This grant is for the purpose of advancing our understanding of cellular and molecular mechanisms underlying prion-like aggregate formation, propagation, and neurotoxicity in Alzheimer’s Disease (AD) and related dementias (AD/ADRD). Many neurodegenerative diseases are characterized by the accumulation of misfolded proteins, similar to classical prion diseases where proteins misfold and self-propagate, leading to neuronal death. This initiative specifically targets the study of how AD/ADRD-relevant proteins, such as Alpha, tau, beta-synuclein, and TDP-43, exhibit these prion-like behaviors. The goal is to elucidate the mechanisms of these conversion events and their propagation, as well as the downstream processes that trigger neurotoxicity, pathological changes, and circuit dysfunction in the brain, contributing to dementia.
Opportunity ID: 342734
General Information
| Document Type: | Grants Notice |
| Funding Opportunity Number: | PAR-23-023 |
| Funding Opportunity Title: | Cellular and Molecular Mechanisms of Prion-Like Aggregate Seeding, Propagation, and Neurotoxicity in AD/ADRD (R01 Clinical Trial Not Allowed) |
| Opportunity Category: | Discretionary |
| Opportunity Category Explanation: | – |
| Funding Instrument Type: | Grant |
| Category of Funding Activity: | Education Health |
| Category Explanation: | – |
| Expected Number of Awards: | – |
| Assistance Listings: | 93.279 — Drug Abuse and Addiction Research Programs |
| Cost Sharing or Matching Requirement: | No |
| Version: | Synopsis 1 |
| Posted Date: | Jul 25, 2022 |
| Last Updated Date: | Jul 25, 2022 |
| Original Closing Date for Applications: | Oct 24, 2022 |
| Current Closing Date for Applications: | Oct 24, 2022 |
| Archive Date: | Nov 29, 2022 |
| Estimated Total Program Funding: | – |
| Award Ceiling: | – |
| Award Floor: | – |
Eligibility
| Eligible Applicants: | City or township governments County governments Independent school districts Small businesses Native American tribal governments (Federally recognized) Others (see text field entitled “Additional Information on Eligibility” for clarification) Private institutions of higher education Public and State controlled institutions of higher education For profit organizations other than small businesses Nonprofits having a 501(c)(3) status with the IRS, other than institutions of higher education Public housing authorities/Indian housing authorities State governments Nonprofits that do not have a 501(c)(3) status with the IRS, other than institutions of higher education Special district governments Native American tribal organizations (other than Federally recognized tribal governments) |
| Additional Information on Eligibility: | Other Eligible Applicants include the following: Alaska Native and Native Hawaiian Serving Institutions; Asian American Native American Pacific Islander Serving Institutions (AANAPISISs); Eligible Agencies of the Federal Government; Faith-based or Community-based Organizations; Hispanic-serving Institutions; Historically Black Colleges and Universities (HBCUs); Indian/Native American Tribal Governments (Other than Federally Recognized); Non-domestic (non-U.S.) Entities (Foreign Organizations); Regional Organizations; Tribally Controlled Colleges and Universities (TCCUs) ; U.S. Territory or Possession. |
Additional Information
| Agency Name: | National Institutes of Health |
| Description: | The accumulation of misfolded proteins in the brain is a key pathological feature shared by many neurodegenerative diseases that can result in dementia such as Alzheimers Disease, Lewy Body Diseases, Frontotemporal Degeneration, and cerebral amyloid angiopathy. Classical prion diseases such as Creutzfeldt-Jakob Disease are a rare family of neurodegenerative disorders that occur when the cellular prion protein (PrPC) undergoes structural conversion to a pathological form (PrPSc), which is usually triggered by its interaction with an infectious variant of the protein that forces the conformational change. Once this process is initiated, it becomes self-propagating until toxic aggregates accumulate within the CNS, leading to neuronal death. Because misfolded proteins of AD/ADRD have been reported to share some features with pathological prion protein at the structural level, it has thus been proposed that ADRD-relevant proteins such as Alpha, tau, beta-synuclein, and TDP-43 (among others) may exhibit prion-like behaviors that lead to toxic aggregate and tangle formation. The goal of this initiative is to promote studies that increase our understanding of the cellular and molecular mechanisms by which such prion-like conversion events occur and are propagated in AD/ADRD, as well as the downstream mechanisms that trigger neurotoxicity, pathological and circuit changes in the brain. |
| Link to Additional Information: | http://grants.nih.gov/grants/guide/pa-files/PAR-23-023.html |
| Grantor Contact Information: | If you have difficulty accessing the full announcement electronically, please contact:
NIH OER Webmaster
OERWebmaster03@od.nih.gov Email:OERWebmaster03@od.nih.gov |
Version History
| Version | Modification Description | Updated Date |
|---|---|---|
Related Documents
There are no related documents on this grant.
Packages
| Agency Contact Information: | NIH OER Webmaster OERWebmaster03@od.nih.gov Email: OERWebmaster03@od.nih.gov |
| Who Can Apply: | Organization Applicants |
| Assistance Listing Number | Competition ID | Competition Title | Opportunity Package ID | Opening Date | Closing Date | Actions |
|---|---|---|---|---|---|---|
| FORMS-G | Use for due dates on or after January 25, 2022 | PKG00276177 | Sep 24, 2022 | Oct 24, 2022 | View |
Package 1
Mandatory forms
342734 RR_SF424_5_0-5.0.pdf
342734 PHS398_CoverPageSupplement_5_0-5.0.pdf
342734 RR_OtherProjectInfo_1_4-1.4.pdf
342734 PerformanceSite_4_0-4.0.pdf
342734 RR_KeyPersonExpanded_4_0-4.0.pdf
342734 PHS398_ResearchPlan_4_0-4.0.pdf
342734 PHSHumanSubjectsAndClinicalTrialsInfo_3_0-3.0.pdf
Optional forms
342734 RR_Budget_3_0-3.0.pdf
342734 RR_SubawardBudget30_3_0-3.0.pdf
342734 PHS398_ModularBudget_1_2-1.2.pdf
342734 PHS_AssignmentRequestForm_3_0-3.0.pdf
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