Climate-specific biosynthetic gene clusters in populations of a lichen-forming fungus

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Environmental Microbiology, 23.2021, 8, S. 4260-4275

Event: Veröffentlichung

(where): Frankfurt am Main

(who): Universitätsbibliothek Johann Christian Senckenberg

(when): 2021

Creator: Singh, Garima
Calchera, Anjuli
Schulz, Meike
Drechsler, Moritz
Bode, Helge Björn
Schmitt, Imke
Dal Grande, Francesco

DOI: 10.1111/1462-2920.15605

URN: urn:nbn:de:hebis:30:3-723992

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 11:02 AM CEST

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Associated

Singh, Garima
Calchera, Anjuli
Schulz, Meike
Drechsler, Moritz
Bode, Helge Björn
Schmitt, Imke
Dal Grande, Francesco
Universitätsbibliothek Johann Christian Senckenberg

Time of origin

2021

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Identification and characterization of selected secondary metabolite biosynthetic pathways from Xenorhabdus nematophila

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Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

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Identification and characterization of selected secondary metabolite biosynthetic pathways from Xenorhabdus nematophila

Identification of the Sfp-type PPTase EppA from the lichenized fungus evernia prunastri

Biosynthetic gene content of the "Perfume Lichens" Evernia prunastri and Pseudevernia furfuracea

ω-Azido fatty acids as probes to detect fatty acid biosynthesis, degradation, and modification

The benzodiazepine-like natural product tilivalline is produced by the entomopathogenic bacterium Xenorhabdus eapokensis

Artificial splitting of a non‐ribosomal peptide synthetase by inserting natural docking domains

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

Hochschulschrift

Chemical and biosynthetic investigations of selected polyketides

Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Hochschulschrift

Identification and characterization of selected secondary metabolite biosynthetic pathways from Xenorhabdus nematophila

Identification of the Sfp-type PPTase EppA from the lichenized fungus evernia prunastri

Biosynthetic gene content of the "Perfume Lichens" Evernia prunastri and Pseudevernia furfuracea

ω-Azido fatty acids as probes to detect fatty acid biosynthesis, degradation, and modification

The benzodiazepine-like natural product tilivalline is produced by the entomopathogenic bacterium Xenorhabdus eapokensis

Artificial splitting of a non‐ribosomal peptide synthetase by inserting natural docking domains

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

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Climate-specific biosynthetic gene clusters in populations of a lichen-forming fungus

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Other Objects (12)

Chemical and biosynthetic investigations of selected polyketides

Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Identification and characterization of selected secondary metabolite biosynthetic pathways from Xenorhabdus nematophila

Identification of the Sfp-type PPTase EppA from the lichenized fungus evernia prunastri

Biosynthetic gene content of the "Perfume Lichens" Evernia prunastri and Pseudevernia furfuracea

ω-Azido fatty acids as probes to detect fatty acid biosynthesis, degradation, and modification

The benzodiazepine-like natural product tilivalline is produced by the entomopathogenic bacterium Xenorhabdus eapokensis

Artificial splitting of a non‐ribosomal peptide synthetase by inserting natural docking domains

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

Chemical and biosynthetic investigations of selected polyketides

Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Identification and characterization of selected secondary metabolite biosynthetic pathways from Xenorhabdus nematophila

Identification of the Sfp-type PPTase EppA from the lichenized fungus evernia prunastri

Biosynthetic gene content of the "Perfume Lichens" Evernia prunastri and Pseudevernia furfuracea

ω-Azido fatty acids as probes to detect fatty acid biosynthesis, degradation, and modification

The benzodiazepine-like natural product tilivalline is produced by the entomopathogenic bacterium Xenorhabdus eapokensis

Artificial splitting of a non‐ribosomal peptide synthetase by inserting natural docking domains

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

Chemical and biosynthetic investigations of selected polyketides

Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Artificial Splitting of a Non‐Ribosomal Peptide Synthetase by Inserting Natural Docking Domains

Identification and characterization of selected secondary metabolite biosynthetic pathways from Xenorhabdus nematophila

Identification of the Sfp-type PPTase EppA from the lichenized fungus evernia prunastri

Biosynthetic gene content of the "Perfume Lichens" Evernia prunastri and Pseudevernia furfuracea

ω-Azido fatty acids as probes to detect fatty acid biosynthesis, degradation, and modification

The benzodiazepine-like natural product tilivalline is produced by the entomopathogenic bacterium Xenorhabdus eapokensis

Artificial splitting of a non‐ribosomal peptide synthetase by inserting natural docking domains

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

Investigation of the Odilorhabdin Biosynthetic Gene Cluster Using NRPS Engineering

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