Popova, Blagovesta

[["dc.bibliographiccitation.firstpage","14"],["dc.bibliographiccitation.journal","Environmental and Experimental Botany"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Hoppenau, Clara E."],["dc.contributor.author","Tran, Van-Tuan"],["dc.contributor.author","Kusch, Harald"],["dc.contributor.author","Aßhauer, Kathrin P."],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Meinicke, Peter"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-04-24T15:04:17Z"],["dc.date.available","2018-04-24T15:04:17Z"],["dc.date.issued","2014"],["dc.description.abstract","The vascular plant pathogen Verticillium dahliae colonizes the xylem fluid where only low nutrient concentrations are provided. Biosynthesis of the vitamin thiamine is connected to oxidative stress. The highly conserved VdThi4 protein is localized in fungal mitochondria and is required under vitamin B1 limiting conditions. Deletion of the corresponding VdTHI4 gene by Agrobacterium-mediated transformation resulted in strains which were impaired in growth on thiamine-free medium and could be rescued by additional vitamin supply or by complementation with the original gene after protoplastation. Furthermore, we show that VdThi4 increases fungal stress tolerance such as UV-damage or oxidative stress. The orthologous sti35 gene of Fusarium oxysporum, another vascular wilt fungus, was shown to be involved in stress response, however to be dispensable for pathogenicity on tomato. In contrast, VdTHI4 is required for fungal-induced tomato disease demonstrated by infection assays with a V. dahliae ΔVdTHI4 deletion strain which is still able to invade plants through the roots but is asymptomatic. Our results suggest remarkable differences between two vascular tomato pathogens where VdThi4 is required for pathogenicity of V. dahliae, whereas F. oxysporum still causes disease when the corresponding Sti35 protein is absent."],["dc.description.sponsorship","Federal Ministry of Education and Research (BMBF)"],["dc.description.sponsorship","Cluster of Excellence and DFG Research Center Nanoscale Microscopy and Molecular Physiology of the Brain"],["dc.identifier.doi","10.1016/j.envexpbot.2013.12.015"],["dc.identifier.other","http://www.sciencedirect.com/science/article/pii/S0098847213002268"],["dc.identifier.pii","S0098847213002268"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13764"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.notes.status","zu prüfen"],["dc.relation.issn","0098-8472"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Verticillium dahliae VdTHI4, involved in thiazole biosynthesis, stress response and DNA repair functions, is required for vascular disease induction in tomato"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1007141"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Heinrich, Gabriele"],["dc.contributor.author","Gross, Carina"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Braus, Gerhard H."],["dc.creator.editor","Brakhage, Axel A."],["dc.date.accessioned","2018-04-23T11:47:09Z"],["dc.date.available","2018-04-23T11:47:09Z"],["dc.date.issued","2018"],["dc.description.abstract","The transition from vegetative growth to multicellular development represents an evolutionary hallmark linked to an oxidative stress signal and controlled protein degradation. We identified the Sem1 proteasome subunit, which connects stress response and cellular differentiation. The sem1 gene encodes the fungal counterpart of the human Sem1 proteasome lid subunit and is essential for fungal cell differentiation and development. A sem1 deletion strain of the filamentous fungus Aspergillus nidulans is able to grow vegetatively and expresses an elevated degree of 20S proteasomes with multiplied ATP-independent catalytic activity compared to wildtype. Oxidative stress induces increased transcription of the genes sem1 and rpn11 for the proteasomal deubiquitinating enzyme. Sem1 is required for stabilization of the Rpn11 deubiquitinating enzyme, incorporation of the ubiquitin receptor Rpn10 into the 19S regulatory particle and efficient 26S proteasome assembly. Sem1 maintains high cellular NADH levels, controls mitochondria integrity during stress and developmental transition."],["dc.identifier.doi","10.1371/journal.pgen.1007141"],["dc.identifier.gro","3142187"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15668"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13306"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Sem1 links proteasome stability and specificity to multicellular development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Rajavel, Abirami"],["dc.contributor.author","Dhamotharan, Karthikeyan"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-06-01T09:42:26Z"],["dc.date.available","2021-06-01T09:42:26Z"],["dc.date.issued","2021"],["dc.description.abstract","Aggregation of α-synuclein (αSyn) into proteinaceous deposits is a pathological hallmark of a range of neurodegenerative diseases including Parkinson’s disease (PD). Numerous lines of evidence indicate that the accumulation of toxic oligomeric and prefibrillar αSyn species may underpin the cellular toxicity and spread of pathology between cells. Therefore, aggregation of αSyn is considered a priority target for drug development, as aggregation inhibitors are expected to reduce αSyn toxicity and serve as therapeutic agents. Here, we used the budding yeast S. cerevisiae as a platform for the identification of short peptides that inhibit αSyn aggregation and toxicity. A library consisting of approximately one million peptide variants was utilized in two high-throughput screening approaches for isolation of library representatives that reduce αSyn-associated toxicity and aggregation. Seven peptides were isolated that were able to suppress specifically αSyn toxicity and aggregation in living cells. Expression of the peptides in yeast reduced the accumulation of αSyn-induced reactive oxygen species and increased cell viability. Next, the peptides were chemically synthesized and probed for their ability to modulate αSyn aggregation in vitro . Two synthetic peptides, K84s and K102s, of 25 and 19 amino acids, respectively, significantly inhibited αSyn oligomerization and aggregation at sub-stoichiometric molar ratios. Importantly, K84s reduced αSyn aggregation in human cells. These peptides represent promising αSyn aggregation antagonists for the development of future therapeutic interventions."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3389/fnmol.2021.659926"],["dc.identifier.pmid","33912013"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85254"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/420"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1662-5099"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Magalhães, Rayne S S"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus, Gerhard H"],["dc.contributor.author","Outeiro, Tiago F"],["dc.contributor.author","Eleutherio, Elis C A"],["dc.date.accessioned","2020-12-10T18:19:12Z"],["dc.date.available","2020-12-10T18:19:12Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1093/femsyr/foy066"],["dc.identifier.eissn","1567-1364"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75156"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The trehalose protective mechanism during thermal stress in Saccharomyces cerevisiae: the roles of Ath1 and Agt1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1006098"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Kleinknecht, Alexandra"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.editor","Lu, Bingwei"],["dc.date.accessioned","2018-09-28T07:41:43Z"],["dc.date.available","2018-09-28T07:41:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Parkinson´s disease (PD) is characterized by the presence of proteinaceous inclusions called Lewy bodies that are mainly composed of α-synuclein (αSyn). Elevated levels of oxidative or nitrative stresses have been implicated in αSyn related toxicity. Phosphorylation of αSyn on serine 129 (S129) modulates autophagic clearance of inclusions and is prominently found in Lewy bodies. The neighboring tyrosine residues Y125, Y133 and Y136 are phosphorylation and nitration sites. Using a yeast model of PD, we found that Y133 is required for protective S129 phosphorylation and for S129-independent proteasome clearance. αSyn can be nitrated and form stable covalent dimers originating from covalent crosslinking of two tyrosine residues. Nitrated tyrosine residues, but not di-tyrosine-crosslinked dimers, contributed to αSyn cytotoxicity and aggregation. Analysis of tyrosine residues involved in nitration and crosslinking revealed that the C-terminus, rather than the N-terminus of αSyn, is modified by nitration and di-tyrosine formation. The nitration level of wild-type αSyn was higher compared to that of A30P mutant that is non-toxic in yeast. A30P formed more dimers than wild-type αSyn, suggesting that dimer formation represents a cellular detoxification pathway in yeast. Deletion of the yeast flavohemoglobin gene YHB1 resulted in an increase of cellular nitrative stress and cytotoxicity leading to enhanced aggregation of A30P αSyn. Yhb1 protected yeast from A30P-induced mitochondrial fragmentation and peroxynitrite-induced nitrative stress. Strikingly, overexpression of neuroglobin, the human homolog of YHB1, protected against αSyn inclusion formation in mammalian cells. In total, our data suggest that C-terminal Y133 plays a major role in αSyn aggregate clearance by supporting the protective S129 phosphorylation for autophagy and by promoting proteasome clearance. C-terminal tyrosine nitration increases pathogenicity and can only be partially detoxified by αSyn di-tyrosine dimers. Our findings uncover a complex interplay between S129 phosphorylation and C-terminal tyrosine modifications of αSyn that likely participates in PD pathology."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1371/journal.pgen.1006098"],["dc.identifier.pmid","27341336"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15831"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","27567"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","27579"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Petroi, Doris"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Taheri-Talesh, Naimeh"],["dc.contributor.author","Irniger, Stefan"],["dc.contributor.author","Shahpasandzadeh, Hedieh"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T08:45:30Z"],["dc.date.available","2018-09-28T08:45:30Z"],["dc.date.issued","2012"],["dc.description.abstract","Parkinson disease is the second most common neurodegenerative disease. The molecular hallmark is the accumulation of proteinaceous inclusions termed Lewy bodies containing misfolded and aggregated α-synuclein. The molecular mechanism of clearance of α-synuclein aggregates was addressed using the bakers' yeast Saccharomyces cerevisiae as the model. Overexpression of wild type α-synuclein or the genetic variant A53T integrated into one genomic locus resulted in a gene copy-dependent manner in cytoplasmic proteinaceous inclusions reminiscent of the pathogenesis of the disease. In contrast, overexpression of the genetic variant A30P resulted only in transient aggregation, whereas the designer mutant A30P/A36P/A76P neither caused aggregation nor impaired yeast growth. The α-synuclein accumulation can be cleared after promoter shut-off by a combination of autophagy and vacuolar protein degradation. Whereas the proteasomal inhibitor MG-132 did not significantly inhibit aggregate clearance, treatment with phenylmethylsulfonyl fluoride, an inhibitor of vacuolar proteases, resulted in significant reduction in clearance. Consistently, a cim3-1 yeast mutant restricted in the 19 S proteasome regulatory subunit was unaffected in clearance, whereas an Δatg1 yeast mutant deficient in autophagy showed a delayed aggregate clearance response. A cim3-1Δatg1 double mutant was still able to clear aggregates, suggesting additional cellular mechanisms for α-synuclein clearance. Our data provide insight into the mechanisms yeast cells use for clearing different species of α-synuclein and demonstrate a higher contribution of the autophagy/vacuole than the proteasome system. This contributes to the understanding of how cells can cope with toxic and/or aggregated proteins and may ultimately enable the development of novel strategies for therapeutic intervention."],["dc.identifier.doi","10.1074/jbc.M112.361865"],["dc.identifier.pmid","22722939"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15838"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.title","Aggregate clearance of α-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0136778"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Schubert, Steffen"],["dc.contributor.author","Bulla, Ingo"],["dc.contributor.author","Buchwald, Daniela"],["dc.contributor.author","Kramer, Wilfried"],["dc.date.accessioned","2017-09-07T11:53:54Z"],["dc.date.available","2017-09-07T11:53:54Z"],["dc.date.issued","2015"],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1371/journal.pone.0136778"],["dc.identifier.gro","3151415"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12100"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8214"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.publisher","Public Library of Science (PLoS)"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A Robust and Versatile Method of Combinatorial Chemical Synthesis of Gene Libraries via Hierarchical Assembly of Partially Randomized Modules"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1009407"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Pätz, Christina"],["dc.contributor.author","Akkermann, Dagmar"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Galka, Dajana"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-04-14T08:28:05Z"],["dc.date.available","2021-04-14T08:28:05Z"],["dc.date.issued","2021"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1371/journal.pgen.1009407"],["dc.identifier.pmid","33657088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82500"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/140"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","1553-7404"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY 4.0"],["dc.title","DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","168"],["dc.bibliographiccitation.journal","Diamond and Related Materials"],["dc.bibliographiccitation.lastpage","178"],["dc.bibliographiccitation.volume","93"],["dc.contributor.author","Merker, Daniel"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Bergfeldt, Thomas"],["dc.contributor.author","Weingärtner, Tobias"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Reithmaier, Johann Peter"],["dc.contributor.author","Popov, Cyril"],["dc.date.accessioned","2020-12-10T14:23:27Z"],["dc.date.available","2020-12-10T14:23:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.diamond.2019.02.003"],["dc.identifier.issn","0925-9635"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71929"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Antimicrobial propensity of ultrananocrystalline diamond films with embedded silver nanodroplets"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Simm, Dominic"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Waack, Stephan"],["dc.contributor.author","Kollmar, Martin"],["dc.date.accessioned","2022-07-01T07:34:51Z"],["dc.date.available","2022-07-01T07:34:51Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Heterologous protein expression is an important method for analysing cellular functions of proteins, in genetic circuit engineering and in overexpressing proteins for biopharmaceutical applications and structural biology research. The degeneracy of the genetic code, which enables a single protein to be encoded by a multitude of synonymous gene sequences, plays an important role in regulating protein expression, but substantial uncertainty exists concerning the details of this phenomenon. Here we analyse the influence of a profiled codon usage adaptation approach on protein expression levels in the eukaryotic model organism Saccharomyces cerevisiae . We selected green fluorescent protein (GFP) and human α-synuclein (αSyn) as representatives for stable and intrinsically disordered proteins and representing a benchmark and a challenging test case. A new approach was implemented to design typical genes resembling the codon usage of any subset of endogenous genes. Using this approach, synthetic genes for GFP and αSyn were generated, heterologously expressed and evaluated in yeast. We demonstrate that GFP is expressed at high levels, and that the toxic αSyn can be adapted to endogenous, low-level expression. The new software is publicly available as a web-application for performing host-specific protein adaptations to a set of the most commonly used model organisms ( https://odysseus.motorprotein.de )."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Georg-August-Universität Göttingen http://dx.doi.org/10.13039/501100003385"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41598-022-13089-1"],["dc.identifier.pii","13089"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112027"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.eissn","2045-2322"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Design of typical genes for heterologous gene expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]