Philip Yeagle

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Professor Emeritus

University of Connecticut
Department of Molecular & Cell Biology
91 North Eagleville Road, Unit 3125
Storrs, CT 06269-3125
Torrey Life Sciences 281H

Telephone: 860-486-6296
Fax: 860- 486-4331
philip.yeagle@uconn.edu

 

Education: B.A. St. Olaf College, Ph.D. Duke University, Postdoc, University of Virginia

Research Interests: Critical problems of membrane protein structure.

Selected Publications:

“Cell Membrane Specializations”, P.L. Yeagle, Encyclopedia of Life Sciences, Wiley, London, in press

“Lipids,” P.L. Yeagle, In: eLS. John Wiley & Sons, Ltd: Chichester (2014) http://www.els.net/ [DOI: 10.1002/9780470015902.a0000711.pub3]

“Non-covalent binding of membrane lipids to membrane proteins,” Philip Yeagle, Biochemica et Biophysica Acta Biomembranes, 1838, 1548–1559 (2014). [10.1016/j.bbamem.2013.11.009]

“Aggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization”, AC Brown, K Boesze-Battaglia, Y Du, FP Stefano, IR Kieba, RF Epand, L Kakalis, PL Yeagle, RM Epand, ET Lally, Cell Microbiol. 14, 869-891 (2012).

“Toward 3D structure of membrane proteins from peptide fragments”, Arlene D. Albert & Philip L.Yeagle, Methods in Molecular Biology, 654, 283-303, Humana Press (2010).

“Cell Membrane Specializations”, P.L. Yeagle, Encyclopedia of Life Sciences, Wiley, London (2010).

“Lipids”, P.L. Yeagle, In: ENCYCLOPEDIA OF LIFE SCIENCES. John Wiley & Sons, Ltd: Chichester http://www.els.net/[DOI: 10.1002/9780470015902.a0000711.pub2] (2009).

“A Small Subset of Signal Peptidase Residues are Perturbed by Signal Peptide Binding”, Monika Musial-Siwek,Philip L. Yeagle,& Debra A. Kendall, Chem. Biol. & Drug Design, 72, 140-146 (2008).

“Solution NMR of signal peptidase, a membrane protein,”M Musial-Siwek, DA Kendall, and PL Yeagle, Biochim Biophys Acta,  1778, 937-44 (2008).

“Three dimensional structures of GPCRs”, Arlene D. Albert and Philip L. Yeagle Biochim. Biophys.Acta, 1768, 808-824 (2007).

“Transmembrane helices may flex to satisfy hydrophobic mismatch,” Michael Bennett, Vincent Lemaître, Anthony Watts and Philip L. Yeagle, Biochim. Biophys. Acta, 1768, 530-537 (2007).

“The tetraspannin protein, peripherin-2, complexes with melanoregulin, a putative membrane fusion regulator”, Kathleen Boesze-Battaglia, Lisa Pankoski-Walker, Cheryl Gretzula, Linda Otis, Bridget Gallagher, Rivka A. Rachel, Nancy A. Jenkins, Neal G. Copeland, Francine Morris, Philip Yeagle and Monika Damek-Poprawa, Biochemistry, 46 1256 – 1272 (2007).

“Peripherin-2: an intracellular analogy to viral fusion proteins”, T. Edrington, R. Lapointe, P.L. Yeagle, Cheryl L. Gretzula, and K. Boesze-Battaglia, Biochemistry, 46 3605-3613 (2007).

“Calcium dependent association of calmodulin with the C-terminal domain of the tetraspannin protein peripherin/rds”, T.C. Edrington V, P.L. Yeagle, Cheryl L. Gretzula, and K. Boesze-Battaglia, Biochemistry, 46, 3862-3871 (2007).

“Differential stability among the transmembrane helices of lactose permease may be important to transport”, Michael Bennett, Robert d’Rozario, Mark Sansom and Philip L. Yeagle, Biochemistry, 45, 8088-8095 (2006).

“Insight into membrane protein structure from high resolution NMR”, Modern Magnetic Resonance, Graham A. Webb, ed. Springer, p331-339 (2006).

“Molecular Dynamic Simulations Of Retinal In Rhodopsin: From The Dark-Adapted State Towards Lumirhodopsin,” Vincent Lemaître, Philip L.Yeagle, & Anthony Watts, Biochemistry44, 12667-80(2005).

“Structural studies of the putative helix 8 in the human β2 adrenergic receptor: an NMR study”, M. Katragadda, M.W. Maciejewski, and P.L. Yeagle, Biochim. Biophys. Acta, 1663, 74-81, (2004).

“Stability of loops in the structure of lactose permease”, Michael Bennett, James A. Yeagle, Mark Maciejewski, James Ocampo, and P. L. Yeagle, Biochemistry, 43, 12829-12837, (2004).

“A conformational trigger for the activation of a G protein by a G protein coupled receptor”, Philip L. Yeagle and Arlene D. Albert, Biochemistry, 42, 1365-1368 (2003).

“Structural studies of Metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin”, Gregory Choi, Judith Landin, Jhenny Flor Galan, Robert R. Birge, Arlene D. Albert and Philip L. Yeagle, Biochemistry, 41, 7318-7324 (2002).

“Use of NMR to study the three dimensional structure of rhodopsin, A. D. Albert and P. L. Yeagle, Methods in Enzymology, v343, 223-231 (2002).

“Structural studies on rhodopsin”, Arlene D. Albert and Philip L. Yeagle, Biochim. Biophys. Acta.1565,183-195 (2002).

“Structures of the Transmembrane Helices of the G-protein Coupled Receptor, Rhodopsin”, Madan Katragadda, Atin Chopra, Michael Bennett, James L. Alderfer, Philip L. Yeagle and Arlene D. Albert, J. Peptide Res., 58: 79-89 (2001).

“Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin”, Madan Katragadda, James L. Alderfer and Philip L. Yeagle, Biophys. J. 81: 1029-1036 (2001).

“Studies on the structure of the G-protein coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms”, Philip L. Yeagle, Gregory Choi, and Arlene D. Albert, Biochemistry, 40, 11932-11937 (2001).

Selected Books:

Reference book, entitled “Structure of Biological Membranes, 2nd edition”, P.L. Yeagle, (editor), CRC Press, Boca Raton, 2004 (ISBN 0-8493-1403-8).

Reference book, entitled “Structure of Biological Membranes, 3rd edition”, P.L. Yeagle, (editor), CRC Press, Boca Raton, 2012 (ISBN 9781439809570).

Textbook, entitled “The Membranes of Cells, 3rd edition, under contract with Academic Press, P.L. Yeagle (sole author).

Essays:

On hindsight and gratitude, Philip Yeagle, ASBMB Today, 13, p18 (2014)

Blogs:

http://www.huffingtonpost.com/dr-philip-l-yeagle/public-universities-tuition_b_2234314.html

http://www.huffingtonpost.com/dr-philip-l-yeagle/federal-college-ratings_b_3948253.html