Andreas Engel, Ph.D.
Professor
Phone: (216) 368-0411
Fax: (216) 368-1300
E-mail: Andreas.Engel@case.edu
RT300 Research Towers
Research:
Research concerns the structure and function of membrane proteins of different origin.
A major effort is invested in the study of aquaglyceroporins. Electron crystallography
and atomic force microscopy are used to analyze two-dimensional crystals assembled
from membrane proteins and lipids
Publications:
Selected Publications:
Braun T, Philippsen A, Wirtz S, Borgnia MJ, Agre P, Kuhlbrandt W, Engel A,
Stahlberg H: The 3.7 A projection map of the glycerol facilitator GlpF: a variant
of the aquaporin tetramer. EMBO Rep 2000, 1:183-189.
Engel A, Müller DJ: Observing single biomolecules at work with the atomic
force microscope. Nat Struct Biol 2000, 7:715-718.
Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi
Y: Structural determinants of water permeation through aquaporin-1. Nature 2000,
407:599-605.
Mantig, E.H., C. van der Does, H. Remigy, A. Engel and A. Driessen (2000).
SecYEG assembles into a tetramer to form the active protein translocation channel.
EMBO J 19, 852-861.
Oesterhelt F, Oesterhelt D, Pfeiffer M, Engel A, Gaub HE, Müller DJ: Unfolding
pathways of individual bacteriorhodopsins. Science 2000, 288:143-146.
Seelert H, Poetsch A, Dencher NA, Engel A, Stahlberg H, Müller DJ: Structural
biology. Proton-powered turbine of a plant motor. Nature 2000, 405:418-419.
Fotiadis, D., Jeno, P., Mini, T., Wirtz, S., Müller, S. A., Fraysse, L., Kjellbom,
P. & Engel, A. (2001). Structural characterization of two aquaporins isolated
from native spinach leaf plasma membranes. J Biol Chem 276, 1707-14.
Sato C, Ueno Y, Asai K, Takahashi K, Sato M, Engel A, Fujiyoshi Y: The voltage-sensitive
sodium channel is a bell-shaped molecule with several cavities. Nature 2001, 409:1047-1051.
Stahlberg H, Müller DJ, Suda K, Fotiadis D, Engel A, Meier T, Matthey U,
Dimroth P: Bacterial Na(+)-ATP synthase has an undecameric rotor. EMBO Rep 2001,
2:229-233.
Scheuring S, Müller DJ, Stahlberg H, Engel HA, Engel A: Sampling the conformational
space of membrane protein surfaces with the AFM. Eur Biophys J 2002, 31:172-178.
Fotiadis D, Liang Y, Filipek S, Saperstein DA, Engel A, Palczewski K: Atomic-force
microscopy: Rhodopsin dimers in native disc membranes. Nature 2003, 421:127-128.
Liang Y, Fotiadis D, Filipek S, Saperstein DA, Palczewski K, Engel A: Organization
of the G protein coupled receptors rhodopsin and opsin in native membranes. J Biol
Chem 2003, 278:21655-21662.
Remigy HW, Caujolle-Bert D, Suda K, Schenk A, Chami M, Engel A: Membrane
protein reconstitution and crystallization by controlled dilution. FEBS Lett 2003,
555:160-169.
Bucior I, Scheuring S, Engel A, Burger M: Carbohydrate-carbohydrate interaction
provides adhesion force and specificity for cellular recognition. J Cell Biol 2004,
165:529 - 537.
Hoogenboom, B. W., Frederix, P. L. T. M., Yang, J. L., Martin, S., Pellmont, Y.,
Steinacher, M., Zäch, S., Langenbach, E., Heimbeck, H.-J., Engel, A. & Hug,
H. J. (2005). A Fabry–Perot interferometer for micrometer-sized cantilevers. Appl.
Phys. Let. 86:74101(1-3).
Frederix , P., Gullo, M., Akiyama, T., Tonin, A., de Rooij, N., Staufer, U. & Engel,
A. (2005). Assessment of insulated conductive cantilevers for biology and electrochemistry.
Nanotechnology 16, 997-1005.
Schenk, A.D., Werten, P.J., Scheuring, S., de Groot, B.L., Müller, S.A., Stahlberg,
H., Philippsen, A., & Engel, A. (2005). The 4.5A Structure of Human AQP2.
J. Mol. Biol. 350, 278–289.
Müller, C.A. Broz, P., Müller, Ringler, P., Erne-Brand, F., Sorg, I., Kuhn, M.,
Engel, A. & Cornelis G.R. (2005). The V-Antigen of Yersinia Forms a Distinct
Structure at the Tip of Injectisome Needles. Science 310, 674-676.
Grange, W., Duckely, M., Hustle, S., Jacob, S., Engel, A. & Hegner, M. (2008).
VirE2: a unique ssDNA compacting molecular machine. PLoS, 6, e44.
Hartmann, C., Chami, M., Zachariae, U., de Groot, B., Engel, A. & Grütter,
M. (2008). Vacuolar protein sorting: Two different functional states of the AAA-ATPase
Vps4p. J Mol Biol, 377, 352-63.