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Mario Pinar

Researcher at Spanish National Research Council

Publications -  29
Citations -  7125

Mario Pinar is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Golgi apparatus & Endosome. The author has an hindex of 15, co-authored 25 publications receiving 5709 citations. Previous affiliations of Mario Pinar include University of Salamanca.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
Journal ArticleDOI

Maturation of late Golgi cisternae into RabERAB11 exocytic post-Golgi carriers visualized in vivo

Areti Pantazopoulou, +3 more
- 15 Aug 2014 - 
TL;DR: Maturation of Golgi cisternae into post-Golgi carriers is directly visualized using the Aspergillus nidulans Ypt31/RAB11 homologue RabE as a reporter of post-golgi identity.
Journal Article

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2459 more
- 01 Jan 2016 - 
Journal ArticleDOI

TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabERAB11

Mario Pinar, +7 more
- 07 Apr 2015 - 
TL;DR: Evidence obtained by exploiting hypA1-mediated destabilization of HypATrs120/HypCTrs130/Trs65 assembly onto the TRAPPI core indicates that these subunits sculpt a second RAB binding site on TRAPP apparently independent from that for RabORAB1, which would explain TRAPPII in vitro activity on two RABs.