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Cover Picture: Proteomics 10'09
Publication year - 2009
Publication title -
proteomics
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200990034
Subject(s) - proteomics , period (music) , biology , physics , genetics , gene , acoustics
In this issue of Proteomics you will find the following highlighted articles: Elongating pigs: self‐stuffing sausages? Sorry, not ready for release to market yet, the recipe is still in scale‐up. The story: during development, pig embryos go through dramatic shape changes prior to implantation, beginning with 1‐2 mm spheres on day 10 of gestation, change to 6‐10 mm ovoids on day 11, then, in a 4‐hour period between days 11 and 12, to thin filaments >100 mm long (possibly enough for a British breakfast but still short for most wursts or American hot dogs). This stage is of particular interest to pig farmers and breeders because it is the period of highest fetal wastage, up to 20% losses are observed. Degrelle et al. report on the proteomic changes observed during this dramatic transition. Using 2‐DE and MALDI‐TOF or LC‐MS/MS peptide mass fingerprinting, they identified 275 proteins differing between ovoid and filamentous forms, 175 unique, 162 annotated for GO and 148 mapped into functional networks. Degrelle, S. A. et al., Proteomics 2009, 9 , 2678–2694. Itsy bitsy spider went up the water spout, ... Along came the thundershowers in California and washed him out, but not before he'd collected some nice data on the network he clung to until the shower had passed. “Got to keep my mouth shut,” he thought, “What happened to that drought?” Antonov et al. have created a publically available “spider” which has been put to work reanalyzing the connections on the almost 300 networks and lists of proteins published in this journal in the last five years. The spider is part of a more statistically robust method of creating and validating the proposed protein‐protein interaction (PPI) network. After mapping proteins onto the organismal network by expected distance apart and ontological criteria, a p ‐value can be calculated. The new method appears to be much more informative than the “active‐subnetwork” method. Antonov, A. V. et al., Proteomics 2009, 9 , 2740–2749. Yes, we have nocodazole today And how do you know we have nocodazole? Our microtubules have no motion, our phosphopeptides never go. Our cycles are arrested, so we sit with spindles frozen like up at Lake Tahoe... A number of drugs exert their power through modification of microtubules, an area Nagano et al . chose to re‐examine in this paper. They added to the value of the work by looking simultaneously at the responses of three cell lines to one drug and using the best current LC‐MS practices for identification and characterization of phosphorylation sites. They turned up >1500 sites in >700 phosphoproteins. Of particular interest was the context of the sites – phosphoserine followed by proline, or phosphoserine followed by aspartate or glutamate were the most common sequences but the frequency differed by cell line: pSerPro was highest in NCI‐H460 cells, lowest in HeLa; pSerAsp/Glu highest in HeLa, lowest in NCI‐H460. Nagano, K. et al., Proteomics 2009, 9 , 2861–2874.

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