Publications by authors named "Marion Herrmann"

Metabolites and lipids are the final products of enzymatic processes, distinguishing the different cellular functions and activities of single cells or whole tissues. Understanding these cellular functions within a well-established model system requires a systemic collection of molecular and physiological information. In the current report, the green alga Chlamydomonas reinhardtii was selected to establish a comprehensive workflow for the detailed multi-omics analysis of a synchronously growing cell culture system.

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Purpose: The majority of gastric cancers are diagnosed at advanced stages, characterized by robust therapy resistance. The oncoprotein hypoxia-inducible factor 1 (HIF-1) is associated with therapy resistance, partly via activation of the DNA damage response. We have noted a robust ability of gastric cancer cells to functionally compensate the loss of HIF-1 in vitro.

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In recent years proteomics became increasingly important to functional genomics. Although a large amount of data is generated by high throughput large-scale techniques, a connection of these mostly heterogeneous data from different analytical platforms and of different experiments is limited. Data mining procedures and algorithms are often insufficient to extract meaningful results from large datasets and therefore limit the exploitation of the generated biological information.

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Large numbers of protein expression changes are usually observed in mouse models for neurodegenerative diseases, even when only a single gene was mutated in each case. To study the effect of gene dose alterations on the cellular proteome, we carried out a proteomic investigation on murine embryonic stem cells that either overexpressed individual genes or displayed aneuploidy over a genomic region encompassing 14 genes. The number of variant proteins detected per cell line ranged between 70 and 110, and did not correlate with the number of modified genes.

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The availability of easy-to-handle, sensitive, and cost-effective protein staining protocols for 2-DE, in conjunction with a high compatibility for subsequent MS analysis, is still a prerequisite for successful proteome research. In this article we describe a quick and easy-to-use methodological protocol based on sensitive, homogeneous, and MS-compatible silver nitrate protein staining, in combination with an in-gel digestion, employing the Millipore 96-well ZipPlate system for peptide preparation. The improved quality and MS compatibility of the generated protein digests, as compared to the otherwise weakly MS-compatible silver nitrate staining, were evaluated on real tissue samples by analyzing 192 Coomassie-stained protein spots against their counterparts from a silver-stained 2-DE gel.

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In the present work the complexity in the 2D-gel protein pattern of murin lenticular alphaA-Crystallin was analyzed. An in depth study of the different protein isoforms was done combining different proteomic tools. Lens proteins of four different ages, from embryo to 100-week-old mice, were separated by large 2D-PAGE, revealing an increase in the number and intensity of the spots of alphaA-Crystallin during the process of aging.

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The present study shows that on average, exposure to a 15 min, 5 kHz tone modulated sinusoidally in amplitude at 16 Hz with a 100% depth does not affect significantly amplitude modulation (AM) detection thresholds measured between 4 and 64 Hz when listeners are extensively trained to the AM detection task, with and without adaptor before data collection. These results are compatible with previous work given that a clear 6-dB adaptation effect was observed during the first pilot trials. However, the results reveal that adaptation effects are not robust, and suggest that the mechanisms underlying adaptation to AM must be reevaluated.

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Posttranslational modifications are of great interest because of their relevance in biological systems as proteins are commonly activated or deactivated by phosphorylation, glycation and acetylation [1, 2]. During eye lens aging the number of the alphaA-crystallin isoproteins increases. This could be observed by the use of 2D-PAGE (two-dimensional gel electrophoresis).

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Article Synopsis
  • The study analyzed the mouse brain proteome, revealing 8,767 proteins and identifying 1,324 polymorphic proteins through advanced techniques like two-dimensional electrophoresis and mass spectrometry.
  • 665 of these proteins were genetically mapped, highlighting that many variations in proteins are due to changes in their conformation and mass.
  • The findings suggest that some proteins may act as polygenic traits, with implications for understanding the genetic factors relevant to diseases.
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