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, James H. Park is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
2021 |
Park, James H |
K22Activity Code Description: To provide support to outstanding newly trained basic or clinical investigators to develop their independent research skills through a two phase program; an initial period involving and intramural appointment at the NIH and a final period of support at an extramural institution. The award is intended to facilitate the establishment of a record of independent research by the investigator in order to sustain or promote a successful research career. |
Defining Structural and Genetic Requisites of Glutamylation in Polarized Cells @ Veterans Biomedical Research Institute
PROJECT SUMMARY Through mass spectrometry, glutamylation is becoming recognized as an important post-translational modifi- cation (PTM) in polarized neuronal cells such as the retinal photoreceptor and hippocampal pyramidal cells. Despite this greater awareness of glutamylation, there exist gaps in our understanding of (1) how glutamyla- tion specifically occurs in the photoreceptor, (2) which specific glutamylase(s) are necessary for hippocampal development, and (3) how a neurodegenerative state affects glutamylation levels. In addressing those gaps, the long-term goal is to understand how glutamylation annotates the cytoskeleton for specialized roles. The central hypothesis is that the homeostasis of glutamylation, the most abundant post-translational modification in the nervous system, is essential to neuronal and retinal health and that aberrant glutamylation levels may serve as an adjunctive biomarker. The central hypothesis will be challenged by three specific aims: (1) gain a structural understanding of how a glutamylase, Tubulin Tyrosine Ligase-Like 5 (TTLL5) recognizes a novel non-tubulin target (RPGR-ORF15, the most commonly mutated gene in retinitis pigmentosa (RP)) in the reti- nal photoreceptor and assess how point mutations informed by the structural complex impacts in oculo RPGR-ORF15 glutamylation and opsin trafficking. (2) Identify which of the nine glutamylases are necessary for hippocampal pyramidal cytoskeleton development, function, and maintenance and to determine which glu- tamylase(s) could be perturbed in a neurodegenerative state like Alzheimer's disease (AD), and (3) examine how glutamylation levels are affected in neurodegenerative samples. This juxtaposition of RP and AD high- lights the fundamental role glutamylation plays in maintaining cytoskeletal structure and functions across var- ied polarized cell types such as photoreceptors and hippocampal neurons. The proposed research is signifi- cant because defining the structural requirements of glutamylation in the photoreceptor will have relevance to basic photoreceptor biology and help RP patients who carry mutations in TTLL5's Cofactor Interaction Do- main (CID) or RPGR-ORF15's Basic Domain (BD) identified by Next Generation Sequencing (NGS). Be- cause rational therapeutics is structure dependent, a structure of the CID-BD is needed especially since we currently possess no homology models for CID. More broadly, a structural understanding of how a glutamyl- ase recognizes a non-tubulin retinal target will lay the groundwork to understand how TTLL paracatalytic re- gions functions as recognition adaptors for substrate targets. This will emerge as a unifying theme for the TTLL superfamily as the family is further explored and implicated as an etiology of disease by NGS. Likewise, defining the genetic requirements of glutamylation in the hippocampal cells will broaden our understanding of which glutamylases play a role in the development and maintenance of the hippocampal cytoskeleton. This expanded understanding will lay the foundation to assess glutamylation as a diagnostic biomarker to detect neurodegeneration in CSF and brain tissue.
|
0.895 |