Covalent attachment of pyridoxal-phosphate derivatives to 14-3-3 proteins
نویسندگان
چکیده
منابع مشابه
The 14-3-3 proteins
So what’s so interesting about them? In 1996 14-3-3 was found to bind to a variety of oncoproteins including Raf-1, polyoma middle T, and Bcr-Abl. Since then the 14-3-3 proteins have been shown to bind to a wide variety of proteins involved in signal transduction, cell cycle and apoptosis. These proteins include Cdc25, NFAT, Bad, Cbl, A20, PI 3-kinase, IRS-1, MEKK, p130Cas, glucocorticoid recep...
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Bacterial surface proteins are key players in host-symbiont or host-pathogen interactions. How these proteins are targeted and displayed at the cell surface are challenging issues of both fundamental and clinical relevance. While surface proteins of Gram-negative bacteria are assembled in the outer membrane, Gram-positive bacteria predominantly utilize their thick cell wall as a platform to anc...
متن کامل14-3-3 proteins in apoptosis.
The once obscure members of the 14-3-3 protein family play significant roles in the determination of cell fate. By inhibiting the pro-apoptotic BAD (Bcl-2-antagonist of cell death) and the transcription factor FKHRL-1, 14-3-3 displays important anti-apoptotic characteristics. To date, five points of interaction of 14-3-3 with the apoptotic machinery have been identified. How these interactions ...
متن کاملCovalent binding of 3-pyridinealdehyde nicotinamide adenine dinucleotide and substrate to glyceraldehyde 3-phosphate dehydrogenase.
Glyceraldehyde 3-phosphate dehydrogenase (D-glyceraldehyde-3-phoshate:nicotinamide adenine dinucleotide oxidoreductase (phosphorylating), EC 1.2.1.12) forms a complex with 3-pyridinealdehyde-NAD which survives precipitation with 7% perchloric acid. The molar ratio bound 3-pyridinealdehyde-NAD to the enzyme is 2.5 to 2.9. Lactate, malate, and alcohol dehydrogenases do not form acid-precipitable ...
متن کاملPhosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from heterotrophic cells of wheat interacts with 14-3-3 proteins.
Glyceraldehyde-3-phosphate dehydrogenases catalyze key steps in energy and reducing power partitioning in cells of higher plants. Phosphorylated non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) present in heterotrophic cells of wheat (Triticum aestivum) was activated up to 3-fold by MgCl2. The effect was not observed with the non-phosphorylated enzyme found in leaves. The div...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2012
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1116592109