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18 pages, 236 KiB

Open AccessArticle

by Erin Schoneveld

Arts 2019, 8(2), 43; https://doi.org/10.3390/arts8020043 - 28 Mar 2019

Cited by 5 | Viewed by 7531

This article evaluates contemporary filmmaker Naomi Kawase’s (b. 1969–) status within Japan’s film industry as well as her place among women directors. Using Kawase’s three award winning features Suzaku (Moe no suzaku, 1997), Shara (Sharasōju, 2003), and Mogari (Mogari no mori, 2007) as the basis of my analysis, I examine the way in which these films illuminate the construction of Kawase’s female authorship in relation to a specific location. While Kawase has made a number of critically and commercially successful films since 2007, I limit my discussion to her early narrative works set in Nara, Japan in order to illuminate the significance of the international film festival apparatus in establishing and upholding the discourse of auteurism in relation to regional identity. Through my analysis I argue that Kawase successfully negotiates this discourse through a strategy of self-promotion that emphasizes a “cinema of place” within the broader context of international film festivals such as Cannes. Kawase’s “cinema of place” ultimately allows her to rearticulate the meaning of female authorship within an art cinema context by representing a new national cinema that challenges the structures and boundaries of Japan’s studio system. Full article

(This article belongs to the Special Issue Japanese Transnational Cinema)

12 pages, 1326 KiB

Open AccessArticle

Substitution at the C-3 Position of Catechins Has an Influence on the Binding Affinities against Serum Albumin

by Masaki Ikeda, Manabu Ueda-Wakagi, Kaori Hayashibara, Rei Kitano, Masaya Kawase, Kunihiro Kaihatsu, Nobuo Kato, Yoshitomo Suhara, Naomi Osakabe and Hitoshi Ashida

Molecules 2017, 22(2), 314; https://doi.org/10.3390/molecules22020314 - 18 Feb 2017

Cited by 14 | Viewed by 6736

Abstract

It is known that catechins interact with the tryptophan (Trp) residue at the drug-binding site of serum albumin. In this study, we used catechin derivatives to investigate which position of the catechin structure strongly influences the binding affinity against bovine serum albumin (BSA) and human serum albumin (HSA). A docking simulation showed that (−)-epigallocatechin gallate (EGCg) interacted with both Trp residues of BSA (one at drug-binding site I and the other on the molecular surface), mainly by π–π stacking. Fluorescence analysis showed that EGCg and substituted EGCg caused a red shift of the peak wavelength of Trp similarly to warfarin (a drug-binding site I-specific compound), while 3-O-acyl-catechins caused a blue shift. To evaluate the binding affinities, the quenching constants were determined by the Stern–Volmer equation. A gallate ester at the C-3 position increased the quenching constants of the catechins. Against BSA, acyl substitution increased the quenching constant proportionally to the carbon chain lengths of the acyl group, whereas methyl substitution decreased the quenching constant. Against HSA, neither acyl nor methyl substitution affected the quenching constant. In conclusion, substitution at the C-3 position of catechins has an important influence on the binding affinity against serum albumin. Full article

(This article belongs to the Section Natural Products Chemistry)

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