{"title":"Novel product development and future directions in support of proteomics standardization, biobanking, and binder validation using CRISPR knockout technology","authors":"Kevin Ray","doi":"10.1016/j.euprot.2015.07.007","DOIUrl":"10.1016/j.euprot.2015.07.007","url":null,"abstract":"","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Page 77"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.07.007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257324","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Peter Raus , Bharath Raghuraman Kumar , Martijn Pinkse , Peter Verhaert
{"title":"Bottom–up protein identifications from microliter quantities of individual human tear samples. Important steps towards clinical relevance.","authors":"Peter Raus , Bharath Raghuraman Kumar , Martijn Pinkse , Peter Verhaert","doi":"10.1016/j.euprot.2015.06.005","DOIUrl":"10.1016/j.euprot.2015.06.005","url":null,"abstract":"<div><p>A relatively simple combination of Schirmer strip sampling with straightforward sensitive nanoLC quadrupole-Orbitrap tandem mass spectrometry after a minimum of sample processing steps allows for replicate proteomic analysis of single human tears, i.e., without the requirement for sample pooling. This opens the way to clinical applications of the analytical workflow, e.g., to monitor disease progression or treatment efficacy within individual patients. Proof of concept is provided by triplicate analyses of a singular sampling of tears of a dry eye patient, before and one and two months after minor salivary gland transplantation. To facilitate comparison with the outcome of previously reported analytical protocols, we also include the data from a typical healthy young adult tear sample as obtained by our streamlined method.</p><p>With 375 confidently identified proteins in the healthy adult tear, the obtained results are comprehensive and in large agreement with previously published observations on pooled samples of multiple patients. We conclude that, to a limited extent, bottom–up tear protein identifications from individual patients may have clinical relevance.</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 8-13"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.06.005","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257197","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
D. Baiwir , G. Mazzucchelli , N. Smargiasso , F. Quesada-Calvo , E. De Pauw , M. Malaise , E. Louis , M.-A. Meuwis
{"title":"Comparison of serum fractionation methods by data independent label-free proteomics","authors":"D. Baiwir , G. Mazzucchelli , N. Smargiasso , F. Quesada-Calvo , E. De Pauw , M. Malaise , E. Louis , M.-A. Meuwis","doi":"10.1016/j.euprot.2015.07.009","DOIUrl":"10.1016/j.euprot.2015.07.009","url":null,"abstract":"<div><p>Off-line sample prefractionations applied prior to biomarker discovery proteomics are options to enable more protein identifications and detect low-abundance proteins. This work compared five commercial methods efficiency to raw serum analysis using label-free proteomics. The variability of the protein quantities determined for each process was similar to the unprefractionated serum. A 49% increase in protein identifications and 12.2% of reliable quantification were obtained. A 61 times lower limit of protein quantitation was reached compared to protein concentrations observed in raw serum. The concentrations of detected proteins were confronted to estimated reference values.</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 14-22"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.07.009","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257396","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Analysis of the surface, secreted, and intracellular proteome of Propionibacterium acnes","authors":"Yang Yu , Jackson Champer , Jenny Kim","doi":"10.1016/j.euprot.2015.06.003","DOIUrl":"10.1016/j.euprot.2015.06.003","url":null,"abstract":"<div><p><em>Propionibacterium acnes</em>, plays an important role in acne vulgaris and other diseases. However, understanding of the exact mechanisms of <em>P. acnes</em> pathogenesis is limited. Few studies have investigated its proteome, which is essential for vaccine development. Here, we comprehensively investigate the proteome of <em>P. acnes</em> strain ATCC 6919, including secreted, cell wall, membrane, and cytosolic fractions in three types of growth media. A total of 531 proteins were quantified using an Orbitrap mass spectrometer and bioinformatically categorized for localization and function. Several, including PPA1939, a highly expressed surface and secreted protein, were identified as potential vaccine candidates.</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 1-7"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.06.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257169","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Branka Radic-Sarikas , Uwe Rix , Alexey Stukalov , Manuela Gridling , André C. Müller , Jacques Colinge , Giulio Superti-Furga , Keiryn L. Bennett
{"title":"Enhancing cognate target elution efficiency in gel-free chemical proteomics","authors":"Branka Radic-Sarikas , Uwe Rix , Alexey Stukalov , Manuela Gridling , André C. Müller , Jacques Colinge , Giulio Superti-Furga , Keiryn L. Bennett","doi":"10.1016/j.euprot.2015.09.002","DOIUrl":"10.1016/j.euprot.2015.09.002","url":null,"abstract":"<div><p>Gel-free liquid chromatography mass spectrometry coupled to chemical proteomics is a powerful approach for characterizing cellular target profiles of small molecules. We have previously described a fast and efficient elution protocol; however, altered target profiles were observed. We hypothesised that elution conditions critically impact the effectiveness of disrupting drug-protein interactions. Thus, a number of elution conditions were systematically assessed with the aim of improving the recovery of all classes of proteins whilst maintaining compatibility with immunoblotting procedures. A double elution with formic acid combined with urea emerged as the most efficient and generically applicable elution method for chemical proteomics</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 43-53"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.09.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257653","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Gregory W. Watson , Samanthi Wickramasekara , Claudia S. Maier , David E. Williams , Roderick H. Dashwood , Emily Ho
{"title":"Assessment of global proteome in LNCaP cells by 2D-RP/RP LC–MS/MS following sulforaphane exposure","authors":"Gregory W. Watson , Samanthi Wickramasekara , Claudia S. Maier , David E. Williams , Roderick H. Dashwood , Emily Ho","doi":"10.1016/j.euprot.2015.08.002","DOIUrl":"10.1016/j.euprot.2015.08.002","url":null,"abstract":"<div><p>The phytochemical sulforaphane can induce cell cycle arrest and apoptosis in metastatic prostate cancer cells, though the mechanism of action is not fully known. We conducted a global proteome analysis in LNCaP metastatic prostate cancer cells to characterize how global protein signature responds to sulforaphane. We conducted parallel analyses to evaluate semi-quantitative 1-dimensional versus 2-dimensional liquid chromatography tandem mass spectrometry (LC–MS/MS) and their utility in characterizing whole cell lysate. We show that 2-dimensional LC–MS/MS can be a useful tool for characterizing global protein profiles and identify TRIAP1 as a novel regulator of cell proliferation in LNCaP metastatic prostate cancer cells.</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 34-40"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.08.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257500","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Irina Boggs , Brad Hine , Grant Smolenski , Kasper Hettinga , Lina Zhang , Thomas T. Wheeler
{"title":"Changes in the repertoire of bovine milk proteins during mammary involution","authors":"Irina Boggs , Brad Hine , Grant Smolenski , Kasper Hettinga , Lina Zhang , Thomas T. Wheeler","doi":"10.1016/j.euprot.2015.09.001","DOIUrl":"10.1016/j.euprot.2015.09.001","url":null,"abstract":"<div><p>Changes of abundance that occur in the repertoire of low abundance milk proteins after cessation of milk removal have not been characterised. Skimmed milk and whey from cows sampled at day 0 and either day 3 or day 8 after drying off were subjected to three untargeted proteomics techniques; 2-D gel electrophoresis, GeLC-MS, and dimethyl isotopic labelling of tryptic peptides. The changes observed included 45 fragments of abundant milk proteins and 36 host-defence proteins, suggesting activation of proteolysis and inflammation. The findings form a basis for adding value to dairy production.</p></div>","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 65-75"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.09.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257527","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The EuPA Company Club: Emphasis on the synergy with EuPA’s Initiatives beyond education—Towards further integration with EuPA’s goals and objectives","authors":"Andrea Urbani, Andrey Lisitsa, Peter Verhaert","doi":"10.1016/j.euprot.2015.06.007","DOIUrl":"10.1016/j.euprot.2015.06.007","url":null,"abstract":"","PeriodicalId":38260,"journal":{"name":"EuPA Open Proteomics","volume":"9 ","pages":"Pages 41-42"},"PeriodicalIF":0.0,"publicationDate":"2015-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.euprot.2015.06.007","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"54257218","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}