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High-probability grants
According to our matching algorithm, Dale B. Schenk is the likely recipient of the following grants.
| Years |
Recipients |
Code |
Title / Keywords |
Matching
score |
| 1989 |
Schenk, Dale B |
R43Activity Code Description:
To support projects, limited in time and amount, to establish the technical merit and feasibility of R&D ideas which may ultimately lead to a commercial product(s) or service(s). |
Characterization-Amyloid Precursor Fragments in Plasma @ Athena Neurosciences, Inc.
Alzheimer's disease is currently thought to affect as many as 1-3 million people in the USA alone. It has recently been found that the core A4 peptide of the senile plaques (one hallmark of the disease) is derived from a precursor protein 695-750 amino acids long. It is not known how the conversion of the precursor to the A4 protein occurs, but it is possible that specific polypeptide fragments are released into serum or CSF that could be detected by an immunoassay of appropriate specificity and sensitivity. Monoclonal antibodies will be raised to the full length precursor molecule derived from cDNA transfected mammalian cells overexpressing the amyloid precursor. The antibodies will be characterized using our expressed precursor molecule. In addition, antisera will also be prepared from bacterially expressed fragments of the precursor molecule and corresponding synthetic peptides. These antibodies will be used to develop highly sensitive fluorometric immunoassays against various regions of the amyloid precursor. These assays will then be evaluated for their diagnostic potential using numerous patient samples obtained from our comprehensive groups of collaborators.
|
0.912 |
| 1989 |
Schenk, Dale B |
R43Activity Code Description:
To support projects, limited in time and amount, to establish the technical merit and feasibility of R&D ideas which may ultimately lead to a commercial product(s) or service(s). |
Identification of Alzheimer-Specific Antigens in Csf @ Athena Neurosciences, Inc.
The objective of the proposal is to define antigens in the CSF that are specific to Alzheimer's disease. This effort has two important potential results. The first is a CSF-based diagnostic immunoassay for use as both a diagnostic marker and as a useful adjunct to monitor eventual therapy. The methodology to identify the diagnostic markers involves the screening of-a large number of monoclonal antibodies with a highly sensitive and predictive fluorometric test. The assay is configured in such a way that only monoclonal antibodies of diagnostic potential are identified. In addition, the immuno-genes that are to be used are those related directly to the disease. Thus, the proposed research plan brings together macromolecules known to be involved in Alzheimer's disease with a sensitive high volume screen capable of detecting antibodies of diagnostic potential. The ultimate goal of the research plan will be to immunoaffinity purify and structurally characterize antigens that are specifically elevated in Alzheimer's disease.
|
0.912 |
| 1990 — 1991 |
Schenk, Dale B |
R44Activity Code Description:
To support in - depth development of R&D ideas whose feasibility has been established in Phase I and which are likely to result in commercial products or services. SBIR Phase II are considered 'Fast-Track' and do not require National Council Review. |
Characterization of B-Amyloid Precursor Fragments @ Athena Neurosciences, Inc.
Alzheimer's disease is currently thought to affect as many as 1-3 million people in the USA alone. It has recently been found that the core A4 peptide of the senile plaques (one hallmark of the disease) is derived from a precursor protein 695-750 amino acids long. It is not known how the conversion of the precursor to the A4 protein occurs, but it is possible that specific polypeptide fragments are released into serum or CSF that could be detected by an immunoassay of appropriate specificity and sensitivity. Monoclonal antibodies will be raised to the full length precursor molecule derived from cDNA transfected mammalian cells overexpressing the amyloid precursor. The antibodies will be characterized using our expressed precursor molecule. In addition, antisera will also be prepared from bacterially expressed fragments of the precursor molecule and corresponding synthetic peptides. These antibodies will be used to develop highly sensitive fluorometric immunoassays against various regions of the amyloid precursor. These assays will then be evaluated for their diagnostic potential using numerous patient samples obtained from our comprehensive groups of collaborators.
|
0.912 |
