Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Biochemistry
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Amino Acids
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Curr Opin Plant Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: BMC Plant Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Drugs Exptl Clin Res
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (2)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- 0 (25)
- Plant Physiol. (24)
- Plant J. (20)
- Phytochemistry (19)
- Plant Cell (10)
- FEBS Lett. (9)
- J. Exp. Bot. (9)
- PLOS ONE (9)
- Planta (9)
- bioRxiv (9)
- New Phytol. (8)
- Proc. Natl. Acad. Sci. U.S.A. (8)
- Trends Plant Sci. (8)
- Front. Plant Sci. (7)
- Plant Cell Physiol. (7)
- Biol. Chem. (5)
- Curr. Opin. Plant Biol. (5)
- J. Biol. Chem. (5)
- Methods Mol. Biol. (5)
- Plant Growth Regul. (5)
- Theor. Appl. Genet. (5)
- J. Plant Physiol. (4)
- Nat. Plants (4)
- Nucleic Acids Res. (4)
- Plant Signal Behav. (4)
- Ann. Bot. (3)
- Bot. Acta (3)
- EMBO J. (3)
- Int. J. Mol. Sci. (3)
- J. Plant Growth Regul. (3)
- Nat. Commun. (3)
- Physiol. Plant. (3)
- Anal. Biochem. (2)
- Annu. Rev. Plant Biol. (2)
- BMC Plant Biol. (2)
- Biochem. Soc. Trans. (2)
- Chromatographia (2)
- Curr. Biol. (2)
- Fett/Lipid (2)
- Gene (2)
- Genetika (2)
- J. Chromatogr. A (2)
- J. Gen. Virol. (2)
- Mol. Biol. Evol. (2)
- Mol. Plant (2)
- New Biotechnol. (2)
- Plant Biol. (2)
- Plant Mol. Biol. (2)
- Plant Sci. (2)
- RNA Biol. (2)
- Science (2)
- Seed Sci. Res. (2)
- Virology (2)
- Virus Res. (2)
- eLife (2)
- ACS Chem. Biol. (1)
- Acta Biol. Szeged. (1)
- Acta Physiol. Plant. (1)
- Amino Acids (1)
- Annu. Plant Rev. (1)
- Annu. Rev. Microbiol. (1)
- Annu. Rev. Phytopathol. (1)
- AoB PLANTS (1)
- Autophagy (1)
- BBA-Mol. Cell Biol. Lipids (1)
- BIOspektrum (1)
- BMC Biol. (1)
- BMC Evol. Biol. (1)
- BMC Genomics (1)
- Bio Protoc. (1)
- BioEssays (1)
- Biocell (1)
- Biochem. J. (1)
- Biochemistry (1)
- Biochimie (1)
- Biologia (1)
- Biologie in unserer Zeit (1)
- Biology of Plant-Microbe Interactions (1)
- Biotechnol. Lett. (1)
- Braz. J. Plant Physiol. (1)
- Bull. Environ. Contam. Toxicol. (1)
- Cell (1)
- Cell Rep. (1)
- Cereal Res. Commun. (1)
- ChemBioChem (1)
- ChemRxiv (1)
- Cold Spring Harb. Perspect. Biol. (1)
- Curr. Opin. Biotech. (1)
- Cytoskeleton (1)
- Dev. Cell (1)
- Ecotoxicol. Environ. Saf. (1)
- Electron. J. Biotechnol. (1)
- Environ. Sci. Pollut. Res. (1)
- Equine Vet. Educ. (1)
- Equine Vet. J. (1)
- Eur. J. Biochem. (1)
- Eur. J. Plant Pathol. (1)
- Front Cell Dev Biol (1)
- Genome (1)
- J. Agr. Food Chem. (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Demuth, H.-U. (1)
- Gebre-Mariam, T. (1)
- Hoffmann, T. (1)
- Imming, P. (1)
- Kahsay, B. N. (1)
- Manhart, S. (1)
- Moeller, L. (1)
- Neubert, R. H. H. (1)
- Rosche, F. (1)
- Schilling, S. (1)
- Wasternack, C. (1)
- Ziegler, J. (1)
Zeige Ergebnisse 1 bis 2 von 2.
Kahsay, B. N.; Ziegler, J.; Imming, P.; Gebre-Mariam, T.; Neubert, R. H. H.; Moeller, L.; Free amino acid contents of selected Ethiopian plant and fungi species: a search for alternative natural free amino acid sources for cosmeceutical applications Amino Acids 53, 1105-1122, (2021) DOI: 10.1007/s00726-021-03008-5
Free amino acids (FAAs), the major constituents of the natural moisturizing factor (NMF), are very important for maintaining the moisture balance of human skin and their deficiency results in dry skin conditions. There is a great interest in the identification and use of nature-based sources of these molecules for such cosmeceutical applications. The objective of the present study was, therefore, to investigate the FAA contents of selected Ethiopian plant and fungi species; and select the best sources so as to use them for the stated purpose. About 59 different plant species and oyster mushroom were included in the study and the concentrations of 27 FAAs were analyzed. Each sample was collected, lyophilized, extracted using aqueous solvent, derivatized with Fluorenylmethoxycarbonyl chloride (Fmoc-Cl) prior to solid-phase extraction and quantified using Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometric (LC-ESI–MS/MS) system. All the 27 FAAs were detected in most of the samples. The dominant FAAs that are part of the NMF were found at sufficiently high concentration in the mushroom and some of the plants. This indicates that FAAs that could be included in the preparations for the management of dry skin condition can be obtained from a single natural resource and the use of these resources for the specified purpose have both economic and therapeutic advantage in addition to fulfilling customer needs.
Schilling, S.; Hoffmann, T.; Rosche, F.; Manhart, S.; Wasternack, C.; Demuth, H.-U.; Heterologous Expression and Characterization of Human Glutaminyl Cyclase: Evidence for a Disulfide Bond with Importance for Catalytic Activity Biochemistry 41, 10849-10857, (2002) DOI: 10.1021/bi0260381
Glutaminyl cyclase (QC, EC 2.3.2.5) catalyzes the formation of pyroglutamate residues from glutamine at the N-terminus of peptides and proteins. In the current study, human QC was functionally expressed in the secretory pathway of Pichia pastoris, yielding milligram quantities after purification from the supernatant of a 5 L fermentation. Initial characterization studies of the recombinant QC using MALDI-TOF mass spectrometry revealed correct proteolytic processing and N-glycosylation at both potential sites with similar 2 kDa extensions. CD spectral analysis indicated a high α-helical content, which contrasts with plant QC from Carica papaya. The kinetic parameters for conversion of H-Gln-Tyr-Ala-OH by recombinant human QC were almost identical to those previously reported for purified bovine pituitary QC. However, the results obtained for conversion of H-Gln-Gln-OH, H-Gln-NH2, and H-Gln-AMC were found to be contradictory to previous studies on human QC expressed intracellularly in E. coli. Expression of QC in E. coli showed that approximately 50% of the protein did not contain a disulfide bond that is present in the entire QC expressed in P. pastoris. Further, the enzyme was consistently inactivated by treatment with 15 mM DTT, whereas deglycosylation had no effect on enzymatic activity. Analysis of the fluorescence spectra of the native, reduced, and unfolded human QC point to a conformational change of the protein upon treatment with DTT. In terms of the different enzymatic properties, the consequences of QC expression in different environments are discussed.