Coupling between codon usage, translation and protein export in Escherichia coli

Signal sequences

von HEIJNE, G. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90046-4 · Cited by 2,176 · see citing works

X-ray structure of a protein-conducting channel

van den Berg, B., Clemons, W., Collinson, I. R., Modis, Y., Hartmann, E., Harrison, S. C., & Rapoport, T. A. (2003) · Nature · doi:10.1038/nature02218 · Cited by 1,252 · see citing works

The signal peptide

von HEIJNE, G. (1990) · The Journal of Membrane Biology · doi:10.1007/bf01868635 · Cited by 1,140 · see citing works

Regulation of translation via mRNA structure in prokaryotes and eukaryotes

Kozak, M. (2005) · Gene · doi:10.1016/j.gene.2005.06.037 · Cited by 747 · see citing works

The Signal Recognition Particle

Keenan, R. J., Freymann, D. M., Stroud, R. M., & Walter, P. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.755 · Cited by 639 · see citing works

Protein Translocation Across the Bacterial Cytoplasmic Membrane

Driessen, A. J. M., & Nouwen, N. P. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.160747 · Cited by 610 · see citing works

Codon usage in regulatory genes in Escherichia coli does not reflect selection for ‘rare’ codons

Sharp, P. M., & Li, W. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.19.7737 · Cited by 587 · see citing works

Codon usage determines translation rate in Escherichia coli

Sørensen, M. A., Kurland, C. G., & Pedersen, S. B. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90260-x · Cited by 579 · see citing works

The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane

Hartl, F.-U., Lecker, S., Schiebel, E., Hendrick, J. P., & Wickner, W. (1990) · Cell · doi:10.1016/0092-8674(90)90160-g · Cited by 562 · see citing works

YidC mediates membrane protein insertion in bacteria.

Samuelson, J. C., Chen, M., Jiang, F., Möller, I., Wiedmann, M., Kuhn, A., Phillips, G. J., & Dalbey, R. E. (2000) · Nature · doi:10.1038/35020586 · Cited by 538 · see citing works

Correlation of competence for export with lack of tertiary structure of the mature species: A study in vivo of maltose-binding protein in E. coli

Randall, L. L., & HARDY, S. J. S. (1986) · Cell · doi:10.1016/0092-8674(86)90074-7 · Cited by 464 · see citing works

Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation

Komar, A. A., Lesnik, T., & Reiss, C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01566-5 · Cited by 386 · see citing works

L23 protein functions as a chaperone docking site on the ribosome

Krämer, G., Rauch, T., Rist, W., Vorderwülbecke, S., Patzelt, H., Schulze‐Specking, A., Ban, N., Deuerling, E., & Bukau, B. (2002) · Nature · doi:10.1038/nature01047 · Cited by 359 · see citing works

The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein

Collier, D. N., Bankaitis, V. A., Weiss, J. B., & Bassford, P. J. (1988) · Cell · doi:10.1016/0092-8674(88)90389-3 · Cited by 325 · see citing works

The Rieske protein from Paracoccus denitrificans is inserted into the cytoplasmic membrane by the twin‐arginine translocase

Bachmann, J., Bauer, B., Zwicker, K., Ludwig, B., & Anderka, O. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05480.x · Cited by 306 · see citing works

Codon usage can affect efficiency of translation of genes inEscherichia coli

Robinson, M. K., Lilley, R. J., Little, S., Emtage, J. S., Yarranton, G. T., Stephens, P., Millican, A. T., Eaton, M. A. W., & Humphreys, G. O. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.17.6663 · Cited by 297 · see citing works

Mechanisms of protein localization

Silhavy, T. J., Benson, S. A., & Emr, S. D. (1983) · Microbiological Reviews · doi:10.1128/mr.47.3.313-344.1983 · Cited by 281 · see citing works

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

Valent, Q. A., Kendall, D. A., High, S., Kusters, R., Oudega, B., & Luirink, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00236.x · Cited by 280 · see citing works

Escherichia coli ribosomes translate in vivo with variable rate.

Pedersen, S. B. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02227.x · Cited by 270 · see citing works

Absolute in vivo translation rates of individual codons in Escherichia coli

Sørensen, M. A., & Pedersen, S. B. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90211-n · Cited by 270 · see citing works

The E. coli ffh gene is necessary for viability and efficient protein export

Phillips, G. J., & Silhavy, T. J. (1992) · Nature · doi:10.1038/359744a0 · Cited by 269 · see citing works

Protein Targeting to the Bacterial Cytoplasmic Membrane

Fekkes, P., & Driessen, A. J. M. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.161-173.1999 · Cited by 266 · see citing works

Modulation of Folding Pathways of Exported Proteins by the Leader Sequence

Park, S., Liu, G., Topping, T., Cover, W. H., & Randall, L. L. (1988) · Science · doi:10.1126/science.3278378 · Cited by 249 · see citing works

Rates of aminoacyl-tRNA selection at 29 sense codons in vivo

Curran, J. F., & Yarus, M. (1989) · Journal of Molecular Biology · doi:10.1016/0022-2836(89)90170-8 · Cited by 239 · see citing works

Targeting proteins to membranes: structure of the signal recognition particle

Egea, P. F., Stroud, R. M., & Walter, P. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.03.007 · Cited by 236 · see citing works

Role of positive charge on the amino-terminal region of the signal peptide in protein secretion across the membrane.

Inouye, S., Soberón, X., Franceschini, T., Nakamura, K., Itakura, K., & Inouye, M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3438 · Cited by 234 · see citing works

Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation.

Randall, L. L. (1983) · Cell · doi:10.1016/0092-8674(83)90352-5 · Cited by 234 · see citing works

A Kinetic Partitioning Model of Selective Binding of Nonnative Proteins by the Bacterial Chaperone SecB

HARDY, S. J. S., & Randall, L. L. (1991) · Science · doi:10.1126/science.1989077 · Cited by 231 · see citing works

Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor

Miller, J. D., Bernstein, H. D., & Walter, P. (1994) · Nature · doi:10.1038/367657a0 · Cited by 222 · see citing works

Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli.

Vlasuk, G. P., Inouye, S., Ito, H., Itakura, K., & Inouye, M. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32343-3 · Cited by 212 · see citing works

Influence of the codon following the AUG initiation codon on the expression of a modified lacZ gene in Escherichia coli.

Looman, A. C., Bodlaender, J. M., COMSTOCK, L. J., Eaton, D., Jhurani, P., de Boer, H. A., & van Knippenberg, P. H. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02530.x · Cited by 208 · see citing works

The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal

Lee, H. C., & Bernstein, H. D. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051484198 · Cited by 204 · see citing works

The structural basis of protein targeting and translocation in bacteria.

Driessen, A. J. M., Manting, E. H., & van der Does, C. (2001) · Nature Structural Biology · doi:10.1038/88549 · Cited by 198 · see citing works

Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.

Cabelli, R. J., Dolan, K. M., Qian, L. P., & Oliver, D. B. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54245-9 · Cited by 193 · see citing works

SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli.

Matsuyama, S., Fujita, Y., & Mizushima, S.-I. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05652.x · Cited by 193 · see citing works

Discrimination between SRP- and SecA/SecB-dependent substrates involves selective recognition of nascent chains by SRP and trigger factor.

Beck, K., Wu, L., Brunner, J., & Müller, M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.134 · Cited by 189 · see citing works

Silent mutations affect in vivo protein folding in Escherichia coli

Cortazzo, P., Červeñanský, C., Marı́n, M., Reiss, C. J., Ehrlich, R., & Deana, A. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00226-7 · Cited by 179 · see citing works

Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor

Valent, Q. A., de Gier, J. L., von HEIJNE, G., Kendall, D. A., ten Hagen‐Jongman, C. M., Oudega, B., & Luirink, J. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4431808.x · Cited by 171 · see citing works

The signal recognition particle and its interactions during protein targeting

Halić, M., & Beckmann, R. (2005) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2005.01.013 · Cited by 167 · see citing works

Synonymous codon usage influences the local protein structure observed

Saunders, R., & Deane, C. M. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq495 · Cited by 165 · see citing works

Codon bias at the 3′-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli

Stenström, C. M., Jin, H., Major, L. L., Tate, W. P., & Isaksson, L. A. (2001) · Gene · doi:10.1016/s0378-1119(00)00550-3 · Cited by 165 · see citing works

In Vitro Studies with Purified Components Reveal Signal Recognition Particle (SRP) and SecA/SecB as Constituents of Two Independent Protein-targeting Pathways of<i>Escherichia coli</i>

Koch, H.-G., Hengelage, T., Neumann-Haefelin, C., MacFarlane, J., Hoffschulte, H. K., Schimz, K.-L., Mechler, B., & Müller, M. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.7.2163 · Cited by 160 · see citing works

Direct Observation of Chaperone-Induced Changes in a Protein Folding Pathway

Bechtluft, P., van Leeuwen, R. G. H., Tyreman, M., Tomkiewicz, D., Nouwen, N. P., Tepper, H. L., Driessen, A. J. M., & Tans, S. J. (2007) · Science · doi:10.1126/science.1144972 · Cited by 155 · see citing works

Substrate specificity of the SecB chaperone.

Knoblauch, N. T. M., Rüdiger, S., Schönfeld, H.-J., Driessen, A. J. M., Schneider-Mergener, J., & Bukau, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.48.34219 · Cited by 154 · see citing works

Signal recognition particle-depencent protein targeting, universal to all kingdoms of life

Koch, H.-G., Moser, M., & Müller, M. (2003) · Reviews of Physiology, Biochemistry and Pharmacology · doi:10.1007/s10254-002-0002-9 · Cited by 154 · see citing works

Protein targeting by the signal recognition particle

Grudnik, P., Bange, G., & Sinning, I. (2009) · Biological Chemistry · doi:10.1515/bc.2009.102 · Cited by 152 · see citing works

Assembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle

de Gier, J. L., Mansournia, P., Valent, Q. A., Phillips, G. J., Luirink, J., & von HEIJNE, G. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01354-3 · Cited by 152 · see citing works

Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on theEscherichia coliribosome

Ullers, R. S., Houben, E. N. G., Raine, A., ten Hagen‐Jongman, C. M., Ehrenberg, M., Brunner, J., Oudega, B., Harms, N., & Luirink, J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302130 · Cited by 142 · see citing works

Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization.

Tani, K., Tokuda, H., & Mizushima, S.-I. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44908-8 · Cited by 141 · see citing works

A kinetic model of protein synthesis. Application to hemoglobin synthesis and translational control.

Bergmann, J. E., & Lodish, H. F. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86406-2 · Cited by 140 · see citing works

Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo

Kumamoto, C. A., & Francetić, O. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.8.2184-2188.1993 · Cited by 107 · see citing works

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane

Matsumoto, G., Yoshihisa, T., & Ito, K. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6384 · Cited by 95 · see citing works

Signal peptide mutants ofEscherichia coli

Gennity, J. M., Goldstein, J., & Inouye, M. (1990) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00763167 · Cited by 92 · see citing works

Thermodynamic Characterization of the Reversible, Two-State Unfolding of Maltose Binding Protein, a Large Two-Domain Protein

Ganesh, C., Shah, A. N., Swaminathan, C. P., Surolia, A., & Varadarajan, R. (1997) · Biochemistry · doi:10.1021/bi961967b · Cited by 91 · see citing works

Trigger factor binds to ribosome–signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor

Buskiewicz, I. A., Deuerling, E., Gu, S.-Q., Jöckel, J., Rodnina, M. V., Bukau, B., & Wintermeyer, W. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402231101 · Cited by 86 · see citing works

SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane

Oliver, D. B. (1993) · Molecular Microbiology · doi:10.1111/j.1365-2958.1993.tb01107.x · Cited by 86 · see citing works

Codon choice and gene expression: synonymous codons differ in their ability to direct aminoacylated-transfer RNA binding to ribosomes in vitro.

Thomas, L. K., Dix, D. B., & Thompson, R. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4242 · Cited by 81 · see citing works

Translation rate modification by preferential codon usage: Intragenic position effects

Liljenström, H., & von HEIJNE, G. (1987) · Journal of Theoretical Biology · doi:10.1016/s0022-5193(87)80251-5 · Cited by 80 · see citing works

Analysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide

Puziss, J. W., Fikes, J. D., & Bassford, P. J. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.5.2303-2311.1989 · Cited by 79 · see citing works

SecB—A chaperone dedicated to protein translocation

Bechtluft, P., Nouwen, N. P., Tans, S. J., & Driessen, A. J. M. (2009) · Molecular BioSystems · doi:10.1039/b915435c · Cited by 77 · see citing works

SecB, a molecular chaperone with two faces

Driessen, A. J. M. (2001) · Trends in Microbiology · doi:10.1016/s0966-842x(01)01980-1 · Cited by 72 · see citing works

High-Level Periplasmic Expression in Escherichia coli Using a Eukaryotic Signal Peptide: Importance of Codon Usage at the 5′ End of the Coding Sequence

Humphreys, D. P., Sehdev, M., Chapman, A. P., Ganesh, R., Smith, B. J., King, L. M., Glover, D. J., Reeks, D. G., & Stephens, P. E. (2000) · Protein Expression and Purification · doi:10.1006/prep.2000.1286 · Cited by 69 · see citing works

Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coli

Bowers, C. W., Lau, F. K., & Silhavy, T. J. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.19.5697-5705.2003 · Cited by 68 · see citing works

Effect of Signal Peptide on the Stability and Folding Kinetics of Maltose Binding Protein

Beena, K., Udgaonkar, J. B., & Varadarajan, R. (2004) · Biochemistry · doi:10.1021/bi0360509 · Cited by 66 · see citing works

Positively charged lysine at the N‐terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids

Nesmeyanova, M. A., Karamyshev, A. L., Karamysheva, Z. N., Kalinin, A. E., Ksenzenko, V. N., & Kajava, A. V. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00052-5 · Cited by 66 · see citing works

The E. coli SRP: preferences of a targeting factor

de Gier, J. L., Valent, Q. A., von HEIJNE, G., & Luirink, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00402-x · Cited by 63 · see citing works

Kinetic Analysis of the Translocation of Fluorescent Precursor Proteins into Escherichia coli Membrane Vesicles

de Keyzer, J., van der Does, C., & Driessen, A. J. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208449200 · Cited by 62 · see citing works

Interaction of Bacillus subtilis CsaA with SecA and precursor proteins

Müller, J. P., Ozegowski, J., Vettermann, S., Swaving, J., van Wely, K. H. M., & Driessen, A. J. M. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3480367 · Cited by 60 · see citing works

Enhancement of Translation Initiation by A/T-Rich Sequences Downstream of the Initiation Codon in Escherichia coli

Qing, G., Xia, B., & Inouye, M. (2003) · Microbial Physiology · doi:10.1159/000077244 · Cited by 59 · see citing works

Experimental confirmation of a key role for non-optimal codons in protein export

Zalucki, Y. M., & Jennings, M. P. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.126 · Cited by 59 · see citing works

Biased codon usage in signal peptides: A role in protein export

Zalucki, Y. M., Beacham, I. R., & Jennings, M. P. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.01.005 · Cited by 57 · see citing works

Selection for efficient translation initiation biases codon usage at second amino acid position in secretory proteins

Zalucki, Y. M., Power, P. M., & Jennings, M. P. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm577 · Cited by 54 · see citing works

Leader peptidase

Dalbey, R. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb01844.x · Cited by 54 · see citing works

Whole genome analysis reveals a high incidence of non-optimal codons in secretory signal sequences of Escherichia coli

Power, P. M., Jones, R. A., Beacham, I. R., Bucholtz, C. A., & Jennings, M. P. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.022 · Cited by 49 · see citing works

Bacterial secretome: the assembly manual and operating instructions (Review)

Economou, A. (2002) · Molecular Membrane Biology · doi:10.1080/09687680210152609 · Cited by 48 · see citing works

The rapid evolution of signal peptides is mainly caused by relaxed selection on non-synonymous and synonymous sites

Li, Y., Xie, Z., Du, Y., Zhou, Z. M., Mao, X., Lv, L., & Li, Y. (2009) · Gene · doi:10.1016/j.gene.2009.01.015 · Cited by 44 · see citing works

Rare codons in E. coli and S. typhimurium signal sequences

Burns, D. M., & Beacham, I. R. (1985) · FEBS Letters · doi:10.1016/0014-5793(85)81048-6 · Cited by 39 · see citing works

Targeting and insertion of heterologous membrane proteins in E. coli

Raine, A., Ullers, R. S., Pavlov, M. Y., Luirink, J., Wikberg, J. E. S., & Ehrenberg, M. (2003) · Biochimie · doi:10.1016/s0300-9084(03)00130-5 · Cited by 38 · see citing works

The conformation of a nascent polypeptide inside the ribosome tunnel affects protein targeting and protein folding

Peterson, J. H., Woolhead, C. A., & Bernstein, H. D. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07325.x · Cited by 34 · see citing works

Reversible formation of on‐pathway macroscopic aggregates during the folding of maltose binding protein

Ganesh, C., Zaidi, F. N., Udgaonkar, J. B., & Varadarajan, R. (2001) · Protein Science · doi:10.1110/ps.8101 · Cited by 32 · see citing works

Secretory signal sequence non-optimal codons are required for expression and export of β-lactamase

Zalucki, Y. M., Gittins, K. L., & Jennings, M. P. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.11.093 · Cited by 31 · see citing works

The crystal structure of the ttCsaA protein: an export‐related chaperone from Thermus thermophilus

Kawaguchi, S., Müller, J., Linde, D., Kuramitsu, S., Shibata, T., Inoue, Y., Vassylyev, D. G., & Yokoyama, S. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.562 · Cited by 30 · see citing works

A chemically cross‐linked nonlinear proOmpA molecule can be translocated into everted membrane vesicles of Escherichia coli in the presence of the proton motive force

Tani, K., & Mizushima, S. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80741-k · Cited by 27 · see citing works

Signal sequence non-optimal codons are required for the correct folding of mature maltose binding protein

Zalucki, Y. M., Jones, C. E., Ng, P. S. K., Schulz, B. L., & Jennings, M. P. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.03.010 · Cited by 21 · see citing works

Whole genome analysis of non-optimal codon usage in secretory signal sequences of Streptomyces coelicolor

Li, Y., Li, Y., Chen, J., Dong, H., Guan, W., & Zhou, H. (2006) · Biosystems · doi:10.1016/j.biosystems.2006.02.006 · Cited by 15 · see citing works

Comparative Study on the Effect of Signal Peptide Codons and Arginine Codons on the Expression of Human Interferon-α1 Gene in Escherichia coli

Saraffova, A., Maximova, V. A., Ivanov, I. G., & Haidar, M. A. (1996) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.1996.16.745 · Cited by 1 · see citing works

The ribosome in action: Tuning of translational efficiency and protein folding

Rodnina, M. V. (2016) · Protein Science · doi:10.1002/pro.2950 · Cited by 211 · see citing works

Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways.

Kudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.03.016 · Cited by 177 · see citing works

The Yin and Yang of codon usage

Komar, A. A. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw207 · Cited by 175 · see citing works

Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments

Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works

Optimisation of signal peptide for recombinant protein secretion in bacterial hosts

Low, K. O., Muhammad Mahadi, N., & Md. Illias, R. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-4831-z · Cited by 130 · see citing works

Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum

Hemmerich, J., Rohe, P., Kleine, B., Jurischka, S., Wiechert, W., Freudl, R., & Oldiges, M. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0604-6 · Cited by 73 · see citing works

Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region

Mirzadeh, K., Shilling, P. J., Elfageih, R., Cumming, A. J., Cui, H., Rennig, M., Nørholm, M. H. H., & Daley, D. O. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-01339-8 · Cited by 45 · see citing works

Large-scale analysis of conserved rare codon clusters suggests an involvement in co-translational molecular recognition events

Chartier, M., Gaudreault, F., & Najmanovich, R. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts149 · Cited by 51 · see citing works

Enhancement of antibody fragment secretion into the Escherichia coli periplasm by co-expression with the peptidyl prolyl isomerase, FkpA, in the cytoplasm

Levy, R., Ahluwalia, K., Bohmann, D. J., Giang, H. M., Schwimmer, L. J., Issafras, H., Reddy, N. B., Chan, C., Horwitz, A. H., & Takeuchi, T. (2013) · Journal of Immunological Methods · doi:10.1016/j.jim.2013.04.010 · Cited by 34 · see citing works

Whisper mutations: cryptic messages within the genetic code

Fåhræus, R., Marı́n, M., & Olivares‐Illana, V. (2015) · Oncogene · doi:10.1038/onc.2015.454 · Cited by 28 · see citing works

Quantifying codon usage in signal peptides: Gene expression and amino acid usage explain apparent selection for inefficient codons

Cope, A. L., Hettich, R. L., & Gilchrist, M. A. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.09.010 · Cited by 24 · see citing works

High‐yield production of recombinant CRM197, a non‐toxic mutant of diphtheria toxin, in the periplasm of Escherichia coli

Goffin, P., Dewerchin, M., Rop, P. D., Blais, N., & Dehottay, P. (2017) · Biotechnology Journal · doi:10.1002/biot.201700168 · Cited by 24 · see citing works

Silent Polymorphisms: Can the tRNA Population Explain Changes in Protein Properties?

Fernández-Calero, T., Cabrera-Cabrera, F., Ehrlich, R., & Marı́n, M. (2016) · Life · doi:10.3390/life6010009 · Cited by 23 · see citing works

High‐level extracellular secretion of organophosphorous hydrolase of Flavobacterium sp. in Escherichia coli BL21(DE3)pLysS

Falahati‐pour, S. K., Lotfi, A. S., Ahmadian, G., Baghizadeh, A., Behroozi, R., & Haghighi, F. (2015) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1438 · Cited by 17 · see citing works

The role of signal sequence proximal residues in the mature region of bacterial secreted proteins in E. coli

Musik, J. E., Zalucki, Y. M., Beacham, I. R., & Jennings, M. P. (2022) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2022.184000 · Cited by 16 · see citing works

Site-saturation mutagenesis of mutant l -asparaginase II signal peptide hydrophobic region for improved excretion of cyclodextrin glucanotransferase

Ismail, A., & Illias, R. M. (2017) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-017-1980-6 · Cited by 10 · see citing works

Escherichia coli: The Leading Model for the Production of Recombinant Proteins

Tucci, P., Veroli, V., Señorale, M., & Marı́n, M. (2016) · Springer eBooks · doi:10.1007/978-981-10-2555-6_6 · Cited by 6 · see citing works

Expression in Bacteria and Refolding

Akiba, H., & Tsumoto, K. (2016) · Springer protocols handbooks/Springer protocols · doi:10.1007/978-4-431-56030-2_1 · Cited by 5 · see citing works

Editorial: In vivo protein folding – at the crossroad between basic research and biotechnology

Marı́n, M., & Blondel, M. (2011) · Biotechnology Journal · doi:10.1002/biot.201100020

T-G-A Deficiency Pattern in Protein-Coding Genes and Its Potential Reason

Jin, Y.-T., Pu, D., Guo, H., Deng, Z., Chen, L., & Guo, F. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.847325

Additional file 1 of Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region

Mirzadeh, K., Shilling, P. J., Elfageih, R., Cumming, A. J., Cui, H. L., Rennig, M., Nørholm, M. H. H., & Daley, D. O. (2020) · Figshare · doi:10.6084/m9.figshare.12097467

Whole genome analysis reveals a high incidence of non-optimal codons in secretory signal sequences of Escherichia coli

Power, P. M., Jones, R. A., Beacham, I. R., Bucholtz, C. A., & Jennings, M. P. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.022 · Cited by 49 · see citing works

Experimental confirmation of a key role for non-optimal codons in protein export

Zalucki, Y. M., & Jennings, M. P. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.126 · Cited by 59 · see citing works

Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding

Mallik, I., Smith, M. A., & Flower, A. M. (2002) · BMC Microbiology · doi:10.1186/1471-2180-2-32 · Cited by 9 · see citing works

Biased codon usage in signal peptides: A role in protein export

Zalucki, Y. M., Beacham, I. R., & Jennings, M. P. (2009) · Trends in Microbiology · doi:10.1016/j.tim.2009.01.005 · Cited by 57 · see citing works

Identification of a Post-targeting Step Required for Efficient Cotranslational Translocation of Proteins across the Escherichia coli Inner Membrane

Tian, P., & Bernstein, H. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900375200 · Cited by 16 · see citing works