2015
Enabling Low Cost Biopharmaceuticals: A Systematic Approach to Delete Proteases from a Well-Known Protein Production Host Trichoderma reesei. Landowski CP, Huuskonen A, Wahl R, Westerholm-Parvinen A, Kanerva A, Hänninen AL, Salovuori N, Penttilä M, Natunen J, Ostermeier C, Helk B, Saarinen J, Saloheimo M.
PLoS One. 2015 Aug 26;10(8):e0134723. http://www.ncbi.nlm.nih.gov/pubmed/26309247
Swollenin from Trichoderma reesei exhibits hydrolytic activity against cellulosic substrates with features of both endoglucanases and cellobiohydrolases. Andberg, M., Penttilä, M. and Saloheimo, M., Bioresource Technol. 2015, 181:105-113. http://www.ncbi.nlm.nih.gov/pubmed/25643956
Protein body formation in leaves of Nicotiana benthamiana: a concentration-dependent mechanism influenced by the presence of fusion tags. Saberianfar, R., Joensuu, J.J., Conley, A. and Menassa, R. Plant Biotechnol. J. 2015, in press. http://www.ncbi.nlm.nih.gov/pubmed/25640969
2014
Cloning and characterisation of a novel acidic cutinase from Sirococcus conigenus. Nyyssölä, A., Pihlajaniemi, V., Häkkinen, M., Kontkanen, H., Saloheimo, M. and Nakari-Setälä, T. Appl. Microbiol. Biotechnol. 2014, 98: 3639-3650. http://www.ncbi.nlm.nih.gov/pubmed/24121867
Screening of candidate regulators for cellulase and hemicellulase production in Trichoderma reesei and identification of a factor essential for cellulase production. Häkkinen, M., Valkonen, M., Westerholm-Parvinen, A., Aro, N., Arvas, M., Vitikainen, M., Penttilä, M., Saloheimo M. and Pakula, T.. Biotechnology for Biofuels 2015, 7:14. http://www.ncbi.nlm.nih.gov/pubmed/24472375
Comparison of intracellular and secretion-based strategies for production of human α-galactosidase A in the filamentous fungus Trichoderma reesei. Smith, W., Jäntti, J., Oja, M. and Saloheimo, M. BMC Biotechnol. 2014, 14: 91. http://www.ncbi.nlm.nih.gov/pubmed/25344685
Intracellular pH responses in the industrially important fungus Trichoderma reesei. Valkonen, M., Penttilä, M. and Bencina, M.. Fung. Genet. Biol. 2014, 70: 83-90. http://www.ncbi.nlm.nih.gov/pubmed/25046860
Scale-up of hydrophobin-assisted recombinant protein production in tobacco BY-2 suspension cells. Reuter, L., Bailey, M., Joensuu, J., Ritala, A.. Plant Biotechnol. J. 2014, 12: 402-410. http://www.ncbi.nlm.nih.gov/pubmed/24341724
Influence of elastin-like polypeptide and hydrophobin on recombinant hemagglutinin accumulations in transgenic tobacco plants. Phan, H., Hause, B., Hause, G., Arcalis, E., Stoger, E., Maresch, D., Altmann, F., Joensuu, J., and Conrad, U. PLoS ONE 2014, 9:e99347. http://www.ncbi.nlm.nih.gov/pubmed/24914995
Plant-based solutions for veterinary immunotherapeutics and prophylactics. Kolotilin, I., Topp, E., Cox, E., Devriendt, B., Conrad, U., Joensuu, J., Stäger, E., Warzecha, H.,McAllister, T., Potter, A., McLean, M., Hall, C. and Menassa, R..Veterinary Research 2014, 45:117. http://www.ncbi.nlm.nih.gov/pubmed/25559098
Protein production – ER quality control and secretion stress responses in Trichoderma reesei. Saloheimo, M., Pakula, T., Aro, N. and Joensuu, J.. In: Gupta, V.J. et al. (Eds.) Biology and Biotechnology of Trichoderma. Elsevier 2014, Waltham, MA, USA.
2013
Directing enzymatic cross-linking activity to the air-water interface by a fusion protein approach. Paananen, A., Ercili-Cura, D., Saloheimo, M., Lantto, R. and Linder, M..
Soft matter 2013, 9: 1612.
Intracellular protein production in Trichoderma reesei (Hypocrea jecorina) with hydrophobin fusion technology. Mustalahti, E., Saloheimo, M. and Joensuu, J.. New Biotechnol. 2013, 30: 262-268. http://www.ncbi.nlm.nih.gov/pubmed/21971507
Sturucture-function relationships in hydrophobins: probing the role of charged side chains. Lienemann M, Gandier J.-A., Joensuu J.J., Iwanaga A., Takatsuji Y., Haruyama T., Master E., Tenkanen M. and Linder M.B.. Applied and Environmental Microbiology 2013, 79:5533-5538. http://www.ncbi.nlm.nih.gov/pubmed/23835172
Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics. Corchero, J., Gasser, B., Resina, D. Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., Saloheimo, M., Mattanovich, D., Schwartz, S., Tutino, L. and Villaverde, A.. Biotechnology Advances 2013, 31: 140-153. http://www.ncbi.nlm.nih.gov/pubmed/22985698
Experimental and bioinformatic investigation of the proteolytic degradation of the C-terminal domain of a fungal tyrosinase. Faccio, G., Arvas, M., Thöny-Meyer, L. and Saloheimo, M.. J. Inorg. Biochem. 2013, 121: 37–45. http://www.ncbi.nlm.nih.gov/pubmed/23333757
Swollenin aids in the amorphogenesis step during the enzymatic hydrolysis of biomass. Gourlay, K., Hu, J., Arantes, V., Andberg, M., Saloheimo, M., Penttilä, M. and Saddler, J.. Bioresource Technol. 2013, 142: 498-503. http://www.ncbi.nlm.nih.gov/pubmed/23759433
2012
The cargo and the transport system: secreted proteins and protein secretion in Trichoderma reesei (Hypocrea jecorina). Saloheimo, M. and Pakula, T.M.. Microbiology 2012, 158: 46 – 57. http://www.ncbi.nlm.nih.gov/pubmed/22053009
Bacterial tyrosinases and their applications. Faccio, G., Kruus, K., Saloheimo, M. and Thöny-Meyer, L.. Process Biochemistry 2012, 47: 1749 - 1760.
Re-annotation of the CAZy genes of Trichoderma reesei and transcription in the presence of lignocellulosic substrates. Häkkinen, M., Arvas, M., Oja, M., Aro, N., Penttilä, M., Saloheimo M. and Pakula, T.M.. Microbial Cell Factories 2012, 11:134. http://www.ncbi.nlm.nih.gov/pubmed/23035824
Xylanase XYN IV from Trichoderma reesei showing exo- and endo-xylanase activity. Biely, P., Tenkanen, M., Vršanská, M., Puchart, V., Wong, Penttilä, M., Saloheimo, M. and Siika-aho, M.. FEBS J. 2012, 280: 285-301. http://www.ncbi.nlm.nih.gov/pubmed/23167779
Bioseparation of recombinant proteins from plant extract with hydrophobin fusion technology. Joensuu, J.J., Conley, A., Linder, M. and Menassa, R.. In: Methods in Molecular Biology. Volume 824: Recombinant Gene Expression: Reviews and Protocols. 3rd ed. Springer 2012, 527-534.
Transient expression using agroinfiltration and its applications in molecular farming. Menassa, R., Ahmad, A. and Joensuu, J.J.. In: Molecular Farming in Plants: Recent Advances and Future Prospects. Wang, A. & Ma, S. (eds). Springer2012, 183-198.
2011
Correlation of gene expression and protein production rate - a system wide study. Arvas M., Pakula T., Smit B., Rautio J., Koivistoinen H., Jouhten P., Lindfors E., Wiebe M., Penttilä M., Saloheimo M.. BMC Genomics. 2011, 12:616. http://www.ncbi.nlm.nih.gov/pubmed/22185473
Sulfhydryl oxidases: sources, properties, production and applications. Faccio G., Nivala O., Kruus K, Buchert J., Saloheimo M.. Appl. Microbiol. Biotechnol. 2011, 91:957-966. http://www.ncbi.nlm.nih.gov/pubmed/21732243
The effects of disruption of phosphoglucose isomerase gene on carbon utilisation and cellulase production in Trichoderma reesei Rut-C30. Limón M.C., Pakula T., Saloheimo M., Penttilä M..
Microb. Cell Fact. 2011 10:40. http://www.ncbi.nlm.nih.gov/pubmed/21609467
Production and characterisation of AoSOX2 from Aspergillus oryzae, a novel flavin-dependent sulfhydryl oxidase with good pH and temperature stability. Faccio G., Kruus K., Buchert J., Saloheimo M.. Appl. Microbiol. Biotechnol. 2011, 90:941-949. http://www.ncbi.nlm.nih.gov/pubmed/21327412
Influence of growth temperature on the production of antibody Fab fragments in different microbes: a host comparative analysis. Dragosits M., Frascotti G., Bernard-Granger L., Vázquez F., Giuliani M., Baumann K., Rodríguez-Carmona E., Tokkanen J., Parrilli E., Wiebe M.G., Kunert R., Maurer M., Gasser B., Sauer M., Branduardi P., Pakula T., Saloheimo M., Penttilä M., Ferrer P., Luisa Tutino M., Villaverde A., Porro D., Mattanovich D.. Biotechnol. Prog. 2011, 27:38-46. http://www.ncbi.nlm.nih.gov/pubmed/21312353
Transformation system for Hypocrea jecorina (Trichoderma reesei) that favors homologous integration and employs reusable bidirectionally selectable markers. Steiger M.G., Vitikainen M., Uskonen P., Brunner K., Adam G., Pakula T., Penttilä M., Saloheimo M., Mach R.L., Mach-Aigner A.R.. Appl. Environ. Microbiol. 2011, 77:114-21. http://www.ncbi.nlm.nih.gov/pubmed/21075888
Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants. Conley A.J., Joensuu J.J., Richman A., Menassa R.. Plant Biotechnol. J. 2011, 9:419-433.
http://www.ncbi.nlm.nih.gov/pubmed/21338467
2010
Exploring laccase-like multicopper oxidase genes from the ascomycete Trichoderma reesei: a functional, phylogenetic and evolutionary study. Levasseur A., Saloheimo M., Navarro D., Andberg M., Pontarotti P., Kruus K., Record E.. BMC Biochem. 2010, 11:32. http://www.ncbi.nlm.nih.gov/pubmed/20735824
Secreted fungal sulfhydryl oxidases: sequence analysis and characterisation of a representative flavin-dependent enzyme from Aspergillus oryzae. Faccio G., Kruus K., Buchert J., Saloheimo M..
BMC Biochem. 2010, 11:31. http://www.ncbi.nlm.nih.gov/pubmed/20727152
Detecting novel genes with sparse arrays. Arvas M., Haiminen N., Smit B., Rautio J., Vitikainen M., Wiebe M., Martinez D., Chee C., Kunkel J., Sanchez C., Nelson M.A., Pakula T., Saloheimo M., Penttilä M., Kivioja T. Gene. 2010, 467:41-51. http://www.ncbi.nlm.nih.gov/pubmed/20691772
Array comparative genomic hybridization analysis of Trichoderma reesei strains with enhanced cellulase production properties. Vitikainen M., Arvas M., Pakula T., Oja M., Penttilä M., Saloheimo M.. BMC Genomics. 2010, 11:441. http://www.ncbi.nlm.nih.gov/pubmed/20642838
Discovery of a new tyrosinase-like enzyme family lacking a C-terminally processed domain: production and characterization of an Aspergillus oryzae catechol oxidase. Gasparetti C., Faccio G., Arvas M., Buchert J., Saloheimo M., Kruus K.. Appl. Microbiol. Biotechnol. 2010, 86:213-26. http://www.ncbi.nlm.nih.gov/pubmed/19798497
Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Joensuu J.J., Conley A.J., Lienemann M., Brandle J.E., Linder M.B., Menassa R..
Plant Physiol. 2010, 52:622-633. http://www.ncbi.nlm.nih.gov/pubmed/20018596