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HHS Recovery Act Recipient Reporting Readiness Tool

Step 4. Review and Copy the Grant Awards Data

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Award Detail for: N-acetylglutamate Synthase: Structure, Function & Defects
CHILDREN'S RESEARCH INSTITUTE
DUNS Number: 143983562
111 MICHIGAN AVENUE, NW
WASHINGTON, DC 20010-2978
Recipient Report: Grant or Loan
Prime Recipient

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Reporting Information
Award Type Award Number Final Report
Grant 3R01DK064913-06S1 Recipient responsible for this data

Award Recipient Information
Recipient DUNS Number Recipient Account Number Recipient Congressional District
143983562 Recipient responsible for this data Not Available

Award Information
Funding Agency Code Awarding Agency Code Award Date
7529 7529 09-11-2009
Amount of Award Sub Account Number for Program Source (TAS)  
$ 558,800 Recipient responsible for this data
Program Source (TAS)* CFDA Number 
750883 93.701
Total Number of Sub Awards to Individuals Total Amount of Sub Awards to Individuals
Recipient responsible for this data Recipient responsible for this data
Total Number of Payments to Vendors less than $25,000/award Total Amount of Payments to Vendors less than $25,000/award
Recipient responsible for this data Recipient responsible for this data
Total Number of Sub Awards less than $25,000/award Total Amount of Sub Awards less than $25,000/award
Recipient responsible for this data Recipient responsible for this data
Award Description
DESCRIPTION (provided by applicant): This project focuses on the regulation of the N-acetylglutamate synthase (NAGS) gene and its enzyme product which catalyzes the formation of N-acetylglutamate (NAG). While carbamyl phosphate synthetase 1 (CPS1) is often referred to as the first and rate-limiting enzyme of ureagenesis, it requires NAG as an essential allosteric activator. Therefore, the levels of NAG in the mitochondrial matrix of liver and small intestinal epithelial cells play an important role in regulating urea production. This NAGS/NAG system is an emerging target for new treatment of hyperammonemia. New tools that were developed during the previous funding periods will allow us to address many important questions about this system, its clinical relevance, and how it can be exploited to develop new approaches for managing and treating hyperammonemia. The specific aims of this project are to: Aim 1 - Characterize the transcriptional regulation of NAGS and its role in human disease. In this aim we will elucidate the functional importance of two conserved non-coding sequences of the NAGS gene in the regulation of its transcription. This will be accomplished by studying liver and intestine derived cells and by using bioinformatics, reporter, chromatin immunoprecipitation and DNA-pull-down assays. Aim 2 - Determine the structural basis and physiological role of mammalian NAGS activation by L-arginine. This aim will explore (a) structural and mechanistic correlates of the positive regulatory effect of L-arginine on NAGS activity at the protein level by using x-ray crystallography of mammalian NAGS with and without bound substrates and (b) in vivo effect on ureagenesis and other metabolic parameters of arginine activation of NAGS in koNAGS mouse by transfection with arginine-insensitive and sensitive NAGS transgenes. Aim 3 - Characterize the structural and functional interactions between the N-terminus of NAGS and CPS1. This aim will use X-ray crystallography to determine the structural basis of NAGS-CPS1 interaction, and the koNAGS mouse transfected with various NAGS mutants will be studied to identify alterations in nitrogen metabolism that will reveal the functional importance of this interaction. Aim 4 - Determine the mechanism of N-carbamylglutamate (NCG) delivery to hepatocyte and intestinal cell mitochondria. This aim will use affinity labeling and siRNA knock down methods to identify transporters that are involved in delivery of NCG to liver and intestinal cell mitochondria. Overall, the project uses new tools of research to gain new insights into a system that can be exploited for better diagnosis and treatment of NAGS deficiency and other conditions associated with hyperammonemia.

Project Information
Project Name or
Project/Program Title
Project Status Total Federal Amount ARRA Funds
Received/Invoiced
N-acetylglutamate Synthase: Structure, Function & Defects Recipient responsible for this data Recipient responsible for this data
Number of Jobs Description of Jobs Created
Recipient responsible for this data Recipient responsible for this data
Quarterly Activities/Project Description
Recipient responsible for this data
 
Activity Code (NAICS or NTEE-NPC)
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Total Federal Amount of ARRA
Expenditure
Total Federal ARRA
Infrastructure Expenditure
Infrastructure Contact Name
Recipient responsible for this data Recipient responsible for this data Recipient responsible for this data
Infrastructure Contact Email Infrastructure Contact Phone Infrastructure Contact Phone Ext.
Recipient responsible for this data Recipient responsible for this data Recipient responsible for this data
Infrastructure Contact Street Address 1 Infrastructure Contact Street Address 2 Infrastructure Contact Street Address 3
111 MICHIGAN AVENUE, NW Not Available Recipient responsible for this data
Infrastructure City Infrastructure State Infrastructure ZIP Code+4
WASHINGTON DC 20010-2978
Infrastructure Purpose and Rationale
Recipient responsible for this data

Primary Place of Performance
Street Address 1 Street Address 2 City
Not Available Recipient responsible for this data Washington
State Zip Code+4 Congressional District
DC 200102916 98
Country  
US

Recipient Highly Compensated Officers
Prime Recipient Indication of Reporting Applicability # Officer Name Officer Compensation
Recipient responsible for this data 1 Recipient responsible for this data Recipient responsible for this data
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The information provided by this tool is baseline data that the Recipient should include in the Recipient Report that must be submitted to FederalReporting.gov beginning October 1, 2009. The data from this tool can be cut and pasted directly into the Recipient Report.