George Benedek - US grants

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Area:

Visual neuroscience

Website:

http://www.szote.u-szeged.hu/phys/frames/main.htm

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High-probability grants

According to our matching algorithm, George Benedek is the likely recipient of the following grants.

Years	Recipients	Code	Title / Keywords	Matching score
1977 — 1981	Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	N-Particle Distributions For Macromolecular Aggregates @ Massachusetts Institute of Technology	0.909
1977 — 1980	Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	Physical-Chemical Study of the Size, Shape, Polydispersity, and Phase Equilibria of Simple and Mixed Aqueous Micellar Solutions Formed From Steroid and Straight Chain Amphiphiles @ Massachusetts Institute of Technology	0.909
1980 — 1984	Cohen, Richard Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	Study of the N-Particle Distributions For Macromolecular Aggregates @ Massachusetts Institute of Technology	0.909
1984 — 1985	Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	Acquisition and Construction of a Quasielastic Light Scattering Spectrometer @ Massachusetts Institute of Technology	0.909
1984 — 1985	Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	U.S.-France Joint Seminar: Physics and Chemistry of Gelation, March 1984, Nice, France @ Massachusetts Institute of Technology	0.909
1985 — 1988	Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	Light Scattering Studies of Phase Transitions in Protein Water Solutions @ Massachusetts Institute of Technology	0.909
1992 — 1994	Benedek, George [⬀]	N/AActivity Code Description: No activity code was retrieved: click on the grant title for more information	Phase Separation of Ternary Protein Water Solutions @ Massachusetts Institute of Technology This project is an experimental and theoretical investigation of phase separations of ternary aqueous protein solutions. The solutions will be studied by static and dynamic light scattering spectroscopy as well as biochemical chromatographic and centrifugation methods. The theoretical studies will use the Carnahan-Starling mixing entropy and a mean field model for the interaction energies in order to construct a Gibbs free energy for the system. This will potentially provide a route to interpretation and prediction of phase boundaries and compositions of coexisting phases. The results will be of significance for the general area of biomolecular materials purification and processing. Show summary Hide summary	0.909
2006 — 2010	Benedek, George B [⬀]	P01Activity Code Description: For the support of a broadly based, multidisciplinary, often long-term research program which has a specific major objective or a basic theme. A program project generally involves the organized efforts of relatively large groups, members of which are conducting research projects designed to elucidate the various aspects or components of this objective. Each research project is usually under the leadership of an established investigator. The grant can provide support for certain basic resources used by these groups in the program, including clinical components, the sharing of which facilitates the total research effort. A program project is directed toward a range of problems having a central research focus, in contrast to the usually narrower thrust of the traditional research project. Each project supported through this mechanism should contribute or be directly related to the common theme of the total research effort. These scientifically meritorious projects should demonstrate an essential element of unity and interdependence, i.e., a system of research activities and projects directed toward a well-defined research program goal.	Kinetics of Beta Amyloid Aggregation and Fibrillogenesis: Light Scattering Study @ University of California Los Angeles We hypothesize that amyloid beta-protein (A-beta) assembly into oligomers and polymers is a seminal[unreadable] neuropathogenetic process in Alzheimer's disease (AD) and in cerebral amyloid angiopathy (CAA).[unreadable] Inhibiting formation of, or disrupting, A-beta assemblies thus could be of benefit in the treatment of these[unreadable] disorders. To test this hypothesis, a detailed mechanistic knowledge of the assembly process is necessary.[unreadable] Our previous work towards this goal revealed the existence of protofibrillar fibrillogenesis intermediates.[unreadable] These have been found to be neurotoxic in vitro. Recently, in collaborative studies with the Lannfelt group,[unreadable] we reported that protofibrils may be the causative agents in an "Arctic" form of AD. Thus, a concordance of[unreadable] results from fundamental studies of A-beta assembly in vitro with those from clinical investigations in[unreadable] humans supports the involvement of prefibrillar assemblies in AD pathogenesis. In order to understand the[unreadable] structural and thermodynamic principles underlying the formation of these toxic A-beta assemblies, rigorous[unreadable] in vitro studies are necessary. This elucidation process should facilitate later rational design and testing of[unreadable] therapeutic agents. Here, we seek to delve deeply into the thermodynamics and structural biology of early[unreadable] A-beta assembly reactions in order to understand the fundamental factors controlling these processes and[unreadable] to identify and characterize the structures formed. These structures include small prenuclear oligomers,[unreadable] larger micelle-like oligomers, fibril nuclei, and protofibrils. Importantly, knowledge gained regarding the[unreadable] kinetics of formation and the stability of these assemblies will be used to enable functional assays of the[unreadable] biological effects of the assemblies. We propose to accomplish these goals in the context of the following[unreadable] four interconnected aims.[unreadable] Aim 1. To elucidate the thermodynamics of A-beta fibril formation at neutral pH.[unreadable] Aim 2. To determine the structural features of early A-beta assemblies.[unreadable] Aim 3. To determine the mechanism of transformation of early A-beta assemblies into fibril nuclei.[unreadable] Aim 4. To determine the biological activity of early intermediates. Show summary Hide summary	0.926