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RESEARCH
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Pascal Egea, Ph.D.
Contact Information:
Lab Number:
310 983-3516
Office Phone Number:
310-983-3515
Mailing Address:
Box 951737 BSRB 330 615 Charles E. Young Drive South Los Angeles, CA 90095 UNITED STATES
Office Address:
Boyer Hall room 356 611 Charles E Young Drive East Los Angeles, CA 90095 UNITED STATES
Assistant Professor,
Biological Chemistry
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Member,
ACCESS Program: Dept. of Biological Chemistry
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A Short Biography:
Pascal Egea received is B.S. in Molecular and Cellular Biology from the Ecole Normale Supérieure de Lyon (Lyon, France) in 1991. He then went to graduate school at the Université Louis Pasteur (Strasbourg, France) where he studied the structure and function of the retinoic acid receptors in the laboratory of Dr Dino Moras. After completing is Ph.D. in 1999, Pascal went to the University of California in San Francisco for post-doctoral training under the co-mentorship of Professors Robert Stroud and Peter Walter; during this period he studied the signal recognition particle and protein translocation pathways. Pascal joined the Department of Biological Chemistry as an assistant professor in the fall of 2009.
Detailed Biography:
Pascal Egea received is B.S. in Molecular and Cellular Biology from the Ecole Normale Supérieure de Lyon (Lyon, France) in 1991. He then went to graduate school at the Université Louis Pasteur (Strasbourg, France) where he studied the structure and function of the retinoic acid receptors in the laboratory of Dr Dino Moras. After completing is Ph.D. in 1999, Pascal went to the University of California in San Francisco for post-doctoral training under the co-mentorship of Professors Robert Stroud and Peter Walter; during this period he studied the signal recognition particle and protein translocation pathways. Pascal joined the Department of Biological Chemistry as an assistant professor in the fall of 2009.
Egea Pascal F, Muller-Steffner Hélène, Kuhn Isabelle, Cakir-Kiefer Céline, Oppenheimer Norman J, Stroud Robert M, Kellenberger Esther, Schuber Francis Insights into the mechanism of bovine CD38/NAD+glycohydrolase from the
X-ray structures of its michaelis complex and covalently-trapped
intermediates..
PloS one.
2012;
7(4):
e34918.
Korennykh Alexei V, Egea Pascal F, Korostelev Andrei A, Finer-Moore Janet, Stroud Robert M, Zhang Chao, Shokat Kevan M, Walter Peter Cofactor-mediated conformational control in the bifunctional
kinase/RNase Ire1..
BMC biology.
2011;
9:
48.
Korennykh Alexei V, Korostelev Andrei A, Egea Pascal F, Finer-Moore Janet, Stroud Robert M, Zhang Chao, Shokat Kevan M, Walter Peter Structural and functional basis for RNA cleavage by Ire1..
BMC biology.
2011;
9:
47.
Egea, P. F. Napetschnig, J. Walter, P. Stroud, R. M. Structures of SRP54 and SRP19, the two proteins that organize the ribonucleic core of the signal recognition particle from Pyrococcus furiosus.
PLoS One.
2008;
3(10):
e3528.
Egea, P. F. Tsuruta, H. de Leon, G. P. Napetschnig, J. Walter, P. Stroud, R. M. Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.
PLoS One.
2008;
3(11):
e3619.
Egea, P. F. Stroud, R. M. Walter, P. Targeting proteins to membranes: structure of the signal recognition particle.
Curr Opin Struct Biol.
2005;
15(2):
213-20.
Savage, D. F. Egea, P. F. Robles-Colmenares, Y. O'Connell, J. D., 3rd Stroud, R. M. Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z.
PLoS Biol.
2003;
1(3):
E72.
Egea, P. F. Mitschler, A. Moras, D. Molecular recognition of agonist ligands by RXRs.
Mol Endocrinol.
2002;
16(5):
987-97.
Rochel, N. Tocchini-Valentini, G. Egea, P. F. Juntunen, K. Garnier, J. M. Vihko, P. Moras, D. Functional and structural characterization of the insertion region in the ligand binding domain of the vitamin D nuclear receptor.
Eur J Biochem.
2001;
268(4):
971-9.
Egea, P. F. Moras, D. Purification and crystallization of the human RXRalpha ligand-binding domain-9-cisRA complex.
Acta Crystallogr D Biol Crystallogr.
2001;
57(Pt 3):
434-7.
Brown Christopher M, Ray Manisha, Eroy-Reveles Aura A, Egea Pascal, Tajon Cheryl, Craik Charles S Peptide length and leaving-group sterics influence potency of peptide
phosphonate protease inhibitors..
Chemistry & biology.
2011;
18(1):
48-57.
Korennykh, A. V. Egea, P. F. Korostelev, A. A. Finer-Moore, J. Zhang, C. Shokat, K. M. Stroud, R. M. Walter, P. The unfolded protein response signals through high-order assembly of Ire1.
Nature.
2009;
457(7230):
687-93.
Farady, C. J. Egea, P. F. Schneider, E. L. Darragh, M. R. Craik, C. S. Structure of an Fab-protease complex reveals a highly specific non-canonical mechanism of inhibition.
J Mol Biol.
2008;
380(2):
351-60.
Chu, F. Shan, S. O. Moustakas, D. T. Alber, F. Egea, P. F. Stroud, R. M. Walter, P. Burlingame, A. L. Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.
Proc Natl Acad Sci U S A.
2004;
101(47):
16454-9.
Egea, P. F. Shan, S. O. Napetschnig, J. Savage, D. F. Walter, P. Stroud, R. M. Substrate twinning activates the signal recognition particle and its receptor.
Nature.
2004;
427(6971):
215-21.
Egea, P. F. Rochel, N. Birck, C. Vachette, P. Timmins, P. A. Moras, D. Effects of ligand binding on the association properties and conformation in solution of retinoic acid receptors RXR and RAR.
J Mol Biol.
2001;
307(2):
557-76.
Egea, P. F. Klaholz, B. P. Moras, D. Ligand-protein interactions in nuclear receptors of hormones.
FEBS Lett.
2000;
476(1-2):
62-7.
Egea, P. F. Mitschler, A. Rochel, N. Ruff, M. Chambon, P. Moras, D. Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid.
Embo J.
2000;
19(11):
2592-601.
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