Kipriyanov SM, Kupriyanova OA, Little M, Moldenhauer G (1996) Rapid detection of recombinant
antibody fragments directed against cell-surface
antigens by flow cytometry. J Immunol Methods
196:51–62
Kistler HC, Broz K (2015) Cellular compartmentalization of secondary metabolism. Front Microbiol
6:68
Kitamoto N, Matsui J, Kawai Y, Kato A, Yoshino S,
Ohmiya K, Tsukagoshi N (1998) Utilization of the
TEF1-a gene (TEF1) promoter for expression of
polygalacturonase genes, pgaA and pgaB, in Aspergillus oryzae. Appl Microbiol Biotechnol 50:85–92
Kitamoto N, Ono N, Yoshino Yasuda S (2015) Construction of quintuple protease and double amylase gene deletant for heterologous protein
production in Aspergillus oryzae KBN616. Food
Sci Technol Res 21:297–307
Kluge J, Terfehr D, Ku ¨ck U (2018) Inducible promoters
and functional genomic approaches for the genetic
engineering of filamentous fungi. Appl Microbiol
Biotechnol 102:6357–6372
Knudsen PB (2015) Development of scalable high
throughput fermentation approaches for physiological characterisation of yeast and filamentous
fungi. PhD thesis, Technical University of Denmark (DTU)
Krappmann S (2007) Gene targeting in filamentous
fungi: the benefits of impaired repair. Fungal Biol
Rev 21:25–29
Krishnan K, Askew DS (2014) The fungal UPR: a regulatory hub for virulence traits in the mold pathogen Aspergillus fumigatus. Virulence 5:334–340
Kru ¨gel H, Fiedler G, Smith C, Baumberg S (1993)
Sequence and transcriptional analysis of the nourseothricin acetyltransferase-encoding gene nat1
from Streptomyces noursei. Gene 127:127–131
Kubodera T, Yamashita N, Nishimura A (2002) Transformation of Aspergillus sp. and Trichoderma reesei using the pyrithiamine resistance gene (ptrA)
of Aspergillus oryzae. Biosci Biotechnol Biochem
66:404–406
Kupfer DM, Drabenstot SD, Buchanan KL, Hongshing
L, Zhu H, Dyer DW, Roe BA, Murphy JW (2004)
Introns and splicing elements of five diverse fungi.
Eukaryot Cell 3:1088–1100
Kurzatkowski W, To ¨rro ¨nen A, Filipek J, Mach RL, Herzog P, Sowka S, Kubicek CP (1996) Glucoseinduced secretion of Trichoderma reesei xylanases.
Appl Environ Microbiol 62:2859–2865
Kwon MJ, Arentshorst M, Roos ED, Van Den Hondel
CAMJJ, Meyer V, Ram AFJ (2011) Functional characterization of Rho GTPases in Aspergillus niger
uncovers conserved and diverged roles of Rho
proteins within filamentous fungi. Mol Microbiol
79:1151–1167
Lamb TM, Vickery J, Bell-Pedersen D (2013) Regulation
of gene expression in Neurospora crassa with a
copper responsive promoter. G3 3:2273–2280
Landowski CP, Huuskonen A, Wahl R, WesterholmParvinen A, Kanerva A, Ha ¨nninen AL, Salovuori
N, Penttila ¨ M, Natunen J, Ostermeier C, Helk B,
Saarinen J, Saloheimo M (2015) Enabling low cost
biopharmaceuticals: a systematic approach to
delete proteases from a well-known protein
production host Trichoderma reesei. PLoS One
10:1–28
Landowski CP, Mustalahti E, Wahl R, Croute L, Sivasiddarthan D, Westerholm-Parvinen A, Sommer B,
Ostermeier C, Helk B, Saarinen J, Saloheimo M
(2016) Enabling low cost biopharmaceuticals:
high level interferon alpha-2b production in Trichoderma reesei. Microb Cell Factories 15:1–15
Leach DRF (1994) Long DNA palindromes, cruciform
structures, genetic instability and secondary structure repair. BioEssays 16:893–900
Ley A, Coumou HC, Frandsen RJN (2015) Heterologous
expression of MlcE in Saccharomyces cerevisiae
provides resistance to natural and semi-synthetic
statins. Metab Eng Commun 2:117–123
Li H, d’Anjou M (2009) Pharmacological significance of
glycosylation in therapeutic proteins. Curr Opin
Biotechnol 20:678–684
Li J, Wang J, Wang S, Xing M, Yu S, Liu G (2012)
Achieving efficient protein expression in Trichoderma reesei by using strong constitutive promoters. Microb Cell Factories 11:1–10
Li W, Yu J, Li Z, Yin WB (2018) Rational design for
fungal laccase production in the model host Aspergillus nidulans. Sci China Life Sci 61:1–11
Lin C, Baldwin T, Estell D, Fung J, Lin C, Pucci J, Razo J,
Rider B, Throndset W, Trimbur D, Gastel F Van
Ward M (2006) Develop systems for
manufacturing 100,000,000 doses of an emergency
pharmaceutical (e.g. vaccine or monoclonal antibody) within 2 months of product identification.
Progress report, Genencor International, pp 1–21
Linder MB, Qiao M, Laumen F, Selber K, Hyytia ¨ T,
Nakari-Seta ¨la ¨ T, Penttila ¨ ME (2004) Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase
systems. Biochemistry 43:11873–11882
Liu R, Chen L, Jiang Y, Zhou Z, Zou G (2015) Efficient
genome editing in filamentous fungus Trichoderma reesei using the CRISPR/Cas9 system. Cell
Discov 1:1–11
Longley DB, Harkin DP, Johnston PG (2003) 5fluorouracil: mechanisms of action and clinical
strategies. Nat Rev Cancer 3:330–338
Lorang JM, Tuori RP, Martinez JP, Sawyer TL, Redman
RS, Rollins JA, Wolpert TJ, Johnson KB, Rodriguez
RJ, Dickman MB, Ciuffetti LM (2001) Green fluorescent protein is lighting up fungal biology. Appl
Environ Microbiol 67:1987–1994
Lubertozzi D, Keasling JD (2006) Marker and promoter
effects on heterologous expression in Aspergillus
nidulans. Appl Microbiol Biotechnol 72:1014–1023
260
J. K. H. Rendsvig et al.
antibody fragments directed against cell-surface
antigens by flow cytometry. J Immunol Methods
196:51–62
Kistler HC, Broz K (2015) Cellular compartmentalization of secondary metabolism. Front Microbiol
6:68
Kitamoto N, Matsui J, Kawai Y, Kato A, Yoshino S,
Ohmiya K, Tsukagoshi N (1998) Utilization of the
TEF1-a gene (TEF1) promoter for expression of
polygalacturonase genes, pgaA and pgaB, in Aspergillus oryzae. Appl Microbiol Biotechnol 50:85–92
Kitamoto N, Ono N, Yoshino Yasuda S (2015) Construction of quintuple protease and double amylase gene deletant for heterologous protein
production in Aspergillus oryzae KBN616. Food
Sci Technol Res 21:297–307
Kluge J, Terfehr D, Ku ¨ck U (2018) Inducible promoters
and functional genomic approaches for the genetic
engineering of filamentous fungi. Appl Microbiol
Biotechnol 102:6357–6372
Knudsen PB (2015) Development of scalable high
throughput fermentation approaches for physiological characterisation of yeast and filamentous
fungi. PhD thesis, Technical University of Denmark (DTU)
Krappmann S (2007) Gene targeting in filamentous
fungi: the benefits of impaired repair. Fungal Biol
Rev 21:25–29
Krishnan K, Askew DS (2014) The fungal UPR: a regulatory hub for virulence traits in the mold pathogen Aspergillus fumigatus. Virulence 5:334–340
Kru ¨gel H, Fiedler G, Smith C, Baumberg S (1993)
Sequence and transcriptional analysis of the nourseothricin acetyltransferase-encoding gene nat1
from Streptomyces noursei. Gene 127:127–131
Kubodera T, Yamashita N, Nishimura A (2002) Transformation of Aspergillus sp. and Trichoderma reesei using the pyrithiamine resistance gene (ptrA)
of Aspergillus oryzae. Biosci Biotechnol Biochem
66:404–406
Kupfer DM, Drabenstot SD, Buchanan KL, Hongshing
L, Zhu H, Dyer DW, Roe BA, Murphy JW (2004)
Introns and splicing elements of five diverse fungi.
Eukaryot Cell 3:1088–1100
Kurzatkowski W, To ¨rro ¨nen A, Filipek J, Mach RL, Herzog P, Sowka S, Kubicek CP (1996) Glucoseinduced secretion of Trichoderma reesei xylanases.
Appl Environ Microbiol 62:2859–2865
Kwon MJ, Arentshorst M, Roos ED, Van Den Hondel
CAMJJ, Meyer V, Ram AFJ (2011) Functional characterization of Rho GTPases in Aspergillus niger
uncovers conserved and diverged roles of Rho
proteins within filamentous fungi. Mol Microbiol
79:1151–1167
Lamb TM, Vickery J, Bell-Pedersen D (2013) Regulation
of gene expression in Neurospora crassa with a
copper responsive promoter. G3 3:2273–2280
Landowski CP, Huuskonen A, Wahl R, WesterholmParvinen A, Kanerva A, Ha ¨nninen AL, Salovuori
N, Penttila ¨ M, Natunen J, Ostermeier C, Helk B,
Saarinen J, Saloheimo M (2015) Enabling low cost
biopharmaceuticals: a systematic approach to
delete proteases from a well-known protein
production host Trichoderma reesei. PLoS One
10:1–28
Landowski CP, Mustalahti E, Wahl R, Croute L, Sivasiddarthan D, Westerholm-Parvinen A, Sommer B,
Ostermeier C, Helk B, Saarinen J, Saloheimo M
(2016) Enabling low cost biopharmaceuticals:
high level interferon alpha-2b production in Trichoderma reesei. Microb Cell Factories 15:1–15
Leach DRF (1994) Long DNA palindromes, cruciform
structures, genetic instability and secondary structure repair. BioEssays 16:893–900
Ley A, Coumou HC, Frandsen RJN (2015) Heterologous
expression of MlcE in Saccharomyces cerevisiae
provides resistance to natural and semi-synthetic
statins. Metab Eng Commun 2:117–123
Li H, d’Anjou M (2009) Pharmacological significance of
glycosylation in therapeutic proteins. Curr Opin
Biotechnol 20:678–684
Li J, Wang J, Wang S, Xing M, Yu S, Liu G (2012)
Achieving efficient protein expression in Trichoderma reesei by using strong constitutive promoters. Microb Cell Factories 11:1–10
Li W, Yu J, Li Z, Yin WB (2018) Rational design for
fungal laccase production in the model host Aspergillus nidulans. Sci China Life Sci 61:1–11
Lin C, Baldwin T, Estell D, Fung J, Lin C, Pucci J, Razo J,
Rider B, Throndset W, Trimbur D, Gastel F Van
Ward M (2006) Develop systems for
manufacturing 100,000,000 doses of an emergency
pharmaceutical (e.g. vaccine or monoclonal antibody) within 2 months of product identification.
Progress report, Genencor International, pp 1–21
Linder MB, Qiao M, Laumen F, Selber K, Hyytia ¨ T,
Nakari-Seta ¨la ¨ T, Penttila ¨ ME (2004) Efficient purification of recombinant proteins using hydrophobins as tags in surfactant-based two-phase
systems. Biochemistry 43:11873–11882
Liu R, Chen L, Jiang Y, Zhou Z, Zou G (2015) Efficient
genome editing in filamentous fungus Trichoderma reesei using the CRISPR/Cas9 system. Cell
Discov 1:1–11
Longley DB, Harkin DP, Johnston PG (2003) 5fluorouracil: mechanisms of action and clinical
strategies. Nat Rev Cancer 3:330–338
Lorang JM, Tuori RP, Martinez JP, Sawyer TL, Redman
RS, Rollins JA, Wolpert TJ, Johnson KB, Rodriguez
RJ, Dickman MB, Ciuffetti LM (2001) Green fluorescent protein is lighting up fungal biology. Appl
Environ Microbiol 67:1987–1994
Lubertozzi D, Keasling JD (2006) Marker and promoter
effects on heterologous expression in Aspergillus
nidulans. Appl Microbiol Biotechnol 72:1014–1023
260
J. K. H. Rendsvig et al.