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Antonio Miranda-Vizuete

Researcher at Spanish National Research Council

Publications -  105
Citations -  10447

Antonio Miranda-Vizuete is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Thioredoxin & Thioredoxin reductase. The author has an hindex of 41, co-authored 100 publications receiving 9558 citations. Previous affiliations of Antonio Miranda-Vizuete include Pablo de Olavide University & Karolinska Institutet.

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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.
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Cloning and Expression of a Novel Mammalian Thioredoxin

Giannis Spyrou, +3 more
- 31 Jan 1997 - 
TL;DR: A 1276-base pair cDNA from a rat heart cDNA library that encodes a novel thioredoxin (Trx2) of 166 amino acid residues with a calculated molecular mass of 18.2 kDa possessed a dithiol-reducing enzymatic activity and was able to reduce the interchain disulfide bridges of insulin.
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European contribution to the study of ROS : a summary of the findings and prospects for the future from the COST action BM1203 (EU-ROS)

Javier Egea, +151 more
- 01 Oct 2017 - 
TL;DR: The European Cooperation in Science and Technology (COST) provides an ideal framework to establish multi-disciplinary research networks and EU-ROS represents a consortium of researchers from different disciplines who are dedicated to providing new insights and tools for better understanding redox biology and medicine.
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Identification and functional characterization of a novel mitochondrial thioredoxin system in saccharomyces cerevisiae

José Rafael Pedrajas, +5 more
- 05 Mar 1999 - 
TL;DR: An important role of the mitochondrial thioredoxin reductase in protection against oxidative stress in S. cerevisiae is suggested.
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ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress.

Paula Cunnea, +10 more
- 10 Jan 2003 - 
TL;DR: A novel human putative ER co-chaperone (ERdj5) containing domains resembling DnaJ, protein-disulfide isomerase, and thioredoxin domains is characterized, suggesting potential roles for ERdj5 in protein folding and translocation across the ER membrane.