Represents Grant table in the DB

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        {
            "type": "Grant",
            "id": "2964",
            "attributes": {
                "award_id": "1905374",
                "title": "Mechanistic investigation of DNA cleavage and specificity in CRISPR-Cas9",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Mathematical and Physical Sciences (MPS)",
                    "Chemistry of Life Processes"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 9021,
                        "first_name": "Catalina",
                        "last_name": "Achim",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
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                        "comments": null,
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                    }
                ],
                "start_date": "2019-09-01",
                "end_date": "2022-08-31",
                "award_amount": 450000,
                "principal_investigator": {
                    "id": 9022,
                    "first_name": "Giulia",
                    "last_name": "Palermo",
                    "orcid": null,
                    "emails": "",
                    "private_emails": "",
                    "keywords": null,
                    "approved": true,
                    "websites": null,
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                    "affiliations": [
                        {
                            "id": 153,
                            "ror": "",
                            "name": "University of California-Riverside",
                            "address": "",
                            "city": "",
                            "state": "CA",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
                "other_investigators": [],
                "awardee_organization": {
                    "id": 153,
                    "ror": "",
                    "name": "University of California-Riverside",
                    "address": "",
                    "city": "",
                    "state": "CA",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Giulia Palermo from the University of California, Riverside, to investigate the molecular basis of DNA cleavage and specificity in the CRISPR (clustered regularly interspaced short palindromic repeat)-Cas9 system through computational methods. The CRISPR-Cas9 technology is a method that makes precise modification of the genome of an organism (including that of humans) possible.  The technology is based on the use of a nuclease, an enzyme capable of cutting the double stranded DNA, and an RNA molecule that is bound to the enzyme and guides the enzyme to the site in the DNA where the cut is to take place.  This research seeks to understand the mechanism by which the enzyme functions using computational methods developed by Dr. Palermo and her collaborators. The results of this study may aid in the development of more efficient genome editing technologies and their applications in biological research, biofuels production, and the development of drought-resistant crops with enhanced nutritional value. The project involves an outreach and mentoring program, which includes hands-on sessions for high school students from underrepresented minority groups and teachers.\n\nCRISPR-Cas9 is a bacterial adaptive immune system that is revolutionizing basic and applied life sciences by enabling a facile genome editing technology. This project provides detailed understanding of how this system edits and manipulates nucleic acids, which is of importance for improving the genome editing capability.  This research project seeks to characterize the mechanism of DNA cleavage and specificity of the Streptococcus Pyogenes (Sp) CRISPR-Cas9 system by using state-of-the-art computational methods. The project employs a mixed quantum mechanics/molecular mechanics (QM/MM) approach and ab-initio Molecular Dynamics (MD) simulations (using the Born-Oppenheimer and Car-Parrinello approaches) in combination with free energy methods to investigate the catalytic mechanism of DNA cleavage in CRISPR-Cas9. These methodologies may elucidate the catalytic role of metal ions, which are critical for the enzymatic processing of DNA. Classical MD and enhanced sampling techniques are employed to investigate the mechanism of DNA specificity, characterizing the conformational changes arising from the binding of altered DNA sequences and how they affect the catalysis. Theoretical investigations are performed in collaboration with experimentalists.  The new theory assists in the interpretation of experimental data and makes possible predictions that can be tested in the laboratory.\n\nThis award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "4174",
            "attributes": {
                "award_id": "1608009",
                "title": "CDS&E: Cyclic Tetrapeptide Probes For Protein Binding",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Mathematical and Physical Sciences (MPS)",
                    "Chemistry of Life Processes"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 14052,
                        "first_name": "Max",
                        "last_name": "Funk",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
                        "affiliations": []
                    }
                ],
                "start_date": "2016-09-01",
                "end_date": "2020-08-31",
                "award_amount": 500000,
                "principal_investigator": {
                    "id": 14054,
                    "first_name": "Kevin",
                    "last_name": "Burgess",
                    "orcid": null,
                    "emails": "",
                    "private_emails": "",
                    "keywords": null,
                    "approved": true,
                    "websites": null,
                    "desired_collaboration": null,
                    "comments": null,
                    "affiliations": [
                        {
                            "id": 342,
                            "ror": "https://ror.org/01f5ytq51",
                            "name": "Texas A&M University",
                            "address": "",
                            "city": "",
                            "state": "TX",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
                "other_investigators": [
                    {
                        "id": 14053,
                        "first_name": "Thomas R",
                        "last_name": "Ioerger",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
                        "affiliations": []
                    }
                ],
                "awardee_organization": {
                    "id": 342,
                    "ror": "https://ror.org/01f5ytq51",
                    "name": "Texas A&M University",
                    "address": "",
                    "city": "",
                    "state": "TX",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this award, the Chemistry of Life Processes Program in the Chemistry Division is funding Dr. Kevin Burgess of Texas A & M University to discover small molecules that affect how some proteins bind to each other. Protein-protein interactions are important to many biological processes in cells. Thus having small molecules that can either aid or or hinder protein-protein interactions could lead to potential new drugs to help treat various diseases. The project is creating new small molecules and studying their effect on protein-protein interactions. It also combines chemical synthesis, computer-aided molecular design and data-mining training for graduate and undergraduate students to help them tackle problems in contemporary life science.  \n\nCyclic peptides are known to mimic key regions involved in protein-protein interactions, i.e. to be Protein-Protein Interface (PPI) mimics.  While cyclic pentapeptides are easy to make they tend to equilibrate between conformers.  Conversely cyclic tetrapeptides from natural amino acids are difficult to make but are more conformationally stable. Thus, easily synthesized cyclic peptides from genetically encoded amino acids linked by main-chain amides can have ring sizes of 9, 12, 15, etc. i.e. 3n atoms, (n = # amino acids) which misses ring sizes between 12 and 15 that combine conformational rigidity with ease of synthesis.  This work is showing that contrary to some earlier reports, cyclic Tetrapeptides from natural amino acids are conformationally rigid and are more synthetically accessible than previously thought. It is also showing that replacement of a genetically encoded residue with some rigid unnatural amino acids can be used to give cyclic tetrapeptides that rest at a useful crossroads between ease of synthesis and conformational rigidity.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "1549",
            "attributes": {
                "award_id": "2037695",
                "title": "RAPID: Developing a universal modular platform to engineer coronavirus vaccine candidates",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Mathematical and Physical Sciences (MPS)"
                ],
                "program_reference_codes": [
                    "096Z",
                    "7914"
                ],
                "program_officials": [
                    {
                        "id": 4041,
                        "first_name": "Pui",
                        "last_name": "Ho",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
                        "affiliations": []
                    }
                ],
                "start_date": "2020-07-15",
                "end_date": "2022-06-30",
                "award_amount": 200000,
                "principal_investigator": {
                    "id": 4042,
                    "first_name": "Angad P",
                    "last_name": "Mehta",
                    "orcid": null,
                    "emails": "[email protected]",
                    "private_emails": "",
                    "keywords": null,
                    "approved": true,
                    "websites": null,
                    "desired_collaboration": null,
                    "comments": null,
                    "affiliations": [
                        {
                            "id": 281,
                            "ror": "",
                            "name": "University of Illinois at Urbana-Champaign",
                            "address": "",
                            "city": "",
                            "state": "IL",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
                "other_investigators": [],
                "awardee_organization": {
                    "id": 281,
                    "ror": "",
                    "name": "University of Illinois at Urbana-Champaign",
                    "address": "",
                    "city": "",
                    "state": "IL",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this award, the Chemistry of Life Processes program in the Chemistry Division supports the studies by Dr. Angad Mehta at the University of Illinois at Urbana-Champaign to make live attenuated forms of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) that require an unnatural compound to reproduce. SARS-CoV-2 is the virus that causes coronavirus disease 2019 (COVID-19). Live-attenuated viruses have reduced abilities to cause disease, but remain capable of providing immunity in humans. As such, live-attenuated viruses represent one of the effective strategies for the development of vaccines against wide-spread viral infections.  The genomic RNA of the virus must be modified with a methyl group in order to be copied by infected cells, and this methyl group is added by enzymes using the natural compound S-adenosylmethionine (AdoMet). Dr. Mehta’s project engineers SARS-CoV-2 particles that use synthetic forms of AdoMet (called xAdoMet) for this critical methylation step. The resulting engineered SARS-CoV-2* is a live virus in a laboratory, where xAdoMet can be added as a required supplement. The SARS-CoV-2*, however, cannot reproduce in normal cells, where xAdoMet is not present, but can still result in an immune response in an infected patient. The impact on society is that a unique platform is engineered for the development of vaccines to address viral diseases, including the COVID-19 pandemic.  The broader impacts of this project include the strong cross-disciplinary training of graduate students.This goal of this study is to develop live attenuated SARS-CoV-2 particles that are dependent on an unnatural version of an essential cofactor for its replication that is added in a laboratory setting, but not available in the infected host. SARS-CoV-2 requires S-adenosylmethionine (AdoMet) as a cofactor for a critical methylation of the viral RNA by a methyl transferase in order to translate its genes and replicate its genome. Through this project, a strain of the coronavirus (SARS-CoV-2*) is engineered that utilizes and is dependent on an unnatural analogue of AdoMet (xAdoMet) for the critical methylation reactions. Such a virus requires supplements of xAdoMet in a laboratory in order to replicate. Once injected into a host, this viral strain can infect a cell and potentially induce an immune response in the host, but cannot replicate in the absence of exogenous supplementation with xAdoMet. The objectives are to synthesize a series of xAdoMet compounds; use the xAdoMet compounds to engineer SARS-CoV-2* through directed evolution; and test the live attenuated virus for induction of immune response in cell culture. The AdoMet-dependent methylation mechanism is conserved in all known coronavirus pathogens and, therefore, has the potential to serve as a far-reaching and modular platform for vaccine development well beyond SARS-CoV-2.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "14106",
            "attributes": {
                "award_id": "2147792",
                "title": "Plasmon-induced Triplet Energy Transfer (PITET) for Photon Upconversion",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Mathematical and Physical Sciences (MPS)",
                    "OFFICE OF MULTIDISCIPLINARY AC"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 30636,
                        "first_name": "John",
                        "last_name": "Papanikolas",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
                        "affiliations": []
                    }
                ],
                "start_date": "2021-09-01",
                "end_date": null,
                "award_amount": 450000,
                "principal_investigator": {
                    "id": 30637,
                    "first_name": "Ming",
                    "last_name": "Tang",
                    "orcid": null,
                    "emails": "",
                    "private_emails": "",
                    "keywords": null,
                    "approved": true,
                    "websites": null,
                    "desired_collaboration": null,
                    "comments": null,
                    "affiliations": []
                },
                "other_investigators": [],
                "awardee_organization": {
                    "id": 202,
                    "ror": "https://ror.org/03r0ha626",
                    "name": "University of Utah",
                    "address": "",
                    "city": "",
                    "state": "UT",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this award, the Macromolecular, Supramolecular, and Nanochemistry Program in the Chemistry Division is supporting Dr. Ming Lee Tang at the University of California Riverside (UCR) to study the energy transfer process of plasmonic systems.  Plasmonics refers to light-induced oscillation of loosely bound electrons in metals.  This research is important for catalysis, imaging, and energy conversion applications. Minuscule metal particles with dimensions on the order of nanometers have been treasured historically for their beauty in stained glass windows. The vivid colors in stained glass arise from the strong absorption and scattering of light due to plasmons supported by the metal nanoparticles. Dr. Tang’s team is conducting fundamental research that addresses that seeks to efficiently transfer the energy stored as plasmons in metal nanoparticles to neighboring chemical molecules.  The research aims to provide mechanisms to prevent the system from unwanted energy loss through rapid scattering of light or dissipation of energy as heat.  Such advances are essential for the development of metal nanoparticles for intended applications in photocatalysis and in solar cells. The team designs and synthesizes various nanomaterial architectures.  Plasmons tightly confined within the nanoscale metal architectures are then characterized to tune the system to perform useful work upon light activation.  This research also has broader impacts of engaging the general public in the Inland Empire program in Southern California. This outreach program includes interactive demonstrations and science activities at local elementary schools and pre-schools that are led by undergraduate and graduate students.<br/><br/>Dr. Ming Lee Tang’s team at UCR is investigating plasmon-induced triplet energy transfer. The goal is to use light captured by metal nano-antennas for photon upconversion, a process of converting low energy photons from incoherent sources such as the sun to useful high energy photons. Novel light-absorbing nanostructures based on noble metals in this research can absorb near-infrared photons to produce violet photon emissions from neighboring anthracene- and perylene-based chromophores. Specifically, silver nanoprisms and gold nanorods with their localized surface plasmon resonance tuned between 1.5 and 1.8 eV are expected to be resonant with the lowest excited triplet states of the chromophores, so as to photosensitize the molecular triplet states across an oxide barrier. Steady-state photon upconversion measurements will be used to quantify the efficiency of plasmon-induced triplet energy transfer. Time resolved photoluminescence and transient absorption measurements provide independent measurements of the yield and rate of the triplet energy transfer.<br/><br/>This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "5403",
            "attributes": {
                "award_id": "0640934",
                "title": "Fluorous Proteins: Structure, Stability, and Biological Activity",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Unknown",
                    "BIMOLECULAR PROCESSES"
                ],
                "program_reference_codes": [],
                "program_officials": [],
                "start_date": "2007-08-15",
                "end_date": "2010-07-31",
                "award_amount": 435000,
                "principal_investigator": {
                    "id": 18901,
                    "first_name": "E. Neil",
                    "last_name": "Marsh",
                    "orcid": null,
                    "emails": "[email protected]",
                    "private_emails": null,
                    "keywords": "[]",
                    "approved": true,
                    "websites": "[]",
                    "desired_collaboration": "",
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                    "affiliations": [
                        {
                            "id": 169,
                            "ror": "",
                            "name": "Regents of the University of Michigan - Ann Arbor",
                            "address": "",
                            "city": "",
                            "state": "MI",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
                "other_investigators": [
                    {
                        "id": 18900,
                        "first_name": "Hashim M",
                        "last_name": "Al-Hashimi",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
                        "affiliations": []
                    }
                ],
                "awardee_organization": {
                    "id": 169,
                    "ror": "",
                    "name": "Regents of the University of Michigan - Ann Arbor",
                    "address": "",
                    "city": "",
                    "state": "MI",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this award, the Organic and Macromolecular Chemistry Program supports Neil Marsh and Hashim M. Al-Hashimi both of the University of Michigan whose research will advance the area of protein design by engineering some of the novel properties of fluorocarbons into biological molecules. This will be achieved by synthesizing proteins that contain extensively fluorinated ('fluorous') analogs of hydrophobic amino acids in their hydrophobic cores. Fluorous amino acids are predicted to stabilize proteins against unfolding by heat and organic solvents and to facilitate protein: protein recognition through specific fluorocarbon-fluorocarbon interactions. Fluorinated versions of a dimeric RNA-binding protein, Rop, will be synthesized in which the hydrophobic core of Rop will be repacked with the fluorous analog of leucine, hexafluoroleucine. This protein is small enough (63 residues) to be efficiently synthesized by peptide synthesis, which will allow fluorous amino acids to be introduced site specifically. Rop protein has been extensively used as a model system for investigating protein stability and folding, and as a template for protein re-design. These data will serve as a useful reference for the present study. A variety of physical techniques (such as circular dichroism, microcalorimetry and analytical ultracentrifugation) will be used to investigate the effect of fluorination on the biological activity, structure and stability of fluorous Rop proteins. An important innovation will be the use of residual dipolar coupling (RDC) NMR measurements to perform detailed comparisons of the effect of fluorination on the structure and conformational rigidity of the protein. The experiments will address fundamental questions about the impact of fluorination on protein structure and dynamics.\nThis award from the Organic and Macromolecular Chemistry Program supports Professors Neil Marsh and Hashim M. Al-Hashimi both of the University of Michigan whose research will impact attempts to design biosensors and enzymes used in industrial processes, where stability towards extremes of temperature and pH and towards organic solvents is necessary. There is the potential for fluorous proteins to find uses in medical imaging by exploiting the high NMR sensitivity of Fluorine 19 or their enhanced biological stability could lead to uses as therapeutic agents or vehicles for drug delivery. The project will advance the education, training and professional development of undergraduates, graduate students and postdoctoral scientists in the inter-disciplinary area of chemical biology and biophysics. To broaden their education further, a joint interdisciplinary group meeting and journal club will be initiated. Their professional development will be enhanced by active participation in the dissemination of their results, both through drafting manuscripts and progress reports, and through oral and poster presentations at local and national scientific meetings.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "552",
            "attributes": {
                "award_id": "1955074",
                "title": "CAS: Design and Mechanistic Understanding of Selective Electrocatalysts Based on Earth-Abundant Metal Compounds",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Mathematical and Physical Sciences (MPS)"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 1165,
                        "first_name": "Kenneth",
                        "last_name": "Moloy",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
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                    }
                ],
                "start_date": "2020-08-15",
                "end_date": "2023-07-31",
                "award_amount": 650000,
                "principal_investigator": {
                    "id": 1167,
                    "first_name": "Song",
                    "last_name": "Jin",
                    "orcid": null,
                    "emails": "[email protected]",
                    "private_emails": "",
                    "keywords": null,
                    "approved": true,
                    "websites": null,
                    "desired_collaboration": null,
                    "comments": null,
                    "affiliations": [
                        {
                            "id": 263,
                            "ror": "",
                            "name": "University of Wisconsin-Madison",
                            "address": "",
                            "city": "",
                            "state": "WI",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
                "other_investigators": [
                    {
                        "id": 1166,
                        "first_name": "Jordan R",
                        "last_name": "Schmidt",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
                        "desired_collaboration": null,
                        "comments": null,
                        "affiliations": []
                    }
                ],
                "awardee_organization": {
                    "id": 263,
                    "ror": "",
                    "name": "University of Wisconsin-Madison",
                    "address": "",
                    "city": "",
                    "state": "WI",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this award,the Chemical Catalysis Program of the Division of Chemistry is supporting Drs. Song Jin and Jordan Schmidt of the University of Wisconsin-Madison to combine theory and experiment to design, develop, and understand new electrochemical methods to generated hydrogen peroxide  (H2O2) from molecular oxygen. Hydrogen peroxide (H2O2) is an environmentally benign oxidant with many industrial and environmental applications. It is also a recommended disinfectant in general, including for the novel coronavirus responsible for the COVID-19 pandemic. The current commercial production of H2O2 is characterized by significant cost, energy consumption, and safety concerns. To be economically competitive the current process is practiced in a few large, centralized manufacturing plants. In comparison, small scale, decentralized, on-site production of H2O2 directly from oxygen using electricity could be a more effective and sustainable approach. However, electrochemical approaches to H2O2 need to be much more efficient and less costly to be viable. The success of this project can facilitate the efficient decentralized production of H2O2 and have broad technological impacts related to the environment, sustainability, and the healthcare fiels. This project includes a significant educational outreach component and seeks to build a more diverse scientific workforce through inclusive training.Drs. Song Jin and Jordan Schmidt and their team combine theory and experiment to exploit the unique attributes of unexplored metal compound electrocatalysts to design, develop, and understand new and selective electrocatalysts based on metal chalcogenides for the selective two-electron oxygen reduction reaction (2e ORR) in acidic and neutral solutions. Such selective 2e ORR electrocatalysts can facilitate decentralized electrochemical production of H2O2, an environmentally benign oxidant with diverse applications in industrial, environmental, and healthcare settings. Density functional theory calculations and kinetic models provide detailed insights into activity and selectivity and identify promising candidate structures among transition metal chalcogenides for subsequent synthesis and performance evaluation. Electrochemical and (in situ) spectroscopic studies reveal catalyst activity, selectivity, and potential-dependent reaction intermediates, with computational examination providing mechanistic insights into the catalytic mechanism(s) and further design principles governing catalyst selectivity and stability. Understanding and rationally designing complex metal compound catalysts for enabling various selective electrocatalytic reactions can lead to fundamental and transferrable insights into how complex structural motifs influence catalyst activity and selectivity. The success of this project can also facilitate the efficient decentralized electrochemical production of H2O2 and, as such, has the potential for broad scientific and societal impact.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "4355",
            "attributes": {
                "award_id": "1455353",
                "title": "CAREER: Revealing fluorescence mechanisms of emerging fluorescent protein biosensors using femtosecond stimulated Raman spectroscopy",
                "funder": {
                    "id": 3,
                    "ror": "https://ror.org/021nxhr62",
                    "name": "National Science Foundation",
                    "approved": true
                },
                "funder_divisions": [
                    "Mathematical and Physical Sciences (MPS)",
                    "Chemistry of Life Processes"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 14822,
                        "first_name": "Pui",
                        "last_name": "Ho",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
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                    }
                ],
                "start_date": "2015-02-15",
                "end_date": "2021-01-31",
                "award_amount": 650000,
                "principal_investigator": {
                    "id": 14823,
                    "first_name": "Chong",
                    "last_name": "Fang",
                    "orcid": null,
                    "emails": "",
                    "private_emails": "",
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                    "approved": true,
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                    "affiliations": [
                        {
                            "id": 154,
                            "ror": "https://ror.org/00ysfqy60",
                            "name": "Oregon State University",
                            "address": "",
                            "city": "",
                            "state": "OR",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
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                "awardee_organization": {
                    "id": 154,
                    "ror": "https://ror.org/00ysfqy60",
                    "name": "Oregon State University",
                    "address": "",
                    "city": "",
                    "state": "OR",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this CAREER award, the Chemistry of Life Processes Program and the Chemical Structure and Dynamics-A Program in the Chemistry Division are funding Dr. Chong Fang from Oregon State University to study the fluorescence mechanisms of emerging fluorescent protein biosensors. These colorful biomolecules originally derived from jellyfish and later from reef corals have revolutionized cellular imaging and molecular biology for almost two decades. However, these biosensors still suffer from drawbacks such as limited photostability, brightness, penetration depth, and color contrast, which hinder their further applications in physical and life sciences. The bottleneck in improving their functionality is the very limited information available about the underlying structural dynamics of fluorescent proteins, which involve a highly dynamic chromophore in the center of the protein pocket. This pursuit will provide graduate and undergraduate students as well as postdoctoral scholars the opportunity to acquire specialized training in ultrafast spectroscopy, particularly in the molecular vibrational domain, and in biophysical chemistry. The new femtosecond Raman spectroscopic method for fluorescent protein studies, followed by curriculum development and outreach workshops to impact young minds, will yield molecular \"movies\" showing how the embedded chromophore responds to light and choreographs the departure of a single proton or the swing of an aromatic ring. This project will also provide integrated educational programs to create an interactive and sustainable culture of engagement for STEM learners.\n\nThe scientific focus of the research is to elucidate the chromophore motions that control the fluorescence characteristics of proteins related to Green Fluorescent Proteins (GFPs) and of biosensors using newly developed, high resolution, and broadly tunable femtosecond stimulated Raman spectroscopic techniques. The structural evolution of the photoexcited chromophore will be monitored by transient vibrational peaks starting from time zero, quantified by kinetic analysis yielding crucial time constants and accompanied by computational chemistry to map atomic trajectories. The functional relevance of low-frequency skeletal motions along the multidimensional reaction coordinate, especially on the subpicosecond timescale, will be studied. Currently a phenolic ring wagging motion in wild-type GFP has been found to gate excited state proton transfer; the new experiments will make possible the systematic evaluation of governing factors for the chromophore conformational dynamics and emission outcomes in emerging GFP-related biosensors. Insights from this study will enrich physical chemistry and biophysics, and have the potential to guide the rational design of next-generation FP-biosensors with improved properties.",
                "keywords": [],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "6074",
            "attributes": {
                "award_id": "1K38AI163480-01",
                "title": "Systems Biology Approach to SARS-CoV-2 Infection in Individuals with known COVID-19 Contacts: A Prospective Cohort Study",
                "funder": {
                    "id": 4,
                    "ror": "https://ror.org/01cwqze88",
                    "name": "National Institutes of Health",
                    "approved": true
                },
                "funder_divisions": [
                    "National Institute of Allergy and Infectious Diseases (NIAID)"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 20693,
                        "first_name": "Roya",
                        "last_name": "Kalantari",
                        "orcid": null,
                        "emails": "",
                        "private_emails": "",
                        "keywords": null,
                        "approved": true,
                        "websites": null,
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                        "comments": null,
                        "affiliations": []
                    }
                ],
                "start_date": "2021-09-07",
                "end_date": "2023-08-31",
                "award_amount": 108886,
                "principal_investigator": {
                    "id": 20694,
                    "first_name": "Nicholas",
                    "last_name": "Scanlon",
                    "orcid": null,
                    "emails": "",
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                    "approved": true,
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                    "affiliations": [
                        {
                            "id": 265,
                            "ror": "https://ror.org/03czfpz43",
                            "name": "Emory University",
                            "address": "",
                            "city": "",
                            "state": "GA",
                            "zip": "",
                            "country": "United States",
                            "approved": true
                        }
                    ]
                },
                "other_investigators": [],
                "awardee_organization": {
                    "id": 265,
                    "ror": "https://ror.org/03czfpz43",
                    "name": "Emory University",
                    "address": "",
                    "city": "",
                    "state": "GA",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this K38 Mentored Stimulating Access to Research in Residency Transition Scholar (StARRTS) award, I will develop the necessary skills to become an independently funded clinician-scientist, working at the intersection of immunology, systems biology, and vaccinology. My longstanding commitment to translational and clinical research provides me with the foundation for this work. During this Award, I will be mentored by Dr. Nadine Rouphael, an expert in translational immunology, who is interim director of the Hope Clinic, the clinical arm of the Emory Vaccine Center, Dr. Bali Pulendran, an expert in systems biology at Stanford University, Dr. Erin Scherer, an expert in B-cell biology and director of the Hope Clinic Vaccine and Treatment Evaluation Unit (VTEU) Research Laboratory, and Dr. Christina Mehta, an expert in applied biostatistics in the Department of Biostatistics and Bioinformatics at the Rollins School of Public Health of Emory University. I will have hands on clinical research and biostatistical training as well as training in laboratory methods related to systems biology, and will attend workshops in the field. Currently, I am enrolling subjects for my R38 research year and using the combined diagnostic methods of anti-SARS-CoV-2 IgM/IgG testing and symptom-driven SARS-CoV-2 PCR testing to better identify individuals with asymptomatic and mild COVID-19. We hypothesize that a systems biology approach will identify specific baseline immunologic signatures, which predict COVID-19 disease acquisition and severity and that mild and asymptomatic COVID-19 will be characterized by a specific innate and adaptive immune responses. We propose a cohort study to complete the following aims: 1) To identify baseline immunologic markers predictive of COVID-19 disease acquisition and severity, and 2) To characterize the innate and adaptive immune responses to SARS-CoV-2 in individuals with asymptomatic and mildly symptomatic COVID-19. Completion of these aims will provide a better understanding of COVID-19 and position me to transition to independence as a clinician-scientist.",
                "keywords": [
                    "2019-nCoV",
                    "Antibodies",
                    "Antibody Response",
                    "Antibody titer measurement",
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                    "B-Lymphocytes",
                    "Binding",
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                    "Biological Assay",
                    "Biometry",
                    "Blood",
                    "CD4 Positive T Lymphocytes",
                    "CD8-Positive T-Lymphocytes",
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                    "COVID-19 diagnosis",
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                    "skills",
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                    "training opportunity",
                    "transcriptome",
                    "transcriptome sequencing",
                    "vaccinology"
                ],
                "approved": true
            }
        },
        {
            "type": "Grant",
            "id": "10268",
            "attributes": {
                "award_id": "1R13OD034052-01",
                "title": "Annual Symposium on Nonhuman Primates",
                "funder": {
                    "id": 4,
                    "ror": "https://ror.org/01cwqze88",
                    "name": "National Institutes of Health",
                    "approved": true
                },
                "funder_divisions": [
                    "NIH Office of the Director"
                ],
                "program_reference_codes": [],
                "program_officials": [
                    {
                        "id": 6567,
                        "first_name": "MATTHEW ERIN",
                        "last_name": "Arnegard",
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                        "emails": "",
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                        "approved": true,
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                    }
                ],
                "start_date": "2022-08-15",
                "end_date": "2025-08-14",
                "award_amount": 74999,
                "principal_investigator": {
                    "id": 26221,
                    "first_name": "R. PAUL",
                    "last_name": "JOHNSON",
                    "orcid": null,
                    "emails": "",
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                    "approved": true,
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                },
                "other_investigators": [
                    {
                        "id": 6569,
                        "first_name": "JAY",
                        "last_name": "RAPPAPORT",
                        "orcid": null,
                        "emails": "",
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                            {
                                "id": 811,
                                "ror": "",
                                "name": "TULANE UNIVERSITY OF LOUISIANA",
                                "address": "",
                                "city": "",
                                "state": "LA",
                                "zip": "",
                                "country": "United States",
                                "approved": true
                            }
                        ]
                    },
                    {
                        "id": 22870,
                        "first_name": "JOHN H",
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                ],
                "awardee_organization": {
                    "id": 265,
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                    "name": "Emory University",
                    "address": "",
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                    "state": "GA",
                    "zip": "",
                    "country": "United States",
                    "approved": true
                },
                "abstract": "With this R13 application, we request funding to support, in part, the costs for planning, publicizing, and hosting the 39th, 40th, and 41st Annual Symposia on Nonhuman Primate Models for AIDS. For four decades, this symposium has served as the premier scientific forum for the exchange of information, including new research findings and scientific perspectives, among HIV/AIDS investigators whose research includes studies in nonhuman primates (NHPs). Disseminating the latest research findings in NHP models of AIDS while also facilitating discussion and exchange of information between basic scientists and clinicians remains a priority, as do focusing on emerging technologies to accelerate translation of NHP studies into the clinic and engaging a broader and more diverse group of researchers in HIV/AIDS research in NHP models. This meeting, the only one of its kind in the world, convenes an international group of scientists whose research focuses on the study of natural and experimental immunodeficiency virus infections in NHPs, as well as on the development of novel therapeutics, prophylactic vaccines for HIV, and curative approaches. Emerging topics in related infectious diseases (such as COVID-19 pathogenesis, vaccines and treatment) may also be included. The seven National Primate Research Centers (NPRCs) host this meeting in rotation, and upcoming symposia hosts will be the Yerkes (2022), California (2023), and Tulane (2024) NPRCs. We plan a hybrid format with most participants attending in person and others joining online to access oral and poster sessions. The conference will begin on day 1 with registration, a keynote address by a leading HIV/AIDS researcher, and an evening reception. The following two and a half days will include scientific presentations from invited speakers and accepted oral abstracts. Each symposium scientific committee will select session topics and speakers to highlight new and cutting-edge technologies in their respective fields. Each session will open with a 30-minute talk by an invited chair. Individuals whose abstracts are accepted for oral presentations will give the remaining session talks. A poster session will occur on the evening of day 2, and there will be a banquet on the evening of day 3. As is traditional for this symposium, the Journal of Medical Primatology will publish all poster and oral abstracts in a special issue. In partnership with the HIV Vaccine Trials Network (HVTN), the NHP AIDS Symposium will also host a pre-symposium meeting for early stage investigators (ESI). This meeting will be open to the attendees of a linked ESI Conference the HVTN sponsors. ESI attendees and mentors will focus on grant writing, budgeting, and networking, and will participate in a Q&A with NIH Program Officers. We believe bringing together researchers from a variety of diverse backgrounds will generate future collaborations and scientific advances. Knowledge shared and gained at upcoming Annual Nonhuman Primate Models for AIDS Symposia will further the continued, effective use of NHP models to maintain long term control of HIV replication in the absence of antiretroviral therapy and to design interventions to prevent or eradicate HIV infection.",
                "keywords": [
                    "AIDS Vaccines",
                    "AIDS/HIV problem",
                    "Acquired Immunodeficiency Syndrome",
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                ],
                "approved": true
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        },
        {
            "type": "Grant",
            "id": "5975",
            "attributes": {
                "award_id": "1R43AI157578-01",
                "title": "Preclinical Development of GV-MVA-VLP Vaccines Against COVID-19",
                "funder": {
                    "id": 4,
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                "funder_divisions": [
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                    {
                        "id": 20446,
                        "first_name": "Erik J.",
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                ],
                "start_date": "2021-01-05",
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                "award_amount": 299927,
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                    "id": 20447,
                    "first_name": "Mark",
                    "last_name": "Newman",
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                "awardee_organization": {
                    "id": 1212,
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                    "name": "GEOVAX, INC.",
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                "abstract": "With unprecedented speed and scale, SARS-CoV-2 has caused a deadly global pandemic. A safe and effective vaccine to control this new pathogen is desperately needed. To address this need, GeoVax is leveraging its unique GV-MVA-VLPTM platform and advanced antigen design to develop multiple vaccine candidates against COVID-19. Unique among COVID-19 vaccines, the GeoVax candidates are specifically designed to provide highly protective immunity against SARS-CoV-2 while avoiding antibody-dependent enhancement (ADE) and immunopathology that have the potential to render vaccines not only ineffective but actually dangerous. In addition to the identification of the final vaccine candidate, the work proposed here will generate scientific data that are extremely valuable to the overall field of COVID-19 vaccine development, in that testing of our unique vaccines will determine whether application of our approach is able to overcome the ADE and immunopathology risks that plagued SARS vaccines. Under Specific Aim 1, we will complete the construction of GEO-CM02 through GEO-CM04 vaccine candidates. We will then test these candidates to demonstrate antigen expression, manufacturability, formation of VLPs, and genetic stability under conditions designed to simulate those in manufacturing, which will demonstrate the suitability of each vaccine construct as a candidate for full-scale production. Finally, we will produce adequate amount of each vaccine to enable the animal studies planned in Specific Aim 2 and ship the vaccines to our collaborators at the University of Texas Medical Branch. Under Specific Aim 2, we will then perform an immunogenicity and efficacy study in mice transgenic for human angiotensin converting enzyme 2 (hACE2). The hACE2 transgenic mouse model is a rigorous animal model developed for SARS that is well suited for testing of human coronaviruses. We will immunize animals, sample the animals for analysis of immune responses, challenge the animals with SARS-CoV-2, and monitor the animals post-challenge for development of clinical signs of disease. Under Specific Aim 3, we will analyze samples from the hACE2 mouse study to assess the immunogenicity, efficacy and safety (ADE and immunopathology) of our vaccine candidates. Immunogenicity analyses will include binding antibody (BAb) by ELISA, neutralizing antibody (NAb) by serum neutralization assay, antibody-dependent cellular cytotoxicity (ADCC) by cell-based assay, and T cell responses by intracellular cytokine screening (ICS). Efficacy analyses will include viral load and histopathology relative to unvaccinated controls. We will also analyze serum and tissue samples for evidence of ADE and immunopathology to test the hypothesis that our vaccines will avoid these risks associated with SARS vaccines. All these parameters will help to down select the most immunogenic (inducing broad Ab and T cell responses) and safe (lack of ADE and immunopathology upon challenge) vaccine candidate for further testing in non-human primates and Phase 1 human trials.",
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