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Inhibition of Fusarium oxysporum f. sp. nicotianae Growth by Phenylpropanoid Pathway Intermediates
Timothy E,Shull,Jasmina Kurepa,Robert D,Miller,Natalia Martinez-Ochoa,Jan A,Smalle 한국식물병리학회 2020 Plant Pathology Journal Vol.36 No.6
Fusarium wilt in tobacco caused by the fungus Fusarium oxysporum f. sp. nicotianae is a disease‑management challenge worldwide, as there are few effective and environmentally benign chemical agents for its control. This challenge results in substantial losses in both the quality and yield of tobacco products. Based on an in vitro analysis of the effects of different phenylpropanoid intermediates, we found that the early intermediates trans‑cinnamic acid and para‑coumaric acid effectively inhibit the mycelial growth of F. oxysporum f. sp. nicotianae strain FW316F, whereas the downstream intermediates quercetin and caffeic acid exhibit no fungicidal properties. Therefore, our in vitro screen suggests that trans‑cinnamic acid and para‑coumaric acid are promising chemical agents and natural lead compounds for the suppression of F. oxysporum f. sp. nicotianae growth.
Falaschetti, Christine A.,Paunesku, Tatjana,Kurepa, Jasmina,Nanavati, Dhaval,Chou, Stanley S.,De, Mrinmoy,Song, MinHa,Jang, Jung-tak,Wu, Aiguo,Dravid, Vinayak P.,Cheon, Jinwoo,Smalle, Jan,Woloschak, G American Chemical Society 2013 ACS NANO Vol.7 No.9
<P>The multicatalytic ubiquitin–proteasome system (UPS) carries out proteolysis in a highly orchestrated way and regulates a large number of cellular processes. Deregulation of the UPS in many disorders has been documented. In some cases, such as carcinogenesis, elevated proteasome activity has been implicated in disease development, while the etiology of other diseases, such as neurodegeneration, includes decreased UPS activity. Therefore, agents that alter proteasome activity could suppress as well as enhance a multitude of diseases. Metal oxide nanoparticles, often developed as diagnostic tools, have not previously been tested as modulators of proteasome activity. Here, several types of metal oxide nanoparticles were found to adsorb to the proteasome and show variable preferential binding for particular proteasome subunits with several peptide binding “hotspots” possible. These interactions depend on the size, charge, and concentration of the nanoparticles and affect proteasome activity in a time-dependent manner. Should metal oxide nanoparticles increase proteasome activity in cells, as they do <I>in vitro</I>, unintended effects related to changes in proteasome function can be expected.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/ancac3/2013/ancac3.2013.7.issue-9/nn402416h/production/images/medium/nn-2013-02416h_0010.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/nn402416h'>ACS Electronic Supporting Info</A></P>