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Chen M.,Beijing Institute of Radiation Medicine | Chen M.,Tianjing Institute of Hygiene and Environmental Medicine | Yang B.,Beijing Institute of Radiation Medicine | Ying W.,Beijing Institute of Radiation Medicine | And 2 more authors.
Protein and Peptide Letters | Year: 2010

A novel strategy to annotate nsSNP-peptides in human liver proteome based on LC-ESI-MS/MS and peptide database search was proposed. Totally 115 nsSNP-peptides in human liver proteins were annotated using our method. Among them, 42 peptides were found to be amino acid mutation, 73 peptides were wild type, 5 peptides were interpreted with both mutation and wild type. The function of nsSNP-peptide was predicted using SIFT algorithm, and 2 nsSNPs were predicted to be damaged for protein function. The results here show that the strategy is very effective for annotation of nsSNP at peptide level. © 2010 Bentham Science Publishers Ltd. Source

Wang X.,Tianjing Institute of Hygiene and Environmental Medicine | Wang X.,Institute of Health and Environmental Medicine | Gong J.,Tianjing Institute of Hygiene and Environmental Medicine | Gong J.,Institute of Health and Environmental Medicine | And 16 more authors.
Cell Stress and Chaperones | Year: 2010

It has been confirmed that stress plays an important role in the induction and development of cardiovascular diseases, but its mechanism and molecular basis remain unknown. In the present study, a myocardial injury model induced by restraint stress was established in rat. To screen for the related proteins involved in stress-induced myocardial injury, proteomic techniques based on 2-DE and mass spectrometry were used. In our results, ten proteins were found to be altered. The expression of eight of these proteins was increased after restraint stress, including cardiac myosin heavy chain, dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial aldehyde dehydrogenase, H+-transporting ATP synthase, albumin, and apolipoprotein A-I precursor. The expression of uncoupling protein 3 (UCP3) and mitochondrial aconitase was decreased. Most of the proteins were related to energy metabolism. Further research indicated that UCP3 may mediate the myocardial cell response induced by restraint stress. © 2010 Cell Stress Society International. Source

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