Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Veit Goder"'
Autor:
Sergio Lopez, Ana Maria Perez-Linero, Javier Manzano-Lopez, Susana Sabido-Bozo, Alejandro Cortes-Gomez, Sofia Rodriguez-Gallardo, Auxiliadora Aguilera-Romero, Veit Goder, Manuel Muñiz
Publikováno v:
Cells, Vol 9, Iss 5, p 1295 (2020)
The cellular mechanisms that ensure the selectivity and fidelity of secretory cargo protein transport from the endoplasmic reticulum (ER) to the Golgi are still not well understood. The p24 protein complex acts as a specific cargo receptor for GPI-an
Externí odkaz:
https://doaj.org/article/0cf7c4ad0cea4e23b7fdbd1283e94285
Autor:
Veit Goder
Publikováno v:
Molecular & Cellular Oncology, Vol 4, Iss 1 (2017)
The endoplasmic reticulum (ER) is considered a prominent membrane source for the formation of autophagosomes. Recent results from our laboratory revealed a cellular mechanism for the contribution of the ER to autophagosomes in yeast: membranes, toget
Externí odkaz:
https://doaj.org/article/a2946bf9571b46b9b31bbd4d0d25254f
Autor:
Leticia Lemus, Veit Goder
Publikováno v:
Cells, Vol 3, Iss 3, Pp 824-847 (2014)
Quality control of protein folding inside the endoplasmic reticulum (ER) includes chaperone-mediated assistance in folding and the selective targeting of terminally misfolded species to a pathway called ER-associated protein degradation, or simply ER
Externí odkaz:
https://doaj.org/article/a52d4aa5370b44ee99abc1c63d443b82
Publikováno v:
Nature Reviews Molecular Cell Biology.
Autor:
Veit Goder, Leticia Lemus
Publikováno v:
Curr Biol
Autophagy targets cytoplasmic materials for degradation, and influences cell health. Organelle contact and trafficking systems provide membranes for autophagosome formation, but how different membrane systems are selected for use during autophagy rem
Autor:
Veit Goder, Leticia Lemus
Publikováno v:
Autophagy
Clearance of misfolded proteins from the secretory pathway often occurs soon after their biosynthesis by endoplasmic reticulum (ER)-associated protein degradation (ERAD). However, certain types of misfolded proteins are not ERAD substrates and exit t
Autor:
Sofia Rodriguez-Gallardo, Manuel Muñiz, Alejandro Cortes-Gomez, Susana Sabido-Bozo, Sergio López, Javier Manzano-López, Ana Maria Perez-Linero, Veit Goder, Auxiliadora Aguilera-Romero
Publikováno v:
Cells, Vol 9, Iss 1295, p 1295 (2020)
idUS: Depósito de Investigación de la Universidad de Sevilla
Universidad de Sevilla (US)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Cells
idUS. Depósito de Investigación de la Universidad de Sevilla
Volume 9
Issue 5
idUS: Depósito de Investigación de la Universidad de Sevilla
Universidad de Sevilla (US)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Cells
idUS. Depósito de Investigación de la Universidad de Sevilla
Volume 9
Issue 5
This article belongs to the Section Organelle Function.
The cellular mechanisms that ensure the selectivity and fidelity of secretory cargo protein transport from the endoplasmic reticulum (ER) to the Golgi are still not well understood. The p24
The cellular mechanisms that ensure the selectivity and fidelity of secretory cargo protein transport from the endoplasmic reticulum (ER) to the Golgi are still not well understood. The p24
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::029c97cee8d076dc300b2db86476fb7d
Publikováno v:
Current Biology. 31:4025-4037.e5
Summary Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are membrane-conjugated cell-surface proteins with diverse structural, developmental, and signaling functions and clinical relevance. Typically, after biosynthesis and attachment to the
SummaryNewly synthesized proteins of the secretory pathway are quality-controlled inside the endoplasmic reticulum (ER) and, if not properly folded, are retained. An exception are glycosylphosphatidylinositol-anchored proteins (GPI-APs) which can lea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b5d9065925b15fddfebd3810489b459