Differential S-nitrosylation of proteins in Alzheimer's disease.
Zahid S, Khan R, Oellerich M, Ahmed N, Asif AR.SourceNeurochemistry Research Laboratory, Department of Biochemistry, University of Karachi, Karachi 75270, Pakistan; Department of Clinical Chemistry, University Medical Center Goettingen, Robert-Koch-Str. 40, 37075 Goettingen, Germany.
Neuroscience.Neuroscience.2013 Oct 22. pii: S0306-4522(13)00879-8. doi: 10.1016/j.neuroscience.2013.10.026. [Epub ahead of print]
Numerous studies have provided evidence regarding the involvement of protein S-nitrosylation in the progression of Alzheimer's disease (AD) pathology and its implication in the formation and accumulation of misfolded protein aggregates. The identification of S-nitrosylated proteins can be a major st
Rv2140c is one of many conserved Mycobacterium tuberculosis proteins for which no molecular function has been identified. We have determined a high-resolution crystal structure of the Rv2140c gene product, which reveals a dimeric complex that shares strong structural homology with the phosphatidylet
[Roles of phosphatidylethanolamine-binding protein in cell signaling and its biological functions].
Bian JM, Wu N, Li J.SourceDepartment of Pharmacology, Military General Hospital of Beijing PLA, Beijing 100700, China.
Sheng li xue bao : [Acta physiologica Sinica].Sheng Li Xue Bao.2013 Apr 25;65(2):237-43.
Phosphatidylethanolamine-binding protein (PEBP) is a cytoplasm soluble protein with a high conserved structure. It has been approved recently that PEBP is a multifunctional molecule regulating several important cellular signal pathways, including ERK cascade, NF-κB pathway, and signaling of G prote