Structural biologists map the architecture of individual proteins as well as multi-protein complexes and use that information to understand the structure, function, and dynamic interactions of those proteins and complexes. At atomic and molecular resolutions, structural data help scientists rationally design new molecules that selectively modulate the activity of particular proteins. Such inhibitors or activators serve as research tools that allow investigators to study protein activity in living cells or can, in some cases, be developed into new drugs to treat human disease in a targeted manner. Researchers in these areas at Einstein has made considerable investments in instrumentation and infrastructure to build a state-of-the-art program in structural biology using NMR, and a 16 y old instrument is seriously in need of upgrading to contemporary performance and reliability. The upgrade of the console controller and probe for signal detection will increase the throughput for this instrument by more than four fold. The 10 major users and many other users in structural biology, enzymology, and chemical biology will be significantly aided in their NIH funded research in multiple areas of disease and therapeutics. Specific areas include antimicrobials, cancer therapeutics for tumor metastasis, antivirals, cardiac degeneration, Alzheimer's, and reproductive health.

National Institute of Health (NIH)
Office of The Director, National Institutes of Health (OD)
Biomedical Research Support Shared Instrumentation Grants (S10)
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Special Emphasis Panel (ZRG1)
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Levy, Abraham
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Albert Einstein College of Medicine
Schools of Medicine
United States
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Hayama, Ryo; Sparks, Samuel; Hecht, Lee M et al. (2018) Thermodynamic characterization of the multivalent interactions underlying rapid and selective translocation through the nuclear pore complex. J Biol Chem 293:4555-4563
Wang, Ting; Cook, Ian; Leyh, Thomas S (2017) The NSAID allosteric site of human cytosolic sulfotransferases. J Biol Chem 292:20305-20312
Upla, Paula; Kim, Seung Joong; Sampathkumar, Parthasarathy et al. (2017) Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25:434-445
Reyna, Denis E; Garner, Thomas P; Lopez, Andrea et al. (2017) Direct Activation of BAX by BTSA1 Overcomes Apoptosis Resistance in Acute Myeloid Leukemia. Cancer Cell 32:490-505.e10
Warren, Christopher; Matsui, Tsutomu; Karp, Jerome M et al. (2017) Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. Nat Commun 8:2215
Stevens, Adam J; Sekar, Giridhar; Shah, Neel H et al. (2017) A promiscuous split intein with expanded protein engineering applications. Proc Natl Acad Sci U S A 114:8538-8543
Uchime, Onyinyechukwu; Dai, Zhou; Biris, Nikolaos et al. (2016) Synthetic Antibodies Inhibit Bcl-2-associated X Protein (BAX) through Blockade of the N-terminal Activation Site. J Biol Chem 291:89-102
Xia, Yumin; Eryilmaz, Ertan; Zhang, Qiuting et al. (2016) Anti-DNA antibody mediated catalysis is isotype dependent. Mol Immunol 69:33-43
Cook, Ian; Wang, Ting; Girvin, Mark et al. (2016) The structure of the catechin-binding site of human sulfotransferase 1A1. Proc Natl Acad Sci U S A 113:14312-14317
Garner, Thomas P; Reyna, Denis E; Priyadarshi, Amit et al. (2016) An Autoinhibited Dimeric Form of BAX Regulates the BAX Activation Pathway. Mol Cell 63:485-97

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