Structural and Chemical Biology Research Program
Overview
The goal of the Program in Structural and Chemical Biology is to provide a molecular description and interpretation of biological processes associated with oncogenesis and tumor progression. Together, the tools of structural and chemical biology permit investigation of fundamental aspects of cancer biology, the design of small molecule probes for biological discovery, the design and synthesis of small molecule therapeutics, and development of novel molecular and cellular technologies. Program members include those with expertise in organic synthesis, chemical biology, X-ray crystallography and NMR analyses, enzymology, and modeling at the molecular level. Program members provide valuable consultation and technology to other Cancer Center investigators who have identified molecules involved in cellular transformation, and this serves to stimulate the exchange of technology and expertise between members of the Program as well as with other members of the Cancer Center. Program members have provided the leadership for a number of initiatives that have markedly enhanced the technological capabilities available to the cancer community at Duke, including the upgrade and expansion of our X-ray crystallography and NMR facility, establishment of a state-of-the-art proteomics facility, and the establishment of core facilities that provide small molecule synthetic capabilities and enable high-throughput screening of small molecule libraries. The Program includes 21 members from 6 basic and clinical departments within Duke University. From 2004-2008, program members published 868 papers in peer-reviewed journals cited in PubMed. Of these publications, 4.7% are the result of intra-programmatic collaborations and 4.4% due to inter-programmatic collaborations.
High-Impact Journal Publications
Below are recent publications in high-impact journals from Cancer Center members in this program. To see journal articles for a particular member, click on the researcher's name in the
Membership section.
Gao W,Liu W,Mackay JA,Zalutsky MR,Toone EJ,Chilkoti A. In situ growth of a stoichiometric PEG-like conjugate at a protein's N-terminus with significantly improved pharmacokinetics., . Proceedings of the National Academy of Sciences of the United States of America
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Hammes GG,Chang YC,Oas TG. Conformational selection or induced fit: a flux description of reaction mechanism., , (13737-41) - Proceedings of the National Academy of Sciences of the United States of America
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Hamburger JB,Hoertz AJ,Lee A,Senturia RJ,McCafferty DG,Loll PJ. A crystal structure of a dimer of the antibiotic ramoplanin illustrates membrane positioning and a potential Lipid II docking interface., , (13759-64) - Proceedings of the National Academy of Sciences of the United States of America
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Zidar DA,Violin JD,Whalen EJ,Lefkowitz RJ. Selective engagement of G protein coupled receptor kinases (GRKs) encodes distinct functions of biased ligands., , (9649-54) - Proceedings of the National Academy of Sciences of the United States of America
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Erickson HP. Modeling the physics of FtsZ assembly and force generation., , (9238-43) - Proceedings of the National Academy of Sciences of the United States of America
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Shenoy SK,Modi AS,Shukla AK,Xiao K,Berthouze M,Ahn S,Wilkinson KD,Miller WE,Lefkowitz RJ. Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2., , (6650-5) - Proceedings of the National Academy of Sciences of the United States of America
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Augustus AM,Reardon PN,Spicer LD. MetJ repressor interactions with DNA probed by in-cell NMR., . Proceedings of the National Academy of Sciences of the United States of America
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Ma B,Reynolds CM,Raetz CR. Periplasmic orientation of nascent lipid A in the inner membrane of an Escherichia coli LptA mutant., , (13823-8) - Proceedings of the National Academy of Sciences of the United States of America
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Frederick JP,Tafari AT,Wu SM,Megosh LC,Chiou ST,Irving RP,York JD. A role for a lithium-inhibited Golgi nucleotidase in skeletal development and sulfation., , (11605-12) - Proceedings of the National Academy of Sciences of the United States of America
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Shukla AK,Violin JD,Whalen EJ,Gesty-Palmer D,Shenoy SK,Lefkowitz RJ. Distinct conformational changes in {beta}-arrestin report biased agonism at seven-transmembrane receptors., . Proceedings of the National Academy of Sciences of the United States of America
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Click here for these and other high-impact publications in this research program.