Výsledky vyhledávání - "Pascal F. Egea"

Akademický článek

Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels

Autor: Pascal F. Egea

Publikováno v: Frontiers in Cell and Developmental Biology, Vol 9 (2021)

Eukaryotic cells are characterized by their exquisite compartmentalization resulting from a cornucopia of membrane-bound organelles. Each of these compartments hosts a flurry of biochemical reactions and supports biological functions such as genome s

Externí odkaz: https://doaj.org/article/df8c049d309a45dfa02b6b9946f4976b

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Akademický článek

Crossing the Vacuolar Rubicon: Structural Insights into Effector Protein Trafficking in Apicomplexan Parasites

Autor: Pascal F. Egea

Publikováno v: Microorganisms, Vol 8, Iss 6, p 865 (2020)

Apicomplexans form a large phylum of parasitic protozoa, including the genera Plasmodium, Toxoplasma, and Cryptosporidium, the causative agents of malaria, toxoplasmosis, and cryptosporidiosis, respectively. They cause diseases not only in humans but

Externí odkaz: https://doaj.org/article/691ee038151f463f80f9269502366c6b

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Native and Denaturing MS Protein Deconvolution for Biopharma: Monoclonal Antibodies and Antibody–Drug Conjugates to Polydisperse Membrane Proteins and Beyond

Autor: John O. Hui, Stone D.-H. Shi, Pascal F. Egea, John H. Robinson, Jennifer L. Lippens, Michael Nshanian, Dhanashri Bagal, Joseph A. Loo, Marshall Bern, Chawita Netirojjanakul, Iain D. G. Campuzano

Publikováno v: Analytical chemistry, vol 91, iss 15
Anal Chem

Electrospray ionization mass spectrometry (ESI-MS) is a ubiquitously used analytical method applied across multiple departments in biopharma, ranging from early research discovery to process development. Accurate, efficient, and consistent protein MS

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f7aaae0becae8f11e2aee4a6b6824f5
https://doi.org/10.1021/acs.analchem.9b00062

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Rapid LC–MS Method for Accurate Molecular Weight Determination of Membrane and Hydrophobic Proteins

Autor: Iain D. G. Campuzano, Pascal F. Egea, James E. Keener, Amit Vaish, Michael T. Marty, Joseph A. Loo, Jennifer L. Lippens, Chris Spahr

Publikováno v: Analytical Chemistry. 90:13616-13623

Therapeutic target characterization involves many components, including accurate molecular weight (MW) determination. Knowledge of the accurate MW allows one to detect the presence of post-translational modifications, proteolytic cleavages, and impor

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https://doi.org/10.1021/acs.analchem.8b03843

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Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies

Autor: Brian Lu, Duilio Cascio, Andrew P. AhYoung, Pascal F. Egea

Publikováno v: Biochemical and biophysical research communications, vol 488, iss 1
AhYoung, AP; Lu, B; Cascio, D; & Egea, PF. (2017). Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 488(1), 129-135. doi: 10.1016/j.bbrc.2017.05.021. UCLA: Retrieved from: http://www.escholarship.org/uc/item/4hz1b996

Membrane contact sites between organelles serve as molecular hubs for the exchange of metabolites and signals. In yeast, the Endoplasmic Reticulum − Mitochondrion Encounter Structure (ERMES) tethers these two organelles likely to facilitate the non

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a75a900b6d587367b7ad99537544afff
https://doi.org/10.1016/j.bbrc.2017.05.021

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Structure of the human ClC-1 chloride channel

Autor: Yanxiang Cui, Kirstine Calloe, Kaituo Wang, Z. Hong Zhou, Magnus Andersson, Liying Zhang, Kamil Gotfryd, Erik Lindahl, Michael Pusch, Julie Winkel Missel, Pontus Gourdon, Pascal F. Egea, Per Amstrup Pedersen, Sarah Spruce Preisler, Dan A. Klaerke, Christina Grønberg

Publikováno v: PLoS Biology
PLoS biology 17 (2019). doi:10.1371/journal.pbio.3000218
info:cnr-pdr/source/autori:Wang K, Preisler SS, Zhang L, Cui Y, Missel JW, Grønberg C, Gotfryd K1, Lindahl E, Andersson M, Calloe K, Egea PF, Klaerke DA, Pusch M, Pedersen PA, Zhou ZH, Gourdon P/titolo:Structure of the human ClC-1 chloride channel/doi:10.1371%2Fjournal.pbio.3000218/rivista:PLoS biology/anno:2019/pagina_da:/pagina_a:/intervallo_pagine:/volume:17
PLoS Biology, Vol 17, Iss 4, p e3000218 (2019)
PLoS biology, vol 17, iss 4
Wang, K, Preisler, S S, Zhang, L, Cui, Y, Missel, J W, Grønberg, C, Gotfryd, K, Lindahl, E, Andersson, M, Calloe, K, Egea, P F, Klaerke, D A, Pusch, M, Pedersen, P A, Zhou, Z H & Gourdon, P 2019, ' Structure of the human ClC-1 chloride channel ', PLOS Biology, vol. 17, no. 4, e3000218, pp. 1-20 . https://doi.org/10.1371/journal.pbio.3000218

ClC-1 protein channels facilitate rapid passage of chloride ions across cellular membranes, thereby orchestrating skeletal muscle excitability. Malfunction of ClC-1 is associated with myotonia congenita, a disease impairing muscle relaxation. Here, w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24b90ac1f26e3ba5e786eb05e1ac7dc4
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-159072

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Determining the Lipid-Binding Specificity of SMP Domains: An ERMES Subunit as a Case Study

Autor: Pascal F. Egea, Andrew P. AhYoung

Publikováno v: Methods in Molecular Biology ISBN: 9781493991358

Membrane contact sites between the endoplasmic reticulum (ER) and mitochondria function as a central hub for the exchange of phospholipids and calcium. The yeast Endoplasmic Reticulum–Mitochondrion Encounter Structure (ERMES) complex is composed of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5573aaec057cfe4fc2d04630c30f070e
https://doi.org/10.1007/978-1-4939-9136-5_16

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Highlighting membrane protein structure and function: A celebration of the Protein Data Bank

Autor: Ruchika Bajaj, Pascal F. Egea, Fei Li, Robert M. Stroud, Meghna Gupta, Alex J. Vecchio, Ignacio Asial, Brian C. Monk, Joana Paulino, Miles Sasha Dickinson, Shelagh Ferguson-Miller

Publikováno v: Journal of Biological Chemistry. 296:100557

Biological membranes define the boundaries of cells and compartmentalize the chemical and physical processes required for life. Many biological processes are carried out by proteins embedded in or associated with such membranes. Determination of memb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f06d85ca396a63571173d514ff0dc79
https://doi.org/10.1016/j.jbc.2021.100557

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Structure of a putative ClpS N-end rule adaptor protein from the malaria pathogenPlasmodium falciparum

Autor: Christina L. Vizcarra, Pascal F. Egea, Antoine Koehl, Andrew P. AhYoung, Duilio Cascio

Publikováno v: Protein Science. 25:689-701

The N-end rule pathway uses an evolutionarily conserved mechanism in bacteria and eukaryotes that marks proteins for degradation by ATP-dependent chaperones and proteases such as the Clp chaperones and proteases. Specific N-terminal amino acids (N-de

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::476d388c4e866d66f9f91743e55046e5
https://doi.org/10.1002/pro.2868

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