Listed below are a number of articles that provide a broad overview about using different expression systems for the production of recombinant proteins. 

Bacterial expression system

Papaneophytou, C.P. et al. Statistical approaches to maximize recombinant protein expression in Escherichia coli: A general review. Protein Expression and Purification 94, 22–32 (2014)

Kudla, G. Coding-Sequence Determinants of Gene Expression in Escherichia coli. Science 324, 255-258 (2014)

Muntari, B., et al. Recombinant bromelain production in Escherichia coli: process optimization in shake flask culture by response surface methodology. AMB Express 2:12 (2012)

Rouet, R., et al. Expression of high-affinity human antibody fragments in bacteria. Nature Protocols 364VOL.7 NO.2 (2012)

Vincentelli, R. et al. High-throughput protein expression screening and purification in Escherichia coli, Methods 55, 65-72 (2011)

Unger, T., et al. Applications of the Restriction Free (RF) cloning procedure for molecular manipulations and protein expression. Journal of Structural Biology 172, 34-44 (2010). 

Schein, C.H. Soluble Protein Expression in Bacteria. Encyclopedia of Industrial Biotechnology: Bioprocess, Bioseparation, and Cell Technology 1-20 (2010).

Francis, D.M. et al. Strategies to Optimize Protein Expression in E. coli. Current protocols in protein science Chapter 5, Unit 5 24 (2010). 

Brondyk, W.H. Selecting an Appropriate Method for Expressing a Recombinant Protein. Guide to Protein Purification, Second Edition 463, 131-147 (2009). 

Rosano G.L. et al. Rare codon content affects the solubility of recombinant proteins in a codon bias-adjusted Escherichia coli strain. Microbial Cell Factories 8:41 (2009) 

Selleck, W. et al. Recombinant protein complex expression in E. coli. Current protocols in protein science Chapter 5, Unit 5 21 (2008). 

Komar A.A A pause for thought along the co-translational folding pathway. Trends in Biochemical Sciences Vol.34 No.1 (2008) 

Berrow, N.S. et al. A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Research 35, e45 (2007).

Cabrita, L.D., et al. A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnology 6, 12 (2006). 

Duetz, W.A., et al. Methods for Intense Aeration, Growth, Storage, and Replication of Bacterial Strains in Microtiter Plates. Applied and Environmental Microbiology, Vol 66, No. 6, 2641–2646 (2006)

Waugh, D. Making the most of affinity tags. TRENDS in Biotechnology Vol.23 No.6 (2005) 

Goulding C.W. et al. Protein production in Escherichia coli for structural studies by X-ray crystallography. Journal of Structural Biology 142 133–143 (2003

Yeast expression system

Spadiut, O. et al. Microbials for the production of monoclonal antibodies and antibody fragments. Trends in Biotechnology 1:54-60 (2014)

Vogl, T. et al. New opportunities by synthetic biology for biopharmaceutical production in Pichia pastoris. Current Opinion in Biotechnology 6:1094-101 (2013) 

Jiang Y. et al. Purification process development of a recombinant monoclonal antibody expressed in glycoengineered Pichia pastoris. Protein Expression and Purification 76 7–14 (2011) 

Abad, S. et al. Stepwise engineering of a Pichia pastoris D-amino acid oxidase whole cell catalyst. Microbial Cell Factories, 9:24 (2010)

Bollok, M., Resina, D., Valero, F. & Ferrer, P. Recent patents on the Pichia pastoris expression system: expanding the toolbox for recombinant protein production. Recent Patents on Biotechnology 3, 192-201 (2009). 

Cregg, J.M. et al. Expression in the yeast Pichia pastoris. Methods in Enzymology 463, 169-189 (2009). 

Gong B. et al. Characterization of N-Linked Glycosylation on Recombinant Glycoproteins Produced in Pichia pastoris Using ESI-MS and MALDI-TOF. Methods in Molecular Biology, Glycomics: Methods and Protocols, vol. 534 Chapter 16 (2009) 

Ghosalkar A. et al. Optimization of chemically defined medium for recombinant Pichia pastoris for biomass production. Bioresource Technology 99 7906–7910 (2008) 

Hamilton, S.R. & Gerngross, T.U. Glycosylation engineering in yeast: the advent of fully humanized yeast. Current Opinion in Biotechnology 18, 387-392 (2007). 

Lin-Cereghino, J., et al., Condensed protocol for competent cell preparation and transformation of the methylotrophic yeast Pichia pastoris. Biotechniques 38(1): 44–48. (2005)

Suga M. et al. Cryopreservation of competent intact yeast cells for efficient electroporation. Yeast 16: 889-896. (2000) 

Insect cell / BEVS expression system

Fernandes, F. et al. Insect cells as a production platform of complex virus-like particles Expert Rev. Vaccines12(2), 225–236 (2013)

Kost, T. Baculovirus Gene Delivery: A Flexible Assay Development Tool. Current Gene Therapy 10 168-173 (2010)

Airenne, K.J., et. al. In Vivo  Application and Tracking of Baculovirus. Current Gene Therapy, 2010

Madhan, S. et al. Baculovirus as Vaccine Vectors. Current Gene Therapy 10 201-213 (2010)

Trowitzsch, S., et al.  New baculovirus expression tools for recombinant protein complex production. Journal of Structural Biology 172, 45-54 (2010).

Aucoin, M.G., et al.  Bioprocessing of baculovirus vectors: a review. Current Gene Therapy 10, 174-186 (2010).

Jarvis, D.L. Baculovirus-insect cell expression systems. Methods in Enzymology 463, 191-222 (2009).

Chung Y.C., et al., Expression, purification and characterization of enterovirus-71 virus-like particles. World J Gastroenterol; 12(6): 921-927 (2006)

Kost, T.A., et alBaculovirus as versatile vectors for protein expression in insect and mammalian cells. Nature Biotechnology 23, 567-575 (2005).

Weber, W. Optimisation of protein expression and establishment of the Wave Bioreactor for Baculovirus/insect cell culture. Cytotechnology 38: 77–85, (2002)

Mammalian cell expression system

Almo S.C., et al. Better and faster: improvements and optimization for mammalian recombinant protein production. Current Opinion in  Structural Biology. 26:39-43 (2014)

Bandaranayake A.D. et al. Recent advances in mammalian protein production. FEBS Letters. 588 2 253-60 (2014)

Zhang, J. Mammalian Cell Culture for Biopharmaceutical Production. Fermentation and Cell Culture Chapter 12 157-178 (2012)

Baldi. L., et al. Large-scale transfection of mammalian cells. Methods in Molecular Biology Volume 801 13-26 (2012)

Rodrigues, M.E. Technological Progresses in Monoclonal Antibody Production Systems. Biotechnol. Prog. Vol. 26, No. 2 (2010)

Hacker D.L. 25 years of recombinant proteins from reactor-grown cells—Where do we go from here? Biotechnology Advances 27 1023–1027 (2009)

Nettleship, J. et al., The Production of Glycoproteins by Transient Expression in Mammalian Cells. Methods in Molecular Biology: High Throughput Protein Expression and Purification, vol. 498 Chapter 16 (2009)

Lackner, A. A bicistronic baculovirus vector for transient and stable protein expression in mammalian cells. Analytical Biochemistry 380 146–148 (2008) 

Matasci, M. et al. Recombinant therapeutic protein production in cultivated mammalian cells:current status and future prospects. Drug Discovery Today: Technologies 5, e37-e42 (2008).

Baldi, L., et al. Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives. Biotechnology Letters 29, 677-684 (2007).

Barnes, L.M., et al. Mammalian cell factories for efficient and stable protein expression. Current Opinion in Biotechnology 17 381–386 (2006)

Birch, J.R. et al. Antibody production. Advanced Drug Delivery Reviews 58 671 – 685 (2006)

Kunaparaju, R., et al., Epi-CHO, an Episomal  Expression System for Recombinant Protein Production in CHO Cells. Wiley Periodicals, (2005)

Wurm, F.M. Production of recombinant protein therapeutics in cultivated mammalian cells. Nature Biotechnology 22 No. 11 (2004)

In Vitro expression system

Johnston W & Alexandrov K (2014) Production of Eukaryotic Cell-Free Lysate from Leishmania tarentolae. Cell-Free Protein Synthesis, Methods in Molecular Biology, eds Alexandrov K & Johnston WA (Humana Press), Vol 1118, pp 1-15.

Kovtun O, Mureev S, Johnston W, & Alexandrov K (2010) Towards the construction of expressed proteomes using a Leishmania tarentolae based cell-free expression system. PLoS One 5(12):e14388.

Kovtun O, et al. (2011) Leishmania cell-free protein expression system. Methods 55(1):58-64.

Mureev S, Kovtun O, Nguyen UT, & Alexandrov K (2009) Species-independent translational leaders facilitate cell-free expression. Nat Biotechnol 27(8):747-752.