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Gemma Triola

Researcher at Spanish National Research Council

Publications -  59
Citations -  8006

Gemma Triola is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: Membrane & Rab. The author has an hindex of 27, co-authored 57 publications receiving 7338 citations. Previous affiliations of Gemma Triola include Technical University of Dortmund & Max Planck Society.

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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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Small molecule inhibition of the KRAS–PDEδ interaction impairs oncogenic KRAS signalling

Gunther Zimmermann, +10 more
- 30 May 2013 - 
TL;DR: It is reported that interfering with binding of mammalian PDEδ to KRAS by means of small molecules provides a novel opportunity to suppress oncogenic RAS signalling by altering its localization to endomembranes.
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Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo

Shehab Ismail, +9 more
- 01 Dec 2011 - 
TL;DR: The structure of fully modified farnesylated Rheb-GDP in complex with PDEδ is reported and it is demonstrated that the G proteins Arl2 and Arl3 act in a GTP-dependent manner as allosteric release factors for farnesyated cargo.
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Bioorthogonal chemistry for site-specific labeling and surface immobilization of proteins.

Yong-Xiang Chen, +2 more
- 07 Jun 2011 - 
TL;DR: This Account summarizes recent developments and applications of site-specific protein labeling and surface immobilization of proteins, with a special focus on contributions to these fields.
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N-Ras forms dimers at POPC membranes.

Jörn Güldenhaupt, +7 more
- 03 Oct 2012 - 
TL;DR: A dimerization interface is proposed between α-helices 4 and 5 and the loop between β2 and β3 and seems to explain why the residues D47, E49, R135, R161, and R164 of this interface are influencing Ras signaling in cellular physiological experiments, although they are not positioned in the catalytic site.