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Shinya Honda

Researcher at National Institute of Advanced Industrial Science and Technology

Publications -  120
Citations -  2415

Shinya Honda is an academic researcher from National Institute of Advanced Industrial Science and Technology. The author has contributed to research in topics: Autophagy & Protein G. The author has an hindex of 20, co-authored 106 publications receiving 2055 citations. Previous affiliations of Shinya Honda include University of Tokyo & Tokyo Medical and Dental University.

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10 residue folded peptide designed by segment statistics

TL;DR: The performance of the short peptide implies that the methodology employed here can contribute toward development of novel techniques for protein design, but it also yields insights into the raison d'etre of an autonomous element involved in a natural protein.
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Ulk1-mediated Atg5-independent macroautophagy mediates elimination of mitochondria from embryonic reticulocytes

TL;DR: Data indicate that Ulk1-dependent Atg5-independent macroautophagy is the dominant process of mitochondrial clearance from fetal definitive reticulocytes, whereas the mitochondria are engulfed and digested within autophagic structures in wild-type and Atg 5-deficient mice.
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Thermodynamics of a β-hairpin structure: evidence for cooperative formation of folding nucleus

TL;DR: The formation of the beta-hairpin is interpreted as the fashion of a first-order phase transition between two states without any distinguishable intermediates and provides insight into the first folding events of the B1 domain, but also the general principles of proteins in terms of structural hierarchy, stability and folding mechanism.
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Crystal structure of a ten-amino acid protein

TL;DR: A designed molecule consisting of only 10 amino acids is described, which despite its small size, its essential characteristics are consistent with the properties of natural proteins.
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Molecular mechanisms and physiological roles of Atg5/Atg7-independent alternative autophagy

TL;DR: It is found that cells lacking ATG5 or ATG7 can still form autophagosomes/autolysosomes and perform autophagic protein degradation when subjected to certain types of stress.