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  1. Book ; Thesis: Änderungen physiologischer Parameter bei der Schwereübung des Autogenen Trainings und anderen Vigilanzsenkungen

    Polzien, Martina

    2006  

    Author's details vorgelegt von Martina Polzien
    Language German
    Size 69 S., graph. Darst.
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Würzburg, Univ., Diss., 2007
    HBZ-ID HT015221160
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    2007 D 769 order for loan Magazin

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  2. Book ; Thesis: Unterschiede in Wachstum und Entwicklung bei Spaltträgern und Nichtspaltträgern

    Geier, Martina

    1985  

    Author's details vorgelegt von Martina Geier geb. Pein
    Size 103, XVI, 2 Bl. : Ill., graph. Darst.
    Publishing country XA-DDDE
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Berlin, Humboldt-Univ., Diss. A, 1985 (Nicht f.d. Austausch)
    HBZ-ID HT002954701
    Database Catalogue ZB MED Medicine, Health

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    87 E 1714 order for loan Magazin

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  3. Article ; Online: Whole Genome Sequencing Analysis of Effects of CRISPR/Cas9 in

    Schusterbauer, Veronika / Fischer, Jasmin E / Gangl, Sarah / Schenzle, Lisa / Rinnofner, Claudia / Geier, Martina / Sailer, Christian / Glieder, Anton / Thallinger, Gerhard G

    Journal of fungi (Basel, Switzerland)

    2022  Volume 8, Issue 10

    Abstract: The industrially important non-conventional ... ...

    Abstract The industrially important non-conventional yeast
    Language English
    Publishing date 2022-09-21
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2784229-0
    ISSN 2309-608X ; 2309-608X
    ISSN (online) 2309-608X
    ISSN 2309-608X
    DOI 10.3390/jof8100992
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Compact multi-enzyme pathways in P. pastoris.

    Geier, Martina / Fauland, Pia / Vogl, Thomas / Glieder, Anton

    Chemical communications (Cambridge, England)

    2015  Volume 51, Issue 9, Page(s) 1643–1646

    Abstract: We report for the first time the functional simultaneous expression of nine genes from a single 2A peptide based polycistronic expression construct. The feasibility and arising opportunities for the biosynthetic pathway balancing for chemical production ... ...

    Abstract We report for the first time the functional simultaneous expression of nine genes from a single 2A peptide based polycistronic expression construct. The feasibility and arising opportunities for the biosynthetic pathway balancing for chemical production were demonstrated by the co-expression of the violacein and carotenoid biosynthesis pathways.
    MeSH term(s) Biosynthetic Pathways/genetics ; Carotenoids/metabolism ; Enzymes/genetics ; Enzymes/metabolism ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Gene Expression Regulation, Fungal ; Indoles/metabolism ; Multigene Family/genetics ; Pichia/enzymology ; Pichia/genetics
    Chemical Substances Enzymes ; Fungal Proteins ; Indoles ; Carotenoids (36-88-4) ; violacein (QJH0DSQ3SG)
    Language English
    Publishing date 2015-01-31
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c4cc08502g
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Compact multi-enzyme pathways in P. pastoris

    Geier, Martina / Fauland, Pia / Vogl, Thomas / Glieder, Anton

    Chemical communications. 2015 Jan. 15, v. 51, no. 9

    2015  

    Abstract: We report for the first time the functional simultaneous expression of nine genes from a single 2A peptide based polycistronic expression construct. The feasibility and arising opportunities for the biosynthetic pathway balancing for chemical production ... ...

    Abstract We report for the first time the functional simultaneous expression of nine genes from a single 2A peptide based polycistronic expression construct. The feasibility and arising opportunities for the biosynthetic pathway balancing for chemical production were demonstrated by the co-expression of the violacein and carotenoid biosynthesis pathways.
    Keywords Komagataella pastoris ; biochemical pathways ; biosynthesis ; carotenoids ; chemical reactions ; gene expression ; genes ; peptides ; violacein
    Language English
    Dates of publication 2015-0115
    Size p. 1643-1646.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/c4cc08502g
    Database NAL-Catalogue (AGRICOLA)

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  6. Article: Racemization-free and scalable amidation of l-proline in organic media using ammonia and a biocatalyst only

    Pitzer, Julia / Steiner, Kerstin / Schmid, Christian / Schein, Viktor K. / Prause, Christoph / Kniely, Claudia / Reif, Michaela / Geier, Martina / Pietrich, Elena / Reiter, Tamara / Selig, Philipp / Stückler, Clemens / Pöchlauer, Peter / Steinkellner, Georg / Gruber, Karl / Schwab, Helmut / Glieder, Anton / Kroutil, Wolfgang

    Green chemistry. 2022 July 4, v. 24, no. 13

    2022  

    Abstract: Efficient amide formation is of high importance for the chemical and pharmaceutical industry. The direct biocatalytic one-pot transformation of acids into amides without substrate activation is a highly desirable but highly challenging reaction; this is ... ...

    Abstract Efficient amide formation is of high importance for the chemical and pharmaceutical industry. The direct biocatalytic one-pot transformation of acids into amides without substrate activation is a highly desirable but highly challenging reaction; this is why in general the acid is activated using additional reagents before amide formation occurs. In particular, amidation of α-amino acids is challenging and in general requires protection strategies for the amino functionality. A further challenge is the low solubility of the unprotected amino acids in organic solvents. Furthermore, the amidation process is prone to racemisation as observed for the acyl chloride derivative. These three challenges may be addressed using biocatalysis. Here the enzyme catalyzed, racemization-free amidation of unprotected l-proline with ammonia in an organic solvent is described. Comprehensive reaction, solvent and enzyme engineering allowed obtaining high l-prolinamide concentrations. For instance at 145 mM substrate concentration, 80% conversion was achieved employing an immobilized CalB variant and ammonia in 2-methyl-2-butanol at 70 °C. A two-fold increase in l-prolinamide formation was achieved employing the immobilized and engineered enzyme variant CalBopt-24 T245S compared to wild type CalB. In contrast to chemical processes, racemization, halogenated solvents and waste are avoided/minimized and atom efficiency is significantly improved from 45.5% to 86.4%. The excellent optical purity of the obtained product (ee >99%) and the stability of immobilized CalB pave the way for an innovative industrial process to produce l-prolinamide, a key intermediate in drug synthesis.
    Keywords amides ; ammonia ; biocatalysis ; biocatalysts ; drugs ; enzymes ; green chemistry ; pharmaceutical industry ; proline ; solubility ; solvents ; wastes
    Language English
    Dates of publication 2022-0704
    Size p. 5171-5180.
    Publishing place The Royal Society of Chemistry
    Document type Article
    ZDB-ID 2006274-6
    ISSN 1463-9270 ; 1463-9262
    ISSN (online) 1463-9270
    ISSN 1463-9262
    DOI 10.1039/d2gc00783e
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: Human Enzymes for Organic Synthesis.

    Winkler, Margit / Geier, Martina / Hanlon, Steven P / Nidetzky, Bernd / Glieder, Anton

    Angewandte Chemie (International ed. in English)

    2018  Volume 57, Issue 41, Page(s) 13406–13423

    Abstract: Human enzymes have been widely studied in various disciplines. The number of reactions taking place in the human body is vast, and so is the number of potential catalysts for synthesis. Herein, we focus on the application of human enzymes that catalyze ... ...

    Abstract Human enzymes have been widely studied in various disciplines. The number of reactions taking place in the human body is vast, and so is the number of potential catalysts for synthesis. Herein, we focus on the application of human enzymes that catalyze chemical reactions in course of the metabolism of drugs and xenobiotics. Some of these reactions have been explored on the preparative scale. The major field of application of human enzymes is currently drug development, where they are applied for the synthesis of drug metabolites.
    MeSH term(s) Enzymes/metabolism ; Humans
    Chemical Substances Enzymes
    Language English
    Publishing date 2018-09-11
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2011836-3
    ISSN 1521-3773 ; 1433-7851
    ISSN (online) 1521-3773
    ISSN 1433-7851
    DOI 10.1002/anie.201800678
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  8. Article ; Online: Towards systems metabolic engineering in Pichia pastoris.

    Schwarzhans, Jan-Philipp / Luttermann, Tobias / Geier, Martina / Kalinowski, Jörn / Friehs, Karl

    Biotechnology advances

    2017  Volume 35, Issue 6, Page(s) 681–710

    Abstract: The methylotrophic yeast Pichia pastoris is firmly established as a host for the production of recombinant proteins, frequently outperforming other heterologous hosts. Already, a sizeable amount of systems biology knowledge has been acquired for this non- ...

    Abstract The methylotrophic yeast Pichia pastoris is firmly established as a host for the production of recombinant proteins, frequently outperforming other heterologous hosts. Already, a sizeable amount of systems biology knowledge has been acquired for this non-conventional yeast. By applying various omics-technologies, productivity features have been thoroughly analyzed and optimized via genetic engineering. However, challenging clonal variability, limited vector repertoire and insufficient genome annotation have hampered further developments. Yet, in the last few years a reinvigorated effort to establish P. pastoris as a host for both protein and metabolite production is visible. A variety of compounds from terpenoids to polyketides have been synthesized, often exceeding the productivity of other microbial systems. The clonal variability was systematically investigated and strategies formulated to circumvent untargeted events, thereby streamlining the screening procedure. Promoters with novel regulatory properties were discovered or engineered from existing ones. The genetic tractability was increased via the transfer of popular manipulation and assembly techniques, as well as the creation of new ones. A second generation of sequencing projects culminated in the creation of the second best functionally annotated yeast genome. In combination with landmark physiological insights and increased output of omics-data, a good basis for the creation of refined genome-scale metabolic models was created. The first application of model-based metabolic engineering in P. pastoris showcased the potential of this approach. Recent efforts to establish yeast peroxisomes for compartmentalized metabolite synthesis appear to fit ideally with the well-studied high capacity peroxisomal machinery of P. pastoris. Here, these recent developments are collected and reviewed with the aim of supporting the establishment of systems metabolic engineering in P. pastoris.
    Language English
    Publishing date 2017-11-01
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 47165-3
    ISSN 1873-1899 ; 0734-9750
    ISSN (online) 1873-1899
    ISSN 0734-9750
    DOI 10.1016/j.biotechadv.2017.07.009
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  9. Article ; Online: Biocatalytic Characterization of Human FMO5: Unearthing Baeyer-Villiger Reactions in Humans.

    Fiorentini, Filippo / Geier, Martina / Binda, Claudia / Winkler, Margit / Faber, Kurt / Hall, Mélanie / Mattevi, Andrea

    ACS chemical biology

    2016  Volume 11, Issue 4, Page(s) 1039–1048

    Abstract: Flavin-containing mono-oxygenases are known as potent drug-metabolizing enzymes, providing complementary functions to the well-investigated cytochrome P450 mono-oxygenases. While human FMO isoforms are typically involved in the oxidation of soft ... ...

    Abstract Flavin-containing mono-oxygenases are known as potent drug-metabolizing enzymes, providing complementary functions to the well-investigated cytochrome P450 mono-oxygenases. While human FMO isoforms are typically involved in the oxidation of soft nucleophiles, the biocatalytic activity of human FMO5 (along its physiological role) has long remained unexplored. In this study, we demonstrate the atypical in vitro activity of human FMO5 as a Baeyer-Villiger mono-oxygenase on a broad range of substrates, revealing the first example to date of a human protein catalyzing such reactions. The isolated and purified protein was active on diverse carbonyl compounds, whereas soft nucleophiles were mostly non- or poorly reactive. The absence of the typical characteristic sequence motifs sets human FMO5 apart from all characterized Baeyer-Villiger mono-oxygenases so far. These findings open new perspectives in human oxidative metabolism.
    MeSH term(s) Biocatalysis ; Humans ; Oxygenases/metabolism
    Chemical Substances Oxygenases (EC 1.13.-) ; dimethylaniline monooxygenase (N-oxide forming) (EC 1.14.13.8)
    Language English
    Publishing date 2016-04-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.5b01016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Methanol independent induction in Pichia pastoris by simple derepressed overexpression of single transcription factors.

    Vogl, Thomas / Sturmberger, Lukas / Fauland, Pia C / Hyden, Patrick / Fischer, Jasmin E / Schmid, Christian / Thallinger, Gerhard G / Geier, Martina / Glieder, Anton

    Biotechnology and bioengineering

    2018  Volume 115, Issue 4, Page(s) 1037–1050

    Abstract: Carbon source regulated promoters are well-studied standard tools for controlling gene expression. Acquiring control over the natural regulation of promoters is important for metabolic engineering and synthetic biology applications. In the commonly used ... ...

    Abstract Carbon source regulated promoters are well-studied standard tools for controlling gene expression. Acquiring control over the natural regulation of promoters is important for metabolic engineering and synthetic biology applications. In the commonly used protein production host Komagataella phaffii (Pichia pastoris), methanol-inducible promoters are used because of their tight regulation and exceptional strength. Yet, induction with toxic and flammable methanol can be a considerable safety risk and cannot be applied in many existing fermentation plants. Here we studied new regulatory circuits based on the most frequently used alcohol oxidase 1 promoter (P
    MeSH term(s) Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Gene Expression Profiling ; Gene Expression Regulation, Fungal/genetics ; Glucose/metabolism ; Glycerol/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Methanol/metabolism ; Methionine Sulfoxide Reductases/genetics ; Methionine Sulfoxide Reductases/metabolism ; Pichia/enzymology ; Pichia/genetics ; Plasmids/genetics ; Promoter Regions, Genetic/genetics ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances Fungal Proteins ; Membrane Proteins ; Repressor Proteins ; Transcription Factors ; Methionine Sulfoxide Reductases (EC 1.8.4.-) ; Glucose (IY9XDZ35W2) ; Glycerol (PDC6A3C0OX) ; Methanol (Y4S76JWI15)
    Language English
    Publishing date 2018-01-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 280318-5
    ISSN 1097-0290 ; 0006-3592
    ISSN (online) 1097-0290
    ISSN 0006-3592
    DOI 10.1002/bit.26529
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