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Hitoshi Nakatogawa

Researcher at Tokyo Institute of Technology

Publications -  76
Citations -  18888

Hitoshi Nakatogawa is an academic researcher from Tokyo Institute of Technology. The author has contributed to research in topics: Autophagy & ATG8. The author has an hindex of 36, co-authored 70 publications receiving 15280 citations. Previous affiliations of Hitoshi Nakatogawa include National Presto Industries & Graduate University for Advanced Studies.

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Journal ArticleDOI

Membrane Morphology Is Actively Transformed by Covalent Binding of the Protein Atg8 to PE-Lipids

Roland L. Knorr, +5 more
- 18 Dec 2014 - 
TL;DR: The results suggest that a positive feedback exists between the ubiquitin-like reaction and the membrane curvature, which is important for dynamic shape changes of cell membranes, such as those involved in the formation of autophagosomes.
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The NMR structure of the autophagy-related protein Atg8

Hiroyuki Kumeta, +10 more
- 29 Apr 2010 - 
TL;DR: The structure of Atg8 at the peptide-free state is studied, a ubiquitin like protein, and plays an essential role for autophagosome formation in Saccharomyces cerevisiae, which has a crucial function in numerous biological processes including differentiation, antigen presentation and aging.
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Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Daniel J. Klionsky, +2522 more
- 01 Jan 2016 - 
TL;DR: Author(s): Klionsky, DJ; Abdelmohsen, K; Abe, A; Abedin, MJ; Abeliovich, H; A Frozena, AA; Adachi, H, Adeli, K, Adhihetty, PJ; Adler, SG; Agam, G; Agarwal, R; Aghi, MK; Agnello, M; Agostinis, P; Aguilar, PV; Aguirre-Ghis
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Physiological pH and Acidic Phospholipids Contribute to Substrate Specificity in Lipidation of Atg8

Kyoko Oh-oka, +6 more
- 08 Aug 2008 - 
TL;DR: In vitro studies showed that the in vitro phosphatidylserine conjugation of Atg8 is markedly suppressed at physiological pH, and the addition of acidic phospholipids to liposomes also results in the preferential formation of the Atg9-PE conjugate, suggesting that these factors contribute to the selective formation of AtG8-PE in the cell.
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Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7

Masaya Yamaguchi, +11 more
- 01 Dec 2012 - 
TL;DR: In this paper, the mechanism by which the UBL proteins Atg8 and Atg12 are correctly charged by a single activating enzyme, Atg7, then transferred onto their cognate E2 proteins.