NMR resonance assignments for a docking domain pair with an attached thiolation domain from the PAX peptide-producing NRPS from Xenorhabdus cabanillasii
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Biomolecular NMR assignments, 15.2021, 1, S. 229-234
- Event
-
Veröffentlichung
- (where)
-
Frankfurt am Main
- (who)
-
Universitätsbibliothek Johann Christian Senckenberg
- (when)
-
2021
- Creator
- DOI
-
10.1007/s12104-021-10010-1
- URN
-
urn:nbn:de:hebis:30:3-637439
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:26 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Watzel, Jonas
- Sarawi, Sepas
- Duchardt-Ferner, Elke
- Bode, Helge Björn
- Wöhnert, Jens
- Universitätsbibliothek Johann Christian Senckenberg
Time of origin
- 2021
Other Objects (12)
Non-ribosomal peptide synthetase engineering focusing on the condensation domain and the condensation/adenylation domain interface
Chemical and biosynthetic investigations of selected polyketides
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
Cooperation between a T Domain and a Minimal C‐Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS
Cooperation between a T domain and a minimal C-terminal docking domain to enable specific assembly in a multiprotein NRPS
Target identification of peptides from Xenorhabdus and Photorhabdus
Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria
Identification of new natural products from nematode-associated bacteria using mass spectrometry
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
Phototemtide A, a Cyclic Lipopeptide Heterologously Expressed from Photorhabdus temperata Meg1, Shows Selective Antiprotozoal Activity
Non-ribosomal peptide synthetase engineering focusing on the condensation domain and the condensation/adenylation domain interface
Chemical and biosynthetic investigations of selected polyketides
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
Cooperation between a T Domain and a Minimal C‐Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS
Cooperation between a T domain and a minimal C-terminal docking domain to enable specific assembly in a multiprotein NRPS
Target identification of peptides from Xenorhabdus and Photorhabdus
Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria
Identification of new natural products from nematode-associated bacteria using mass spectrometry
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
Phototemtide A, a Cyclic Lipopeptide Heterologously Expressed from Photorhabdus temperata Meg1, Shows Selective Antiprotozoal Activity
Non-ribosomal peptide synthetase engineering focusing on the condensation domain and the condensation/adenylation domain interface
Chemical and biosynthetic investigations of selected polyketides
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
Cooperation between a T Domain and a Minimal C‐Terminal Docking Domain to Enable Specific Assembly in a Multiprotein NRPS
Cooperation between a T domain and a minimal C-terminal docking domain to enable specific assembly in a multiprotein NRPS
Target identification of peptides from Xenorhabdus and Photorhabdus
Investigation and optimization of biosynthetic pathways from entomopathogenic bacteria
Identification of new natural products from nematode-associated bacteria using mass spectrometry
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