John Choi, BS - US grants
Affiliations: | Duke University, Durham, NC |
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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.
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High-probability grants
According to our matching algorithm, John Choi is the likely recipient of the following grants.| Years | Recipients | Code | Title / Keywords | Matching score |
|---|---|---|---|---|
| 1991 — 1995 | Choi, John U | K15Activity Code Description: Undocumented code - click on the grant title for more information. |
Fructosyltransferase From Streptococcus Mutans @ University of Southern California The application is submitted under the Dentist Scientist Award program and outlines a combined curriculum leading to a PhD in Craniofacial Biology and a Certificate in the specialty of Advanced Periodontics. The course-work of the curriculum spans a five-year program with basic science courses for both the doctorate and periodontics certificate completed in the first year an Periodontics clinically-related courses and the clinical practice are spread through years 2 and 5 but are emphasized in years 4 and 5. Laboratory research is present each semester for 5 years until completion of the award program. The major thrust of the thesis research begins in year 2. The research project is a modern protein chemistry and enzymology study of the enzyme fructosyltransferase from Streptococcus mutans. Fructosyltransferases have been only moderately studied even though they are major products of two important oral bacteria, S. mutans and Actinomyces viscosus. The research proposal focuses on an approach to unambiguously identify a peptide segment that contains an active-site amino acid directly involved catalysis. The process is dependent on trapping a fructosyltransferase fructosyl-enzyme covalent complex. As part of the research, enzyme kinetic experiments will be performed to determine the relative steady-state abundance of a fructosyl-enzyme intermediate as an estimate of the anticipated yield of the trapped complex. In the process the kinetic studies will provide the first insight into the enzyme mechanism. If the enzyme behaves similar to the more thoroughly studied enzyme, levansucrase from Bacillus subtillis (which has substantial sequence homology with S. mutans fructosyl-transferase), it will be possible to trap a radiolabeled fructosyl-enzyme complex by rapidly denaturing a reaction of enzyme and radiolabeled sucrose. The covalent complex will be proteolytically digested, and a fructosyl peptide isolated and sequenced. Since the fructosyl bond will likely be very labile and cleaved during sequence analysis, the specific amino acid linked to fructose may require methods such as mass spectrometry fragmentation analysis or on-line fast-atom bombardment mass spectrometry with N- or C-terminal proteolysis. In the final phase of the research, site-directed mutagenesis will be performed on the previously cloned and sequenced ftf gene to confirm identification of the catalytic amino acid and possibly discover additional details of the reaction mechanism. |
0.928 |
| 1998 — 2002 | Choi, John K | K08Activity Code Description: To provide the opportunity for promising medical scientists with demonstrated aptitude to develop into independent investigators, or for faculty members to pursue research aspects of categorical areas applicable to the awarding unit, and aid in filling the academic faculty gap in these shortage areas within health profession's institutions of the country. |
Cmyb During Early Myelopoiesis @ University of Pennsylvania DESCRIPTION (Applicant's Description): The applicant's career goal to combine research with clinical practice of hematopathology is a logical outcome of his c o n t inued interests in carcinogenesis, cellular differentiation, and transcription factors. While he has had a productive research experience with skeletal myocytes and B cell transcription factors, this proposal represents a significant change in research subject and uses many technical approaches that are novel to him. The expression of the hematopoietic-restricted transcription factor c-myb can be disrupted using antisense oligonucleotides and this leads to cell cycle arrest or apoptosis of leukemic cells. Based on these findings, clinical trials of antisense oligonucleotide based therapy against leukemic cells are in progress. Although c-myb is a rational target, it is still less than perfect for treatment of leukemias because it is also expressed by normal hematopoietic cells and is essential for their normal development. A better fundamental understanding of c-myb biology may identify additional and possibly better targets. MYB may play a role in leukemogenesis by physically interacting with transcription co-factors and activating specific genes that promote cellular proliferation. These co-factors and c-myb activated genes are potential targets for antisense based therapies against leukemias. It is possible that some of these targets are essential for cell cycle progression in some leukemic cells but dispensable in normal hematopoietic progenitors. To test this, the expression of known c-myb activated genes and interacting proteins will be suppressed using antisense approaches and cellular proliferation of normal and leukemic cells will be measured. Novel c-myb activated genes will be identified using differential display. The expression of these genes will be suppressed using an antisense approach and the effect on cellular proliferation will be measured. In some leukemias, c-myb may be mutated resulting in altered protein interaction or gene activation. Primary leukemias will be screened for spontaneous c-myb mutations and these mutants will be analyzed for their effects on cellular proliferation using cell counting or tritiated thymidine incorporation, gene activation using RT-PCR or northern blot analysis, and co-factor interaction using co-immunoprecipitation or mammalian two hybrid assay. |
0.928 |