Pascal F. EGEA
University of California San Francisco Medical Center, Université de Strasbourg, École Normale Supérieure de Lyon
Research areas: Biochemistry, Genetics and Molecular Biology · Molecular Biology · Enzyme Structure and Function · Protein Structure and Dynamics · RNA and protein synthesis mechanisms
0000-0003-4432-8625
About
Pascal is a protein chemist and structural biologist with a passion for understanding how changes in the structure and function of molecules and biological membranes affect cellular health in the context of disease or aging.
He earned his PhD in Structural Biology and Molecular Biophysics in France, where he studied structure–function relationships in retinoic acid receptors. He further developed his expertise in protein crystallography and membrane protein biochemistry during his postdoctoral training in the laboratories of Robert Stroud and Peter Walter at UCSF, where he elucidated key molecular mechanisms of membrane protein targeting and biogenesis by the signal recognition particle and its associated translocon, as well as the structure of the UPR sensor Ire1. He then joined the faculty at UCLA, where he studied the architecture and function of ER–membrane contact sites in non-vesicular lipid transport, along with the unique mechanisms of effector protein translocation in the malarial pathogen Plasmodium falciparum. Before joining the Buck Research Institute, he briefly moved into industry, rejoining Peter Walter’s group at Altos Labs, where he contributed to several projects focused on cellular health and resilience in the context of the integrated stress response, nuclear envelope maintenance during aging, and Alzheimer’s disease.
Employment
Employment history is unavailable.
Education
-
UCSF Medical Center Post-Doctoral Fellow2001 - 2004
- 1993 - 1999
-
Université de Strasbourg DEA de Cristallographie et RMN Biologiques1991 - 1992
-
École normale supérieure de Lyon Agregation de Biochimie et Genie Biologique1990 - 1991
-
École normale supérieure de Lyon Magistere de Biologie Moleculaire et Cellulaire1988 - 1990
Projects & Funding
-
Molecular Structure and Function of an Endoplasmic Reticulum-Mitochondrion Tether National Institute of General Medical Sciences2017 - 2022
-
Towards the reconstitution and a structure of the Plasmodium vacuolar translocon National Institute of Allergy and Infectious Diseases2016 - 2019
Publications (41)
- Allosteric disordering of eIF2B regulates the integrated stress response Save
- eIF2B Selectively Anchors and Activates Mutant KRAS Save
- Retention and Rearrangement of Membrane Protein Complexes’ Higher Order Structure by Collisionally Activated Dissociation- and Electron Capture Dissociation-Mass Spectrometry Save
- Allosteric Disordering of eIF2B Regulates the Integrated Stress Response Save
- Part 1. High-Throughput Mass Spectrometry for Biopharma: A Universal Modality and Target Independent Analytical Method for Accurate Biomolecule Characterization Save
- Moving Lipids, by the Numbers Save
- Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels Save
- Highlighting membrane protein structure and function: A celebration of the Protein Data Bank. Save
- Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites Save
- Native and Denaturing MS Protein Deconvolution for Biopharma: Monoclonal Antibodies and Antibody-Drug-Conjugates to Polydisperse Membrane Proteins and Beyond Save
- Structure of the human ClC-1 chloride channel Save
- Determining the Lipid-Binding Specificity of SMP Domains: An ERMES Subunit as a Case Study Save
- Rapid LC–MS Method for Accurate Molecular Weight Determination of Membrane and Hydrophobic Proteins Save
- Malaria parasite translocon structure and mechanism of effector export Save
- Fourier Transform-Ion Cyclotron Resonance Mass Spectrometry as a Platform for Characterizing Multimeric Membrane Protein Complexes Save
- Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies Save
- Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies Save
- Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogen P lasmodium falciparum Save
- Structural mapping of the ClpBATPases of Plasmodium falciparum : Targeting protein folding and secretion for antimalarial drug design Save
- Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly Save