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, Mingxia Huang is the likely recipient of the following grants.
Years |
Recipients |
Code |
Title / Keywords |
Matching score |
2003 — 2007 |
Huang, Mingxia |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
Function and Regulation of Dna Damage Response Genes @ University of Colorado Denver
[unreadable] DESCRIPTION (provided by applicant): The survival of all organisms depends on the faithful transmission of DNA from one cell to its daughter cell. Cells respond to DNA damage by arresting the cell cycle and inducing the transcription of DNA repair genes. The Crt 1 protein has been identified as a key regulator of DNA damage-induced transcription of the genes encoding ribonucleotide reductase (RNR). The broad, long-term objective of this research program is to use modem methods in molecular genetics and biochemistry to understand the mechanisms underlying cellular response to DNA damage. The focus of this project is on the functional studies of Crtl, and to relate this understanding to the regulation of DNA damage response. This proposal also seeks to investigate CRT1-independent mechanism(s) involved in DNA damage-induced transcription. Specific aims of the proposed research are: (1) To characterize the regulation of Crt 1 activities by the upstream checkpoint kinases in order to understand the negative feedback mechanism of the CRTl-mediated DNA damage response. (2) To characterize the interactions between Crtl and the general repressor complex Ssn6/Tup 1 in response to DNA damage in order to understand how the DNA damage checkpoint controls the switch from the repressed state to the induced state. (3) To determine CRTl-independent mechanism(s) involved in the DNA damage-induced transcription of the RNR genes with the ultimate aim of understanding the interplay among different regulatory pathways controlled by the DNA damage checkpoint. Failure of DNA damage response results in genomic instability and cancer predisposition. As a result, this research will contribute to an increased understanding of the complex biology of DNA damage and repair. These studies will also be critical in guiding our efforts to target the DNA damage response process for cancer diagnosis, prevention, and treatment.
|
1 |
2008 — 2012 |
Huang, Mingxia |
R01Activity Code Description: To support a discrete, specified, circumscribed project to be performed by the named investigator(s) in an area representing his or her specific interest and competencies. |
In Vivo Regulation and Inhibition of Ribonucleotide Reductase @ University of Colorado Denver
DESCRIPTION (provided by applicant): The maintenance of adequate and balanced deoxyribonucleotide (dNTP) pools is essential for faithful DNA replication and repair. Loss of normal control of the dNTP pools can lead to cell death, genomic instability, and predisposition to cancer in humans. Regulation of ribonucleotide reductase (RNR) is largely responsible for controlling the relative ratios and amounts of the cellular dNTP pools. The central role of RNR in dNTP biosynthesis has also made it a successful target in the treatment of a number of malignancies. The RNR enzyme comprises of two subunits: the R1 subunit binds the four NDP substrates as well as the allosteric effectors (NTPs and dATP) that govern substrate specificity and turnover rate, and the R2 subunit houses the essential tyrosyl radical required to initiate nucleotide reduction in R1. The enzymatic activity of RNR can be modulated by allostery, transcription, protein inhibitor association, and subcellular compartmentation of its subunits. The budding yeast S. cerevisiae has emerged as a prototypical model system with which to investigate the complex mechanisms regulating the RNR activity. This proposal focuses on the mechanisms that control the RNR activity and consequently cellular dNTP pools by using a combination of biochemical, cell biology, and genetic approaches. Our central hypothesis is that these regulatory mechanisms are integrated to maintain optimal dNTP pools under different growth conditions so as to ensure high fidelity DNA synthesis and repair. Three specific aims are proposed: (1) To test the hypothesis that the Sml1 protein inhibits the RNR enzyme by impeding regeneration of the R1 active site and to define molecular determinants of the R1-Sml1 interaction and Sml1 degradation;(2) To examine the regulation of subcellular localization of the R2 subunit by the cell cycle and DNA damage checkpoints;(3) To characterize the role of the newly identified small protein Sld1 in RNR regulation. Sld1 belongs to a family of small protein RNR regulators, including the S. cerevisiae Sml1 and Sld1, the S. pombe Spd1, and their homologs encoded by other fungal genomes. The emphasis is to gain a mechanistic understanding of how the RNR activity is controlled by these evolutionarily conserved small size RNR regulatory proteins. Lessons learned from studies of the yeast RNR will serve as a paradigm for understanding of RNR regulation and dNTP pool control in eukaryotic cells, and may also suggest new approaches for RNR inhibition and for antitumor and antiviral drug development. PUBLIC HEALTH RELEVENCE: Ribonucleotide reductase is an essential enzyme that provides the building blocks for DNA in all organisms. This enzyme is also a proven target of clinical treatment of human cancers. The overall goal of this project is to understand how the activity of this enzyme is controlled inside the cell and finding new strategy for drug development targeting this enzyme.
|
1 |