018-37445-2 · Cited by 11 · see citing works

Metabolic Engineering for Production of Small Molecule Drugs: Challenges and Solutions

Huttanus, H. M., Sheng, J., & Feng, X. (2016) · Fermentation · doi:10.3390/fermentation2010004 · Cited by 10 · see citing works

Towards automation in biologics production via Raman micro-spectroscopy, laser-induced forward cell transfer and surface-enhanced Raman spectroscopy

Jaeckle, E., Brauchle, E., Nottrodt, N., Wehner, M. M., Lensing, R., Gillner, A., Schenke‐Layland, K., Bach, M., & Burger‐Kentischer, A. (2020) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2020.09.001 · Cited by 9 · see citing works

Octaketide Synthase from Polygonum cuspidatum Implements Emodin Biosynthesis in Arabidopsis thaliana

Guo, Y., Nassar, S., Ma, L., Feng, G., Li, X., Chen, M., Chai, T., Abdel-Rahman, I. A. M., Beuerle, T., Beerhues, L., et al. (2020) · Plant and Cell Physiology · doi:10.1093/pcp/pcaa135 · Cited by 9 · see citing works

Fundamental concepts of protein therapeutics and spacing in oncology: an updated comprehensive review

Far, B. F., Safaei, M., Mokhtari, F., Fallahi, M. S., & Naimi‐Jamal, M. R. (2023) · Medical Oncology · doi:10.1007/s12032-023-02026-5 · Cited by 9 · see citing works

Heterologous Expression of Xylanase xAor from Aspergillus oryzae in Komagataella phaffii T07

Zadorozhny, A. V., Ushakov, V. S., Розанов, А. С., Bogacheva, N. V., Shlyakhtun, V. N., Voskoboev, M. E., Korzhuk, A. V., Romancev, V. A., Bannikova, S. V., Mescheryakova, I. A., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158741 · Cited by 8 · see citing works

Bioinformatics Analysis and Optimization of Cell-Free Protein Synthesis

Tokmakov, A. A., Kurotani, A., Shirouzu, M., Fukami, Y., & Yokoyama, S. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-782-2_2 · Cited by 8 · see citing works

Nonenzymatic Posttranslational Modifications and Peptide Cleavages Observed in Peptide Epimers

Long, C. C., Antevska, A., Mast, D. H., Okyem, S., Sweedler, J. V., & Do, T. D. (2023) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.3c00092 · Cited by 6 · see citing works

Optimization of the human colorectal carcinoma antigen GA733-2 production in tobacco plants

Park, S. H., Ji, K.-Y., Kim, H. M., Cha, S. H., Park, S., Do, J. H., Oh, D., Kang, H. S., Shim, J. S., & Joung, Y. H. (2021) · Plant Biotechnology Reports · doi:10.1007/s11816-020-00657-y · Cited by 6 · see citing works

Comparison of Two Strategies to Generate Antigen-Specific Human Monoclonal Antibodies: Which Method to Choose for Which Purpose?

Ehlers, A. M., Jager, C. F. D. H., Kardol‐Hoefnagel, T., Katsburg, M., Knulst, A. C., & Otten, H. G. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.660037 · Cited by 6 · see citing works

Genome-wide high-throughput signal peptide screening via plasmid pUC256E improves protease secretion in Lactiplantibacillus plantarum and Pediococcus acidilactici

Chen, B.-B., Loo, B. Z. L., Cheng, Y.-Y., Song, P.-H., Fan, H., Latypov, O., & Kittelmann, S. (2022) · BMC Genomics · doi:10.1186/s12864-022-08292-3 · Cited by 4 · see citing works

Molecular Cloning and Characterization of Mx2 for Early Pregnancy Diagnosis in Bubalus bubalis

Batra, K., Nanda, T., Kumar, A., Gupta, A. K., Kumari, R., Kumar, V., Sheoran, N., & Maan, S. (2018) · Proceedings of the National Academy of Sciences India Section B Biological Sciences · doi:10.1007/s40011-018-0993-x · Cited by 5 · see citing works

Pseudomonas response regulators produced in an E. coli heterologous expression host exhibit host-derived post-translational phosphorylation

Garber, M. E., Ocampo, R. F., Lake, J., Kakouridis, A., & Mukhopadhyay, A. (2022) · Scientific Reports · doi:10.1038/s41598-022-13525-2 · Cited by 5 · see citing works

Cell-Free Expression of a Plant Membrane Protein BrPT2 From Boesenbergia Rotunda

Liew, Y. J. M., Lee, Y. K., Khalid, N., Rahman, N. A., & Tan, B. C. (2021) · Molecular Biotechnology · doi:10.1007/s12033-021-00304-z · Cited by 4 · see citing works

Biochemical studies of the synaptic protein otoferlin

Meese, S. (2015) · doi:10.53846/goediss-5234 · Cited by 4 · see citing works

Usage of Cell-Free Protein Synthesis in Post-Translational Modification of μ-Conopeptide PIIIA

Liu, Y., Zhao, Z., Song, Y., Yin, Y., Wu, F., & Jiang, H. (2023) · Marine Drugs · doi:10.3390/md21080421 · Cited by 3 · see citing works

Synthetic Biology at the Hand of Cell-Free Systems

Pandi, A., Borkowski, O., & Faulon, J. (2020) · Springer eBooks · doi:10.1007/978-981-15-0081-7_16 · Cited by 3 · see citing works

Identification of multiple physicochemical and structural properties associated with soluble expression of eukaryotic proteins in cell-free bacterial extracts

Tokmakov, A. A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00295 · Cited by 3 · see citing works

Bacterial two-hybrid systems evolved: innovations for protein-protein interaction research

Richardson, R. M., & Pascal, S. M. (2025) · Journal of Bacteriology · doi:10.1128/jb.00129-25 · Cited by 3 · see citing works

Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy

Mathai, L., Nair, B. G., & Alangode, A. (2026) · Toxins · doi:10.3390/toxins18070286 · Cited by 2 · see citing works

Protein Ligases: Nature’s Gift for Protein/Peptide Synthesis

Ritsema, Y., Li, H., & Zheng, Q. (2025) · BioChem · doi:10.3390/biochem5020011 · Cited by 2 · see citing works

Predicted N‐terminal N‐linked glycosylation sites may underlie membrane protein expression patterns in Saccharomyces cerevisiae

Karki, R., Rimal, S., & Rieth, M. D. (2021) · Yeast · doi:10.1002/yea.3657 · Cited by 2 · see citing works

Recent trends in fungal dairy fermented foods

Kaur, P., & Dua, K. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85793-2.00013-8 · Cited by 2 · see citing works

Protein Post-Translational Modification Prediction

Pang, C. N. I., & Wilkins, M. R. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.20265-3 · Cited by 2 · see citing works

Theoretical Investigation of the Material Usage During On-Bead Enrichment of Post-Translationally Modified Peptides in Suspension Systems

Liu, K., Huang, Y., Huang, T., Yang, P., Kong, J., Shen, H., & Zhang, Q. (2025) · Molecules · doi:10.3390/molecules30153245 · Cited by 1 · see citing works

Semi-rational engineering of a β-farnesene synthase hybrid for enhanced production in Serratia marcescens

Zhao, W., Gou, L., Liu, D., Wu, S., Zhou, X., Fan, T. P. D., Wang, L., & Cai, Y. (2026) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-026-00449-5 · Cited by 1 · see citing works

Selection of Cloning and Expression Plasmid Vectors

Kulkarni, R., Bose, R., & Bose, K. (2022) · Springer eBooks · doi:10.1007/978-981-16-4987-5_3 · Cited by 1 · see citing works

The Application of DNA Viruses to Biotechnology

Schieferecke, A. J., Ralph, N. K., & Schaffer, D. V. (2025) · Viruses · doi:10.3390/v17030414 · Cited by 2 · see citing works

Crystallography of Metabolic Enzymes

Alahuhta, M., Himmel, M. E., Bomble, Y. J., & Lunin, V. V. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0195-2_10 · Cited by 1 · see citing works

A screen for proteins involved in parasitism from Meloidogyne hapla identifies an amphid localized transthyretin-like protein as a potential effector

Polzin, F. (2015) · doi:10.53846/goediss-5324

Biochemical characterization of mammalian NEIL3 and involvement in repair of hydantoin lesions in proliferative tissue.

Krokeide, S. Z. (2013) · NORA - Norwegian Open Research Archives

Equine adenovirus: molecular and host cell receptor characterisation

Mekonnen, A. B. (2017) · Minerva Access (University of Melbourne)

Other Emerging Development Trends

Lu, Y. (2019) · SpringerBriefs in applied sciences and technology · doi:10.1007/978-981-13-1171-0_6

Towards the cell-free expression of glycoproteins

Exley, K. (2017) · Spiral (Imperial College London) · doi:10.25560/68742

Investigating the ameliorative potential of Aspalathus linearis and Cyclopia intermedia against lipid accumulation, lipolysis, oxidative stress and inflammation

Mamushi, M. (2020) · SUNScholar (Stellenbosch University)

Investigating ER Body Localization and the Splice Variant Function of HOTHEAD in Arabidopsis thaliana

Francom, T. (2020) · UWSpace (University of Waterloo)

The immunomodulatory protein, GIF, encoded by orf virus

Keats, T. W. D. (2020) · Otago University Research Archive (University of Otago)

Improvement of in vitro food allergy diagnostics by identifying unique antibody traits

Ehlers, A. M. (2021) · doi:10.33540/190

The ATCUN Motif as a Paramagnetic Beacon in Fragment-based Drug Discovery

Reet, J. V. (2020) · TSpace (University of Toronto)

In silico characterization of interferon-stimulated gene (ISG15) as a biomarker for early pregnancy diagnosis in Bubalus bubalis

Batra, K., & Nanda, T. (2019) · The Indian Journal of Animal Sciences · doi:10.56093/ijans.v89i3.88036

The Design of a MicroRNA Sensor Using an Improved Cell-Free Protein Synthesis System for Low-Limit Biomarker Detection

Copeland, C. E. (2023) · doi:10.31390/gradschool_dissertations.6127

Sequence-based prediction of the effects of histones H1 post-translational modifications: impact on the features related to the function

Kowalski, A. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2316773

Additional file 1 of Genome-wide high-throughput signal peptide screening via plasmid pUC256E improves protease secretion in Lactiplantibacillus plantarum and Pediococcus acidilactici

Chen, B., Loo, B. Z. L., Cheng, Y. Y., Song, P., Fan, H., Latypov, O., & Kittelmann, S. (2022) · Figshare · doi:10.6084/m9.figshare.18318158

Additional file 3 of Genome-wide high-throughput signal peptide screening via plasmid pUC256E improves protease secretion in Lactiplantibacillus plantarum and Pediococcus acidilactici

Chen, B., Loo, B. Z. L., Cheng, Y. Y., Song, P., Fan, H., Latypov, O., & Kittelmann, S. (2022) · Figshare · doi:10.6084/m9.figshare.18318164

Robust TCR production for the structural study of TCR-pMHC complexesPreprint

Oyon-Olea, L., Dichiara-Rodriguez, M. G., Hervás‐Stubbs, S., Erausquin, E., & López‐Sagaseta, J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.12.653033

Proteostasis and pathogenesis: Unraveling the complexity of protein misfolding disorders

Nair, T., Sarkar, D., Murmu, S., Rawat, R. S., & Singha, B. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.08.013

Additional file 4 of Genome-wide high-throughput signal peptide screening via plasmid pUC256E improves protease secretion in Lactiplantibacillus plantarum and Pediococcus acidilactici

Chen, B., Loo, B. Z. L., Cheng, Y. Y., Song, P., Fan, H., Latypov, O., & Kittelmann, S. (2022) · Figshare · doi:10.6084/m9.figshare.18318167

Additional file 2 of Genome-wide high-throughput signal peptide screening via plasmid pUC256E improves protease secretion in Lactiplantibacillus plantarum and Pediococcus acidilactici

Chen, B., Loo, B. Z. L., Cheng, Y. Y., Song, P., Fan, H., Latypov, O., & Kittelmann, S. (2022) · Figshare · doi:10.6084/m9.figshare.18318161

Hyper-expression of functional human basic fibroblast growth factor 2 in Escherichia coli

Manavalan, T., Bi, J., Khongsay, N., Van, N. T. B., Chua, X. Y., Yow, R., Lee, S. Y., Chew, L. J. M., Ottenheim, C., Sugii, S., et al. (2026) · Protein Expression and Purification · doi:10.1016/j.pep.2026.106894 · Cited by 1 · see citing works

Screening of quorum Sensing-Dependent strong promoters in Pseudomonas bijieensis 2P24 for metabolic optimization and Recombinant protein production

Li, J., Ma, H., Tai, N., Fan, Y. Y. K., Nie, M., Tao, X., Wang, Z., Wang, J., Deng, X., Shen, C., et al. (2026) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-026-04832-1

Synthetic Metabolic Circuits for Bioproduction, Biosensing and Biocomputation

Pandi, A. (2019) · doi:10.70675/f0fa6348zd212z40f8z95e3zdb9ce2fafc98

Mapping the structural coverage of Arabidopsis thaliana plant developmental proteins: Insights from Experimental and AlphaFold ApproachesPreprint

Rode, S., Sudarsanam, K., Bhalla, H., Srivastava, A., & Sankaranarayanan, S. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.31.729038

Heterologous Expression and Immunoreactivity of Wheat Amylase–Trypsin Inhibitors

Call, L., Svoboda, T., Krisai, A., Hacker, T., Lauter, K., D'Amico, S., Linhart, B., Amouric, A., Lafond, M., Giardina, T., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27198857

Challenging Post-translational Modifications in the Cell-free Protein Synthesis System

Porche, K. B., Lanclos, C., & Kwon, Y. (2023) · Synthetic biology and engineering · doi:10.35534/sbe.2023.10011 · Cited by 1 · see citing works

Modification of essential factors mediating post-translational processing for high-quality protein expression in Penicillium

Guo, D., Zhao, S., Chen, J., Han, S., Li, Y., Chen, Y., Hu, S., & Hu, Y. (2025) · Engineering Microbiology · doi:10.1016/j.engmic.2025.100194 · Cited by 2 · see citing works

Other Emerging Development Trends

Lu, Y. (2019) · SpringerBriefs in applied sciences and technology · doi:10.1007/978-981-13-1171-0_6

Research progress in protein posttranslational modification site prediction

He, W., Wei, L., & Zou, Q. (2018) · Briefings in Functional Genomics · doi:10.1093/bfgp/ely039 · Cited by 59 · see citing works

Post-translational modifications of protein biopharmaceuticals

Walsh, G. (2010) · Drug Discovery Today · doi:10.1016/j.drudis.2010.06.009 · Cited by 263 · see citing works