Výsledky vyhledávání - "Jhon Rivera‐Monroy"

The intramembrane proteases SPPL2a and SPPL2b regulate the homeostasis of selected SNARE proteins

Autor: Moritz Ballin, Wolfram Griep, Mehul Patel, Martin Karl, Torben Mentrup, Jhon Rivera‐Monroy, Brian Foo, Blanche Schwappach, Bernd Schröder

Publikováno v: The FEBS Journal. 290:2320-2337

Signal peptide peptidase (SPP) and SPP-like (SPPL) aspartyl intramembrane proteases are known to contribute to sequential processing of type II-oriented membrane proteins referred to as regulated intramembrane proteolysis. The ER-resident family memb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67b88ec206d212f07befe44e09ffa478
https://doi.org/10.1111/febs.16610

Zobrazit plný text záznamu

Author response for 'The intramembrane proteases SPPL2a and SPPL2b regulate the homeostasis of selected SNARE proteins'

Autor: null Moritz Ballin, null Wolfram Griep, null Mehul Patel, null Martin Karl, null Torben Mentrup, null Jhon Rivera‐Monroy, null Brian Foo, null Blanche Schwappach, null Bernd Schröder

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::de45aa02179c05902d1ea9a4f90a6f68
https://doi.org/10.1111/febs.16610/v2/response1

Zobrazit plný text záznamu

Endoplasmic reticulum membrane receptors of the GET pathway are conserved throughout eukaryotes

Autor: Martiniano Maria Ricardi, Holger Breuninger, Lisa Yasmin Asseck, Martin Bayer, Christopher Grefen, Niklas Wallmeroth, Minou Nowrousian, Shuping Xing, Dietmar G. Mehlhorn, Kenneth W. Berendzen, Blanche Schwappach, Jhon Rivera Monroy

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America

Significance The GET pathway is required for the insertion of tail-anchored (TA) membrane proteins in the endoplasmic reticulum (ER) of yeast and mammals. Some orthologous genes had also been identified in higher plants with the exception of one of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4316cffd90f2e2ffd8fb9cf048d28407
https://pubmed.ncbi.nlm.nih.gov/33443185

Zobrazit plný text záznamu

The Molecular Basis and Biologic Significance of the β-Dystroglycan-Emerin Interaction

Autor: Wendy Lilián Gómez-Monsivais, James M. Holaska, Jesús Mauricio Ernesto Hernández-Méndez, Jhon Rivera-Monroy, Paulina Margarita Azuara-Medina, Jonathan J. Magaña, Raúl Argüello-García, Steve J. Winder, Bulmaro Cisneros, Feliciano Monterrubio-Ledezma, Ivette Martínez-Vieyra, Efraín Garrido, Alma Alamillo-Iniesta, Jazmin Huerta-Cantillo, Ricardo Mondragon-Gonzalez, Ian García-Aguirre, Fernando Navarro-Garcia, Andrea Brancaccio

Publikováno v: International Journal of Molecular Sciences
International journal of molecular sciences (Online) 21 (2020): 1–20. doi:10.3390/ijms21175944
info:cnr-pdr/source/autori:Gomez-Monsivais W.L.; Monterrubio-Ledezma F.; Huerta-Cantillo J.; Mondragon-Gonzalez R.; Alamillo-Iniesta A.; Garcia-Aguirre I.; Azuara-Medina P.M.; Arguello-Garcia R.; Rivera-Monroy J.E.; Holaska J.M.; Hernandez-Mendez J.M.E.; Garrido E.; Magana J.J.; Winder S.J.; Brancaccio A.; Martinez-Vieyra I.; Navarro-Garcia F.; Cisneros B./titolo:The molecular basis and biologic significance of the ?-dystroglycan-emerin interaction/doi:10.3390%2Fijms21175944/rivista:International journal of molecular sciences (Online)/anno:2020/pagina_da:1/pagina_a:20/intervallo_pagine:1–20/volume:21
International Journal of Molecular Sciences, Vol 21, Iss 5944, p 5944 (2020)
Volume 21
Issue 17
Gómez-Monsiváis, W L, Monterrubio-Ledezma, F, Huerta-Cantillo, J, Mondragon-Gonzalez, R, Alamillo-Iniesta, A, García-Aguirre, I, Azuara-Medina, P M, Arguello-García, R, Rivera-Monroy, J E, Holaska, A M, Hernández-Méndez, J M E, Garrido, E, Javier Magaña, J, Winder, S, Brancaccio, A, Martínez-Vieyra, I, Navarro-Garcia, F & Cisneros, B 2020, ' The molecular basis and biological significance of the β-dystroglycan-emerin interaction ', International Journal of Molecular Sciences, vol. 21, no. 17, 5944 . https://doi.org/10.3390/ijms21175944

&beta
dystroglycan (&beta
DG) assembles with lamins A/C and B1 and emerin at the nuclear envelope (NE) to maintain proper nuclear architecture and function. To provide insight into the nuclear function of &beta
DG, we characterized the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd8369a6bc8ba430d6991cf14c9a6c53
http://europepmc.org/articles/PMC7504044

Zobrazit plný text záznamu

A trap mutant reveals the physiological client spectrum of TRC40

Autor: Christof Lenz, Henning Urlaub, Javier Coy-Vergara, Jhon Rivera-Monroy, Blanche Schwappach

Publikováno v: Journal of Cerll Science
Journal of Cell Science

The transmembrane recognition complex (TRC) pathway targets tail-anchored (TA) proteins to the membrane of the endoplasmic reticulum (ER). While many TA proteins are known to be able to use this pathway, it is essential for the targeting of only a fe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aa30954de7e188a4a402a36096fbb02
https://doi.org/10.1242/jcs.230094

Zobrazit plný text záznamu

An alternative membrane topology permits lipid droplet localization of peroxisomal fatty acyl-CoA reductase 1

Autor: Joachim Füllekrug, Masanori Honsho, Einat Zalckvar, Christos C. Zouboulis, Ralf Bartenschlager, Margarete Poppelreuther, Inés Romero-Brey, Tarik Exner, Wolfgang Stremmel, Bianca Schrul, Jhon Rivera-Monroy, Eden Yifrach

Fatty acyl-CoA reductase 1 (Far1) is an ubiquitously expressed peroxisomal membrane protein generating fatty alcohols required for the biosynthesis of ether lipids. Lipid droplet localization of exogenously expressed and endogenous human Far1 was obs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12bac13db0bfe0666d89f2606470d86e

Zobrazit plný text záznamu

Mice lacking WRB reveal differential biogenesis requirements of tail-anchored proteins in vivo

Autor: Jhon Rivera-Monroy, David P. Corey, Uri Weill, Maya Schuldiner, Anne Clancy, Philipp Ströbel, Javier Coy-Vergara, Kirsten Unthan-Fechner, Sarah Gockel, Tobias Kohl, Fabio Vilardi, Shuh-Yow Lin, Blanche Schwappach, Lena Musiol, Ákos Farkas

Publikováno v: Scientific Reports

Tail-anchored (TA) proteins are post-translationally inserted into membranes. The TRC40 pathway targets TA proteins to the endoplasmic reticulum via a receptor comprised of WRB and CAML. TRC40 pathway clients have been identified using in vitro assay

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efe98af2acabbb5040f10833a797bf83

Zobrazit plný text záznamu

Identification of mycotoxins by UHPLC–QTOF MS in airborne fungi and fungi isolated from industrial paper and antique documents from the Archive of Bogotá

Autor: Michael Sulyok, Félix Hernández, Nancy Isabel Castillo, Martha Lucia Posada-Buitrago, María Ibáñez, Jhon Rivera-Monroy, Juan Camilo Ochoa, Mónica Páez-Castillo, Eduardo Beltrán

Publikováno v: Repositori Universitat Jaume I
Universitat Jaume I

Mold deterioration of historical documents in archives and libraries is a frequent and complex phenomenon that may have important economic and cultural consequences. In addition, exposure to toxic fungal metabolites might produce health problems. In

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03e223de613a0e108005175859792e19

Zobrazit plný text záznamu

Emery-Dreifuss muscular dystrophy mutations impair TRC40-mediated targeting of emerin to the inner nuclear membrane

Autor: Fabio Vilardi, Ralph H. Kehlenbach, Blanche Schwappach, Jhon Rivera Monroy, Kalpana Rajanala, Cara Jamieson, Janine Pfaff

Publikováno v: Journal of Cell Science

Emerin is a tail-anchored protein that is found predominantly at the inner nuclear membrane (INM), where it associates with components of the nuclear lamina. Mutations in the emerin gene cause Emery-Dreifuss muscular dystrophy (EDMD), an X-linked rec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aee3735a3feed9c13746b639e0918a3f
https://doi.org/10.1242/jcs.179333

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání