Posttranslational modifications of fibromodulin.
نویسندگان
چکیده
منابع مشابه
SnapShot: p53 Posttranslational Modifications
P ho sp ho ry la ti o n N-Terminal: S6, S9, S15, T18, S20 ATM, DNAPK, • CK1 ERKs, ATR, p38 • kinase, mTOR, Chk1/Chk2, JNK, MAPKAP2, Hipk4 Activated by DNA damage, UV light, ionizing radiation, replicative senes• cence, or phosphatidylcholines. N-terminal phosphorylation causes p53 stabilization by inhibiting the p53• MDM2 interaction. Knockin mice carrying separate analogs to human Ser18/ • Ser...
متن کاملPosttranslational modifications of tissue factor.
Tissue factor (TF), a membrane protein, is an initiator of blood coagulation in vivo. In this review we discuss how posttranslational modifications affect activity and other properties of TF. Glycosylation of the extracellular domain and the composition of carbohydrates at three glycosylation sites have an influence on TF activity in the extrinsic FXase by increasing the rate of FX proteolysis....
متن کاملTopical Review on Posttranslational Modifications in Chloroplasts Posttranslational Modifications of Chloroplast Proteins: An Emerging Field
Posttranslational modifications of proteins are key effectors of enzyme activity, protein interactions, targeting, and turnover rate, but despite their importance, they are still poorly understood in plants. Although numerous reports have revealed the regulatory role of protein phosphorylation in photosynthesis, various other protein modifications have been identified in chloroplasts only recen...
متن کاملPosttranslational modifications in innate immunity.
Taking into account that a large number of nascent gene translation products are subject to limited proteolytic processing, proteolysis is one of the most common PTMs and due to its irreversible nature needs to be very precisely controlled on multiple levels. Since PTMs play a key role in fundamental cellular processes, including the immune response, it is no surprise that these reactions are t...
متن کاملDynamics of Posttranslational Modifications of p53
The latest experimental evidence indicates that acetylation of p53 at K164 (lysine 164) and K120 may induce directly cell apoptosis under severe DNA damage. However, previous cell apoptosis models only studied the effects of active and/or inactive p53, that is, phosphorylation/dephosphorylation of p53. In the present paper, based partly on Geva-Zatorsky et al. (2006) and Batchelor et al. (2008)...
متن کاملذخیره 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: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)55381-3