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Akira Matsuura

Researcher at Chiba University

Publications -  71
Citations -  9117

Akira Matsuura is an academic researcher from Chiba University. The author has contributed to research in topics: Saccharomyces cerevisiae & Autophagy. The author has an hindex of 29, co-authored 61 publications receiving 8386 citations. Previous affiliations of Akira Matsuura include National Institute for Basic Biology, Japan & Tokyo Institute of Technology.

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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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Apg1p, a novel protein kinase required for the autophagic process in Saccharomyces cerevisiae

TL;DR: It is shown that the APG1 gene, involved in the autophagic process in yeast, encodes a novel type of Ser/Thr protein kinase, suggesting that homologous molecular mechanisms, conserved from unicellular to multicellular organisms, are involved in dynamic membrane flow.
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TLP1: A Gene Encoding a Protein Component of Mammalian Telomerase Is a Novel Member of WD Repeats Family

TL;DR: The rat telomerase protein component 1 gene (TLP1), which is related to the gene for Tetrahymena p80, encodes a 2629 amino acid sequence and produces the TLP1 proteins p240 and p230, which were cloned and characterized and showed that p240 is modified to p230 in vivo.
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Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae.

TL;DR: Results indicate that the precursor form in the cytosol is transferred to the vacuole by autophagy and converted to the active form by vacuolar proteinases, which could be determined easily and accurately by measuring the phosphatase activity.
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Apg10p, a novel protein‐conjugating enzyme essential for autophagy in yeast

TL;DR: It is shown that after activation by Apg7p, Apg12p is transferred to the Cys‐133 residue of Apg10p to form an Apg 12p–Apg10p thioester, which indicates that Apg 10p is a new type of protein‐conjugating enzyme that functions in the ApG12p‐Apg5p conjugation pathway.