Výsledky vyhledávání - "Janschitz, Marion"

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Additional file 4: of Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages

Autor: Janschitz, Marion, Romanov, Natalie, Varnavides, Gina, Hollenstein, David, GĂŠrecovĂĄ, Gabriela, Ammerer, Gustav, Hartl, Markus, Reiter, Wolfgang

Figure S4. Related to Fig. 3. (A) to (C) Annotated MS2 Spectra and transition product peak pattern indicative for Orm2 Thr18 (A), Kic1 Thr625 (B) and Kic1 Tyr634 (C). Note: Transition product peaks of Orm2 Thr18 are well separated from peaks of pepti

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Additional file 3: of Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages

Autor: Janschitz, Marion, Romanov, Natalie, Varnavides, Gina, Hollenstein, David, Gérecová, Gabriela, Ammerer, Gustav, Hartl, Markus, Reiter, Wolfgang

Figure S3. Related to Fig. 3. (A) Gel mobility shift assays performed on newly MQ-identified putative Hog1-targets coupled to HKMT-myc (Kic1, Vps53, Orm2) upon 0, 5, 30 and 45 min of osmostress (+ 0.5 M NaCl). Arrows indicate bands with altered gel m

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Additional file 2: of Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages

Autor: Janschitz, Marion, Romanov, Natalie, Varnavides, Gina, Hollenstein, David, Gérecová, Gabriela, Ammerer, Gustav, Hartl, Markus, Reiter, Wolfgang

Figure S2. Related to Fig. 3. (A) Heatmap showing SILAC ratios of Hog1-dependent (Romanov et al., 2017 [4] and MQ-derived) phosphopeptides at 0, 5, 15 and 30 min after treatment with 0.5 M NaCl of a wild type (left) or hog1Δ (right) strain. (B) Simi

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Additional file 1: of Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages

Autor: Janschitz, Marion, Romanov, Natalie, Varnavides, Gina, Hollenstein, David, Gérecová, Gabriela, Ammerer, Gustav, Hartl, Markus, Reiter, Wolfgang

Figure S1. Related to Fig. 1. (A) Experimental workflow for LC-MS shotgun experiments. SILAC: stable isotope labeling with amino acids in cell culture, MS: mass spectrometry, TiO2: titanium dioxide, SCX: strong cation exchange. (B-D) Histograms of MS

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Additional file 5: of Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages

Autor: Janschitz, Marion, Romanov, Natalie, Varnavides, Gina, Hollenstein, David, Gérecová, Gabriela, Ammerer, Gustav, Hartl, Markus, Reiter, Wolfgang

Figure S5. Related to Fig. 3. Scanned Western blot films showing M-track protein protein proximity results for the individual candidates. (A) Signals obtained from hyperosmotically challenged cells are shown (1 M Sorbitol, 40 min). Areas picked for d

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Novel interconnections of HOG signaling revealed by combined use of two proteomic software packages

Autor: Janschitz, Marion, Romanov, Natalie, Varnavides, Gina, Hollenstein, David Maria, Gérecová, Gabriela, Ammerer, Gustav, Hartl, Markus, Reiter, Wolfgang

Publikováno v: Cell Communication and Signaling : CCS
Cell Communication and Signaling, Vol 17, Iss 1, Pp 1-17 (2019)

Modern quantitative mass spectrometry (MS)-based proteomics enables researchers to unravel signaling networks by monitoring proteome-wide cellular responses to different stimuli. MS-based analysis of signaling systems usually requires an integration

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https://pubmed.ncbi.nlm.nih.gov/31208443

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Dissecting kinase networks in the hyperosmotic stress response in yeast using quantitative mass spectrometry-based and bioinformatical approaches

Autor: Janschitz, Marion Franziska

Zellen verarbeiten Stresssignale ihrer Umwelt mit intrazellulären Signalübertragungsystemen, die oft post-translationelle Modifizierungen beinhalten. Der „High osmolarity glycerol“- Signaltransduktionsweg (HOG-pathway) in Saccharomyces cerevisi

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