Bioengineered protein phosphatase 2A

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Neuronal Functions of Protein Phosphatase 2A

Reversible protein phosphorylation is a common and important form of protein posttranslational modification which determines the proteins’ activities, substrate specificity and inhibitions or degradations, depending on the specific amino acid residue, or combination of residues, being targeted. While protein phosphorylations by kinases have been well studied, the importance of protein dephospho...

متن کامل

Protein phosphatase 2A dysfunction in Alzheimer’s disease

Protein phosphatase 2A (PP2A) is a large family of enzymes that account for the majority of brain Ser/Thr phosphatase activity. While PP2A enzymes collectively modulate most cellular processes, sophisticated regulatory mechanisms are ultimately responsible for ensuring isoform-specific substrate specificity. Of particular interest to the Alzheimer's disease (AD) field, alterations in PP2A regul...

متن کامل

New pathophysiological function of protein phosphatase 2A?

In this issue of the Journal, there is an interesting study by Larsen et al., which provides evidence that in pulmonary hypoxia a new mechanism might be operational that explains the deterioration of heart function in primary pulmonary hypertension. The authors chronically exposed mice to 10% oxygen to mimic hypoxia in patients. The authors had noted in previous studies that this degree of pulm...

متن کامل

Protein phosphatase 2A is a specific protamine-kinase-inactivating phosphatase.

Purified preparations of a protamine protein kinase from bovine kidney cytosol [Damuni, Amick & Sneed (1989) J. Biol. Chem. 264, 6412-6416] were inactivated after incubation with near-homogeneous preparations of protein phosphatase 2A1 and protein phosphatase 2A2. These protein phosphatase 2A-mediated inactivations of the protamine kinase were unaffected by highly purified preparations of inhib...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Bioengineered

سال: 2013

ISSN: 2165-5979,2165-5987

DOI: 10.4161/bioe.22461