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The Mut + strain of Komagataella phaffii ( Pichia pastoris) expresses P AOX1 5 and 10 times faster than Mut s and Mut \u2212 strains: Evidence that formaldehyde or\/and formate are true inducers of AOX. https:\/\/doi.org\/10.1101\/573519.","DOI":"10.1007\/s00253-020-10793-8"},{"key":"10.1016\/j.jbiotec.2025.09.015_bib133","doi-asserted-by":"crossref","first-page":"7801","DOI":"10.1007\/s00253-020-10793-8","article-title":"The mut+ strain of komagataella phaffii (Pichia pastoris) expresses PAOX1 5 and 10 times faster than muts and mut\u2212 strains: evidence that formaldehyde or\/and formate are true inducers of PAOX1","volume":"104","author":"Singh","year":"2020","journal-title":"Appl. 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Colloid Interface Sci."},{"key":"10.1016\/j.jbiotec.2025.09.015_bib157","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1271\/bbb.59.439","article-title":"The phylogenetic relationships of Methanol-assimilating yeasts based on the partial sequences of 18S and 26S ribosomal RNAs: the proposal of komagataella gen. Nov. (Saccharomycetaceae)","volume":"59","author":"Yamada","year":"1995","journal-title":"Biosci. Biotechnol. Biochem"},{"key":"10.1016\/j.jbiotec.2025.09.015_bib158","doi-asserted-by":"crossref","DOI":"10.1016\/j.biotechadv.2025.108570","article-title":"Advances in antimicrobial peptides: from mechanistic insights to chemical modifications","author":"Yang","year":"2025","journal-title":"Biotechnol. 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Microbiol."},{"key":"10.1016\/j.jbiotec.2025.09.015_bib164","doi-asserted-by":"crossref","DOI":"10.1186\/s12934-021-01635-x","article-title":"Design and heterologous expression of a novel dimeric LL37 variant in pichia pastoris","volume":"20","author":"Zhan","year":"2021","journal-title":"Micro Cell Fact."},{"key":"10.1016\/j.jbiotec.2025.09.015_bib165","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s00253-023-12947-w","article-title":"Expression and characterization of the new antimicrobial peptide AP138L-arg26 anti staphylococcus aureus","volume":"108","author":"Zhang","year":"2024","journal-title":"Appl. Microbiol Biotechnol."},{"key":"10.1016\/j.jbiotec.2025.09.015_bib166","article-title":"Antimicrobial peptides: from discovery to developmental applications","author":"Zhang","year":"2025","journal-title":"Appl. Environ. 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