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Specificity of small molecule inhibitors for deubiquitinating enzymes in living cells assessed by activity-based proteomics
*Mikael Altun, *Holger B. Kramer, *Lianne Willems, *Mukram Mackeen, *Edward Kogan, *Rebecca Konietzny, *Cynthia Wright, *Roman Fischer, #Benjamin Nicholson, *Benedikt M. Kessler. *Henry Wellcome Building for Molecular Physiology, Nuffield Department of Clinical Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK, #Progenra Inc, Malvern, PA 19355, USA
Small molecular compounds (PR-619 and P22077) was assessed for their abilities to inhibit DUB function in crude extracts and in cells. Activity-based profiling combined with quantitative mass spectrometry revealed the inhibitory capacity of a broad range of DUBs by the PR-619, whereas P22077 showed specificity towards subsets of DUBs including USP7 in cells. Our results demonstrate the usefulness of activity-based quantitative proteomics to monitor inhibition of endogenous DUBs in vivo.
Capture Compounds towards a targeted reduction of proteome complexity
Erik Duelsner, Aysel Alici, Christian Jurinke, Hubert Koester. caprotec bioanalytics GmbH
Capture Compound Mass Spectrometry (CCMS) enables the enrichment of proteins based on their functionality. CCMS is commercialized as kits for research applications and in collaborations with pharmaceutical companies. The focus is on investigating mechanisms of drug action and avoidance of toxic effects of small molecule drugs.
Quantitative phosphoproteome analysis for the detection of early alterations of signal transduction by dioxin (TCDD)
Melanie Schulz, Ulrich Andrae, Martin R. Larsen. Helmholtz Zentrum München, University of Southern Denmark
2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) is an extremely toxic pollutant and regarded the most potent chemical carcinogen in experimental animals. Most of its biological effects are mediated by binding of TCDD to the cytosolic Ah receptor (AHR). In addition, TCDD cause AHR-dependent alterations in signal transduction that are independent of changes in gene expression. In this study, we have therefore conducted a quantitative phospho proteomic study on TCDD-induced alterations.
Sialylation and Metastasis: from tumor-associated antigens discovery to therapeutic development
Giuseppe Palmisano, Rikke Leth-Larsen and Martin R. Larsen. University of Southern Denmark, Odense, Denmark; Department of Cancer and Inflammation Research, Institute of Molecular Medicine, University of Southern Denmark
Aberrant sialylation affects the metastatic behaviour of cancer cells.We have quantified the sialylated cell surface glycoproteins from cells with different metastatic behaviour.The membrane proteins from isogenic human cell lines were analyzed by a method based on TiO2-HILIC-MS.1200 sialylated glycosites, 116 enzymes involved in the glycoconjugate metabolism and for the first time 4 glycosylation sites of Her2 receptor were identified, showing the importance of this tool for discovery and thera
Proteomic non-small cell lung carcinoma biomarker screening in bronchoalveolar lavage fluid
Tonio Oumeraci 1, Bernd Schmidt 3, Thomas Wolf 1,4, Marc Zapatka 4, Andreas Pich 2, Benedikt Brors 4, Roland Eils 4,5, Brigitte Schlegelberger 1, Nils von Neuhoff 1. 1 Institute of Cell and Molecular Pathology - 2 Department of Toxicology, Hannover Medical School MHH 3 Respiratory Medicine Department of Internal Medicine I, University Hospital Halle, Halle (Saale)
Using a standardized method to acquire MALDI-TOF proteome profile spectra of bronchoalveolar lavage fluid (BALF), we have shown the upregulation of histatin 3 and calgranulin C in a small pilot cohort of NSCLC patients. This pilot study serves to demonstrate that it is feasible to screen a larger NSCLC patient cohort for BALF proteome level biomarkers in a clinical setting.
Hepatitis B virus (HBV) and Human immunodeficiency virus (HIV) antibodies detected by peptide microarrays
ahmed Abd El Wahed1, Ulrike Beutling2, Ronald Frank2, Gerhard Hunsmann1, and Hans-Joachim Fritz3 . 1) Institute of Virology, Universitätsmedizin Göttingen, Georg August University Göttingen, Kreuzbergring 57, D-37075 Göttingen, Germany, 2) Department of Chemical Biology, Helmholtz Centre for Infect
HBV and HIVenv chips with overlapping oligopeptides encompassing the full amino acid sequences of HBV and HIV polypeptides were produced. In addition, a chip displaying a library of random 4608 different 15-mers peptides (4608-RPL) was prepared. Both chips were used for analyzing monoclonal antibodies and sera from HIV- and HBV-infected individuals. Moreover, 4608-RPL could be used for identifying target sequences of antibodies without prior knowledge of the corresponding immunizing antigen.
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