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Kazuhiro Nagata

Researcher at Kyoto Sangyo University

Publications -  310
Citations -  30085

Kazuhiro Nagata is an academic researcher from Kyoto Sangyo University. The author has contributed to research in topics: Endoplasmic reticulum & Heat shock protein. The author has an hindex of 76, co-authored 302 publications receiving 27232 citations. Previous affiliations of Kazuhiro Nagata include Osaka University & Kobe Steel.

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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.
Journal ArticleDOI

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.
Journal ArticleDOI

CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum

TL;DR: This work finds that CHOP directly activates GADD34, which promotes ER client protein biosynthesis by dephosphorylating phospho-Ser 51 of the alpha-subunit of translation initiation factor 2 (eIF2alpha) in stressed cells, and protects cells from ER stress by decreasing client protein load and changing redox conditions within the organelle.
Journal ArticleDOI

A Time-Dependent Phase Shift in the Mammalian Unfolded Protein Response

TL;DR: It is shown here that degradation of misfolded glycoprotein substrates requires transcriptional induction of EDEM (ER degradation-enhancing alpha-mannosidase-like protein), and that this is mediated specifically by IRE1-XBP1 and not by ATF6.