Area:
Molecular Biology, Oncology
We are testing a new system for linking grants to scientists.
The funding information displayed below comes from the
NIH Research Portfolio Online Reporting Tools and the
NSF Award Database.
The grant data on this page is limited to grants awarded in the United States and is thus partial. It can nonetheless be used to understand how funding patterns influence mentorship networks and vice-versa, which has deep implications on how research is done.
You can help! If you notice any innacuracies, please
sign in and mark grants as correct or incorrect matches.
Sign in to see low-probability grants and correct any errors in linkage between grants and researchers.
High-probability grants
According to our matching algorithm, Igor Vivanco is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
2002 — 2004 |
Vivanco, Igor |
F31Activity Code Description: To provide predoctoral individuals with supervised research training in specified health and health-related areas leading toward the research degree (e.g., Ph.D.). |
Molecular Mechanisms of Pi3k-Induced Transformation @ University of California Los Angeles
DESCRIPTION (provided by applicant): Deregulation of signal transduction pathways downstream of receptor tyrosine kinases has been extensively documented in human cancers. The pathway activated phosphotidyl inositol 3-kinase is one that has gain much interest in recent years as a major contributor of tumorigenesis. The biological activity of PI3K is mainly dependent on its ability to phosphorylate the phospholipid PIP2, which results in the generation of the second messenger PIP3. PIP3 can activate a myriad of effectors by serving as a membrane anchor for pleckstrinhomology (PH) domain-containing proteins. The tumor suppressor PTEN, which encodes a dual-specificity phosphatase can oppose PI3K activity by dephosphorylating PIP3 and converting it back to PIP2. It is currently believed that PTEN's tumor suppressing properties are dependent upon this activity. Akt is a serine/threonine kinase that contains a PH domain and is activated by PI3K. It is believed to be a key mediator of PI3K function since it is able to inhibit apoptosis, promote cell growth, and cell proliferation. However, PI3K and Akt loss-of function phenotypes in animal models are not entirely overlapping, suggesting that other PI3K dependent signals are independent of Akt and may be important in PI3K-dependent transformation. We have found that the MAPK JNK, which is known to be involved in apoptosis, differentiation and transformation, can be activated by PTEN loss. Previous studies have demonstrated that JNK is necessary for Bcr-Abl-mediated transformation, and JNK deficient mice are defective in TPA-induced tumorigenesis. Here, we propose to study the role of JNK signaling in tumorigenesis induced by PTEN loss and the mechanistic details of JNK activation in PTEN-deficient cells.
|
1 |