LIVIVO - Search results -

Search results

Result 1 - 10 of total 16

Search options

Article ; Online: Promiscuous Installation of d-Amino Acids in Gene-Encoded Peptides.

Korneli, Madlen / Fuchs, Sebastian W / Felder, Katja / Ernst, Chantal / Zinsli, Léa V / Piel, Jörn

ACS synthetic biology

2021 Volume 10, Issue 2, Page(s) 236–242

Abstract: d-Amino acids can have major effects on the structure, proteolytic stability, and bioactivity of peptides. Proteusin ... ...

Abstract	d-Amino acids can have major effects on the structure, proteolytic stability, and bioactivity of peptides. Proteusin radical
MeSH term(s)	Amino Acids/metabolism ; Amyloid beta-Peptides/biosynthesis ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Antimicrobial Cationic Peptides/biosynthesis ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/genetics ; Cyanobacteria/enzymology ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Escherichia coli Proteins/metabolism ; Metabolic Engineering/methods ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Racemases and Epimerases/metabolism ; Ribosomes/metabolism ; S-Adenosylmethionine/metabolism
Chemical Substances	Amino Acids ; Amyloid beta-Peptides ; Antimicrobial Cationic Peptides ; Escherichia coli Proteins ; protegrin-1 ; S-Adenosylmethionine (7LP2MPO46S) ; Racemases and Epimerases (EC 5.1.-)
Language	English
Publishing date	2021-01-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2161-5063
ISSN (online)	2161-5063
DOI	10.1021/acssynbio.0c00470
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Fabclavine diversity in

Wenski, Sebastian L / Cimen, Harun / Berghaus, Natalie / Fuchs, Sebastian W / Hazir, Selcuk / Bode, Helge B

Beilstein journal of organic chemistry

2020 Volume 16, Page(s) 956–965

Abstract: The global threat of multiresistant pathogens has to be answered by the development of novel antibiotics. Established antibiotic applications are often based on so-called secondary or specialized metabolites (SMs), identified in large screening ... ...

Abstract	The global threat of multiresistant pathogens has to be answered by the development of novel antibiotics. Established antibiotic applications are often based on so-called secondary or specialized metabolites (SMs), identified in large screening approaches. To continue this successful strategy, new sources for bioactive compounds are required, such as the bacterial genera
Language	English
Publishing date	2020-05-07
Publishing country	Germany
Document type	Journal Article
ZDB-ID	2192461-2
ISSN	1860-5397
ISSN	1860-5397
DOI	10.3762/bjoc.16.84
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Bispecific Antibody Detection Using Antigen-Conjugated Synthetic Nucleic Acid Strands.

Mariottini, Davide / Bracaglia, Sara / Barbero, Luca / Fuchs, Sebastian W / Saal, Christoph / Moniot, Sebastien / Knuehl, Christine / Baranda, Lorena / Ranallo, Simona / Ricci, Francesco

ACS sensors

2023 Volume 8, Issue 11, Page(s) 4014–4019

Abstract: We report here the development of two different sensing strategies based on the use of antigen-conjugated nucleic acid strands for the detection of a bispecific antibody against the tumor-related proteins Mucin1 and epidermal growth factor receptor. Both ...

Abstract	We report here the development of two different sensing strategies based on the use of antigen-conjugated nucleic acid strands for the detection of a bispecific antibody against the tumor-related proteins Mucin1 and epidermal growth factor receptor. Both approaches work well in serum samples (nanomolar sensitivity), show high specificity against the two monospecific antibodies, and are rapid. The results presented here demonstrate the versatility of DNA-based platforms for the detection of bispecific antibodies and could represent a versatile alternative to other more reagent-intensive and time-consuming analytical approaches.
MeSH term(s)	Antibodies, Bispecific/metabolism
Chemical Substances	Antibodies, Bispecific
Language	English
Publishing date	2023-10-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2379-3694
ISSN (online)	2379-3694
DOI	10.1021/acssensors.3c01717
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Initiation of the flexirubin biosynthesis in Chitinophaga pinensis.

Schöner, Tim A / Fuchs, Sebastian W / Schönau, Christian / Bode, Helge B

Microbial biotechnology

2014 Volume 7, Issue 3, Page(s) 232–241

Abstract: Bacteria from the Bacteroidetes phylum are known producers of the chemotaxonomic relevant flexirubins. These orange pigments comprise a non-isoprenoid aryl-polyene carboxylic acid esterified with a dialkylresorcinol. Herein, we report a gene cluster from ...

Abstract	Bacteria from the Bacteroidetes phylum are known producers of the chemotaxonomic relevant flexirubins. These orange pigments comprise a non-isoprenoid aryl-polyene carboxylic acid esterified with a dialkylresorcinol. Herein, we report a gene cluster from Chitinophaga pinensis encoding the biosynthesis of the polyene moiety and the biochemical characterization of a tyrosine ammonia-lyase and a 4-coumarate-CoA ligase responsible for the initiation of the polyene biosynthesis. Additionally, the flexirubin of C. pinensis was characterized by a combination of feeding experiments, high-performance liquid chromatography tandem mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry.
MeSH term(s)	Ammonia-Lyases/genetics ; Ammonia-Lyases/metabolism ; Bacteroidetes/genetics ; Bacteroidetes/metabolism ; Biosynthetic Pathways/genetics ; Chromatography, High Pressure Liquid ; Coenzyme A Ligases/genetics ; Coenzyme A Ligases/metabolism ; Multigene Family ; Polyenes/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Tandem Mass Spectrometry
Chemical Substances	Polyenes ; flexirubins (54363-90-5) ; Ammonia-Lyases (EC 4.3.1.-) ; L-tyrosine ammonia-lyase (EC 4.3.1.-) ; Coenzyme A Ligases (EC 6.2.1.-) ; 4-coumarate-CoA ligase (EC 6.2.1.12)
Language	English
Publishing date	2014-01-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2406063-X
ISSN	1751-7915 ; 1751-7907
ISSN (online)	1751-7915
ISSN	1751-7907
DOI	10.1111/1751-7915.12110
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Low-molecular-weight metabolites secreted by Paenibacillus larvae as potential virulence factors of American foulbrood.

Schild, Hedwig-Annabell / Fuchs, Sebastian W / Bode, Helge B / Grünewald, Bernd

Applied and environmental microbiology

2014 Volume 80, Issue 8, Page(s) 2484–2492

Abstract: The spore-forming bacterium Paenibacillus larvae causes a severe and highly infective bee disease, American foulbrood (AFB). Despite the large economic losses induced by AFB, the virulence factors produced by P. larvae are as yet unknown. To identify ... ...

Abstract	The spore-forming bacterium Paenibacillus larvae causes a severe and highly infective bee disease, American foulbrood (AFB). Despite the large economic losses induced by AFB, the virulence factors produced by P. larvae are as yet unknown. To identify such virulence factors, we experimentally infected young, susceptible larvae of the honeybee, Apis mellifera carnica, with different P. larvae isolates. Honeybee larvae were reared in vitro in 24-well plates in the laboratory after isolation from the brood comb. We identified genotype-specific differences in the etiopathology of AFB between the tested isolates of P. larvae, which were revealed by differences in the median lethal times. Furthermore, we confirmed that extracts of P. larvae cultures contain low-molecular-weight compounds, which are toxic to honeybee larvae. Our data indicate that P. larvae secretes metabolites into the medium with a potent honeybee toxic activity pointing to a novel pathogenic factor(s) of P. larvae. Genome mining of P. larvae subsp. larvae BRL-230010 led to the identification of several biosynthesis gene clusters putatively involved in natural product biosynthesis, highlighting the potential of P. larvae to produce such compounds.
MeSH term(s)	Animals ; Bees/microbiology ; Larva/microbiology ; Molecular Weight ; Paenibacillus/metabolism ; Paenibacillus/pathogenicity ; Virulence ; Virulence Factors/metabolism
Chemical Substances	Virulence Factors
Language	English
Publishing date	2014-02-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	223011-2
ISSN	1098-5336 ; 0099-2240
ISSN (online)	1098-5336
ISSN	0099-2240
DOI	10.1128/AEM.04049-13
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 201: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Identification and biosynthesis of a novel xanthomonadin-dialkylresorcinol-hybrid from Azoarcus sp. BH72.

Schöner, Tim A / Fuchs, Sebastian W / Reinhold-Hurek, Barbara / Bode, Helge B

PloS one

2014 Volume 9, Issue 3, Page(s) e90922

Abstract: A novel xanthomonadin-dialkylresorcinol hybrid named arcuflavin was identified in Azoarcus sp. BH72 by a combination of feeding experiments, HPLC-MS and MALDI-MS and gene clusters encoding the biosynthesis of this non-isoprenoid aryl-polyene containing ... ...

Abstract	A novel xanthomonadin-dialkylresorcinol hybrid named arcuflavin was identified in Azoarcus sp. BH72 by a combination of feeding experiments, HPLC-MS and MALDI-MS and gene clusters encoding the biosynthesis of this non-isoprenoid aryl-polyene containing pigment are reported. A chorismate-utilizing enzyme from the XanB2-type producing 3- and 4-hydroxybenzoic acid and an AMP-ligase encoded by these gene clusters were characterized, that might perform the first two steps of the polyene biosynthesis. Furthermore, a detailed analysis of the already known or novel biosynthesis gene clusters involved in the biosynthesis of polyene containing pigments like arcuflavin, flexirubin and xanthomonadin revealed the presence of similar gene clusters in a wide range of bacterial taxa, suggesting that polyene and polyene-dialkylresorcinol pigments are more widespread than previously realized.
MeSH term(s)	Anisoles/chemistry ; Anisoles/metabolism ; Azoarcus/chemistry ; Azoarcus/genetics ; Azoarcus/metabolism ; Biological Products/chemistry ; Biological Products/metabolism ; Gas Chromatography-Mass Spectrometry ; Gene Order ; Genome, Bacterial ; Molecular Structure ; Multigene Family ; Pigments, Biological/genetics ; Pigments, Biological/metabolism ; Polyenes/chemistry ; Polyenes/metabolism ; Reproducibility of Results ; Resorcinols/chemistry ; Resorcinols/metabolism ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Anisoles ; Biological Products ; Pigments, Biological ; Polyenes ; Resorcinols ; xanthomonadin I
Language	English
Publishing date	2014-03-11
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0090922
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Fabclavines: bioactive peptide-polyketide-polyamino hybrids from Xenorhabdus.

Fuchs, Sebastian W / Grundmann, Florian / Kurz, Michael / Kaiser, Marcel / Bode, Helge B

Chembiochem : a European journal of chemical biology

2014 Volume 15, Issue 4, Page(s) 512–516

Abstract: The structure of the fabclavines-unique mixtures of nonribosomally derived peptide-polyketide hybrids connected to an unusual polyamino moiety-has been solved by detailed NMR and MS methods. These compounds have been identified in two different ... ...

Abstract	The structure of the fabclavines-unique mixtures of nonribosomally derived peptide-polyketide hybrids connected to an unusual polyamino moiety-has been solved by detailed NMR and MS methods. These compounds have been identified in two different entomopathogenic Xenorhabdus strains, thereby leading also to the identification of the fabclavine biosynthesis gene cluster. Detailed analysis of these clusters and initial mutagenesis experiments allowed the prediction of a biosynthesis pathway in which the polyamino moiety is derived from an unusual type of fatty acid synthase that is normally involved in formation of polyunsaturated fatty acids. As fabclavines show broad-spectrum activity against bacteria, fungi, and other eukaryotic cells, they might act as "protection factors" against all kinds of food competitors during the complex life cycle of Xenorhabdus, its nematode host, and their insect prey.
MeSH term(s)	Biological Products/chemistry ; Biological Products/isolation & purification ; Biological Products/metabolism ; Fatty Acid Synthases/genetics ; Fatty Acid Synthases/metabolism ; Fatty Acids, Unsaturated/biosynthesis ; Fatty Acids, Unsaturated/chemistry ; Magnetic Resonance Spectroscopy ; Molecular Conformation ; Multigene Family ; Oligopeptides/biosynthesis ; Oligopeptides/chemistry ; Oligopeptides/isolation & purification ; Peptides/chemistry ; Polyamines/chemistry ; Polyamines/isolation & purification ; Polyketide Synthases/genetics ; Polyketide Synthases/metabolism ; Polyketides/chemistry ; Xenorhabdus/chemistry ; Xenorhabdus/genetics ; Xenorhabdus/metabolism
Chemical Substances	Biological Products ; Fatty Acids, Unsaturated ; Oligopeptides ; Peptides ; Polyamines ; Polyketides ; fabclavine Ia ; Polyketide Synthases (79956-01-7) ; Fatty Acid Synthases (EC 2.3.1.85)
Language	English
Publishing date	2014-03-03
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.201300802
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: A Lanthipeptide-like N-Terminal Leader Region Guides Peptide Epimerization by Radical SAM Epimerases: Implications for RiPP Evolution.

Fuchs, Sebastian W / Lackner, Gerald / Morinaka, Brandon I / Morishita, Yohei / Asai, Teigo / Riniker, Sereina / Piel, Jörn

Angewandte Chemie (International ed. in English)

2016 Volume 55, Issue 40, Page(s) 12330–12333

Abstract: Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the ... ...

Abstract	Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the prototype members polytheonamides being generated by almost 50 maturation steps, including introduction of d-residues at multiple positions by an unusual radical SAM epimerase. A region in the protein-like N-terminal leader of proteusin precursors is identified that is crucial for epimerization. It resembles a precursor motif previously shown to mediate interaction in thioether bridge-formation in class I lanthipeptide biosynthesis. Beyond this region, similarities were identified between proteusin and further RiPP families, including class I lanthipeptides. The data suggest that common leader features guide distinct maturation types and that nitrile hydratase-like enzymes are ancestors of several RiPP classes.
Language	English
Publishing date	2016--26
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2011836-3
ISSN	1521-3773 ; 1433-7851
ISSN (online)	1521-3773
ISSN	1433-7851
DOI	10.1002/anie.201602863
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

Article ; Online: Neutral loss fragmentation pattern based screening for arginine-rich natural products in Xenorhabdus and Photorhabdus.

Fuchs, Sebastian W / Sachs, Christian C / Kegler, Carsten / Nollmann, Friederike I / Karas, Michael / Bode, Helge B

Analytical chemistry

2012 Volume 84, Issue 16, Page(s) 6948–6955

Abstract: Although sharing a certain degree of structural uniformity, natural product classes exhibit variable functionalities such as different amino acid or acyl residues. During collision induced dissociation, some natural products exhibit a conserved ... ...

Abstract	Although sharing a certain degree of structural uniformity, natural product classes exhibit variable functionalities such as different amino acid or acyl residues. During collision induced dissociation, some natural products exhibit a conserved fragmentation pattern close to the precursor ion. The observed fragments result from a shared set of neutral losses, creating a unique fragmentation pattern, which can be used as a fingerprint for members of these natural product classes. The culture supernatants of 69 strains of the entomopathogenic bacteria Photorhabdus and Xenorhabdus were analyzed by MALDI-MS(2), and a database comprising MS(2) data from each strain was established. This database was scanned for concordant fragmentation patterns of different compounds using a customized software, focusing on relative mass differences of the fragment ions to their precursor ion. A novel group of related natural products comprising 25 different arginine-rich peptides from 16 different strains was identified due to its characteristic neutral loss fragmentation pattern, and the structures of eight compounds were elucidated. Two biosynthesis gene clusters encoding nonribosomal peptide synthetases were identified, emphasizing the possibility to identify a group of structurally and biosynthetically related natural products based on their neutral loss fragmentation pattern.
MeSH term(s)	Amino Acid Sequence ; Arginine/chemistry ; Biological Products/analysis ; Biological Products/chemistry ; Peptides/analysis ; Peptides/chemistry ; Photorhabdus/chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Xenorhabdus/chemistry
Chemical Substances	Biological Products ; Peptides ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2012-08-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/ac300372p
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4033: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Structure elucidation and biosynthesis of lysine-rich cyclic peptides in Xenorhabdus nematophila.

Fuchs, Sebastian W / Proschak, Anna / Jaskolla, Thorsten W / Karas, Michael / Bode, Helge B

Organic & biomolecular chemistry

2011 Volume 9, Issue 9, Page(s) 3130–3132

Abstract: Thirteen novel PAX (peptide-antimicrobial-Xenorhabdus) peptides were identified in Xenorhabdus nematophila HGB081. Their structures including the absolute configuration were elucidated using a combination of labeling experiments, detailed MS/MS ... ...

Abstract	Thirteen novel PAX (peptide-antimicrobial-Xenorhabdus) peptides were identified in Xenorhabdus nematophila HGB081. Their structures including the absolute configuration were elucidated using a combination of labeling experiments, detailed MS/MS experiments, the advanced Marfey's method, and a detailed analysis of the biosynthesis gene cluster, which was identified as well.
MeSH term(s)	Lysine/chemistry ; Molecular Structure ; Peptides, Cyclic/biosynthesis ; Peptides, Cyclic/chemistry ; Xenorhabdus/chemistry ; Xenorhabdus/metabolism
Chemical Substances	Peptides, Cyclic ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2011-05-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2097583-1
ISSN	1477-0539 ; 1477-0520
ISSN (online)	1477-0539
ISSN	1477-0520
DOI	10.1039/c1ob05097d
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

To top

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito