We have organized the Consortium Administrative Core based on the premise that productive collaborations do not necessarily require physically proximity. However, to nurture and maximize their collective output the proper leadership and administrative structure must be in place. We recognize a need to set in place an effective environment to foster the full engagement of each investigator and their staffs in the total science picture and to provide the scope of resources that not only facilitates, but also enhances individual research. Thus, the key motivation behind the organization of the present administrative structure is "efficient integration". This integrafion will be key to our hwo major goals: promofing the highest quality science and fostering breakthroughs in the projects that bind us together, as well as maximizing the Consortium's impact by disseminafing advances in membrane protein structure and dynamics within and beyond its virtual walls.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Specialized Center--Cooperative Agreements (U54)
Project #
Application #
Study Section
Special Emphasis Panel (ZGM1-CBB-3)
Project Start
Project End
Budget Start
Budget End
Support Year
Fiscal Year
Total Cost
Indirect Cost
University of Chicago
United States
Zip Code
Poudel, Kumud R; Dong, Yongming; Yu, Hang et al. (2016) A time course of orchestrated endophilin action in sensing, bending, and stabilizing curved membranes. Mol Biol Cell 27:2119-32
Tian, Yutao; Aursnes, Marius; Hansen, Trond Vidar et al. (2016) Atomic determinants of BK channel activation by polyunsaturated fatty acids. Proc Natl Acad Sci U S A 113:13905-13910
Tong, Jihong; Wu, Zhe; Briggs, Margaret M et al. (2016) The Water Permeability and Pore Entrance Structure of Aquaporin-4 Depend on Lipid Bilayer Thickness. Biophys J 111:90-9
McCoy, Jason G; Ren, Zhenning; Stanevich, Vitali et al. (2016) The Structure of a Sugar Transporter of the Glucose EIIC Superfamily Provides Insight into the Elevator Mechanism of Membrane Transport. Structure 24:956-64
Khelashvili, George; Schmidt, Solveig Gaarde; Shi, Lei et al. (2016) Conformational Dynamics on the Extracellular Side of LeuT Controlled by Na+ and K+ Ions and the Protonation State of Glu290. J Biol Chem 291:19786-99
Laguerre, Aisha; Löhr, Frank; Henrich, Erik et al. (2016) From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins. Structure 24:1830-1841
Castillo, Juan P; Sánchez-Rodríguez, Jorge E; Hyde, H Clark et al. (2016) β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel. Proc Natl Acad Sci U S A 113:E3231-9
Zhu, Shujia; Stein, Richard A; Yoshioka, Craig et al. (2016) Mechanism of NMDA Receptor Inhibition and Activation. Cell 165:704-14
Lee, Hui Sun; Im, Wonpil (2016) G-LoSA: An efficient computational tool for local structure-centric biological studies and drug design. Protein Sci 25:865-76
Arrigoni, Cristina; Rohaim, Ahmed; Shaya, David et al. (2016) Unfolding of a Temperature-Sensitive Domain Controls Voltage-Gated Channel Activation. Cell 164:922-36

Showing the most recent 10 out of 196 publications