The past 30 years of cancer research have yielded remarkable therapeutic advances along two main fronts. “Targeted therapies” were developed against oncogenic “driver” tyrosine and serine/threonine kinases or key downstream signaling components. Concomitantly, powerful new “immune therapies,” including cell therapies and “immune checkpoint inhibitors” (e.g., anti-CTLA4, anti-PD1, anti-PDL1), emerged. These new modalities complement or replace conventional chemo- and radiation therapy, and are literally lifesaving for some patients.
The Lin lab develops theoretical models and uses computational tools to find the performance limits of complex biological systems. These systems often occupy a tiny functional fraction of a much larger space, mostly consisting of nonfunctional systems. This is true whether considering the conformational space of macromolecules or the connectivity space of neural networks. From this perspective, the conceptual challenge is to understand how the structure of the space dictates the types of search algorithms that can find the functional subspace in the relevant time-scale.
Harold Boone is the Product R&D Director for The Dow Elastomers & Polymer Processing R&D group with capabilities located in Lake Jackson, TX, and Shanghai, China. He is responsible for the development of a broad innovation portfolio focused on new olefin elastomer products and technologies. Harold joined Dow as an organic polymer chemist in 1996 in Dow’s Central Research investigating thermally stable perfluoroaryl ether polymers for interlayer dielectrics and fundamental studies of polar monomer interactions with olefin polymerization catalysts. Harold has held several sci
Glycosylation is a post-translational modification that affects cellular adhesion and host-pathogen interactions, with changes occurring during differentiation, immune response, and in cancerous tissue. Though as much as 70% of the proteome is glycosylated, determining the structure of these modifications is difficult. My research involves the expression and analysis of glycoproteins to develop a molecular understanding of how glycan heterogeneity and structure affect glycoprotein function.
Visualizing charge transfer across length scales
Erin L. Ratcliff1
1Laboratory for Interface Science of Printable Electronic Materials, Department of Materials Science and Engineering, University of Arizona, Tucson, AZ 85721
Dr Gonen is an expert in electron crystallography and cryo EM. He determined the 1.9Å resolution structure of the water channel aquaporin-0 by electron crystallography, the highest resolution for any protein determined by cryo EM techniques at the time. Dr Gonen established his own laboratory at the University of Washington in 2005 together with the very first cryo EM laboratory in the Pacific Northwest, a resource that continues to benefit many researchers at the UW School of Medicine and beyond.
Catalytic and Stoichiometric Reactivity Facilitated by New Supporting Ligands with Electropositive Metals
Department of Chemistry, University of California, Berkeley, and Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley CA 94720-1460
Abstract: Living, chain-growth methods for synthesizing conjugated polymers have the potential to access to new materials with varying sequences, lengths and end-groups. We recently used these methods to synthesize conjugated materials with random, block and gradient sequences of a poly(3-hexylthiophene) (P3HT) backbone and side-chain fullerenes (PC61BM). These polymers were evaluated as compatibilizers in photovoltaic devices with P3HT:PC61BM as the active layer.
Dr. Meanwell has led drug discovery programs in the cardiovascular, neurosciences and virology therapeutic areas, work that has resulted in the advancement of over 30 clinical candidates for the prevention of thrombosis, the treatment of stroke and therapy for viral infections, including human immunodeficiency virus-1 (HIV-1), hepatitis C virus (HCV) and respiratory syncytial virus (RSV).
Protein phosphorylation is critical for regulation in eukaryotic cells. The human genome encodes more than 500 protein kinases, making this one of the largest gene families. Although very diverse in how they receive and transmit signals, all protein kinases share a conserved catalytic core. While it is essential to understand how these enzymes function as catalysts, it is equally important to understand how they are regulated, how they function as scaffolds, and how they are localized.