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Thomas J. Melia

Researcher at Yale University

Publications -  56
Citations -  9843

Thomas J. Melia is an academic researcher from Yale University. The author has contributed to research in topics: Autophagosome & Autophagy. The author has an hindex of 30, co-authored 46 publications receiving 8003 citations. Previous affiliations of Thomas J. Melia include Columbia University.

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Guidelines for the use and interpretation of assays for monitoring autophagy

Daniel J. Klionsky, +1287 more
- 01 Apr 2012 - 
TL;DR: These guidelines are presented for the selection and interpretation of methods for use by investigators who aim to examine macroautophagy 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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Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins

TL;DR: A fundamental role is demonstrated of the SM protein: to act as a stimulatory subunit of its cognate SNARE fusion machinery, enhancing fusion specificity in a reconstituted system.
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SNARE proteins are required for macroautophagy

TL;DR: Evidence is provided for the involvement of exocytic Q/t-SNAREs in autophagosome formation, acting in the recruitment of key autophagy components to the site of autophagic formation, and in regulating the organization of Atg9 into tubulovesicular clusters.
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Acetylation Targets Mutant Huntingtin to Autophagosomes for Degradation

TL;DR: It is reported here that posttranslational modification of the mutant Huntingtin (Htt) by acetylation at lysine residue 444 facilitates trafficking of mutant Htt into autophagosomes, significantly improves clearance of the mutants protein by macroautophagy, and reverses the toxic effects of mutant huntingtin in primary striatal and cortical neurons and in a transgenic C. elegans model of HD.
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The Legionella Effector RavZ Inhibits Host Autophagy Through Irreversible Atg8 Deconjugation

TL;DR: It is found that the intracellular pathogen Legionella pneumophila could interfere with autophagy by using the bacterial effector protein RavZ to directly uncouple Atg8 proteins attached to phosphatidylethanolamine on autophagosome membranes, which could not be reconjugated by Atg7 and Atg3.