Literature DB >> 9593914

Structure-activity relationships of some complex I inhibitors.

H Miyoshi1.   

Abstract

A wide variety of complex I inhibitors act at or close to the ubiquinone reduction site. Identification of the structural factors required for exhibiting inhibitory actions on the basis of structure-activity relationships is useful to elucidate the manner in which inhibitors interact with the enzyme. This review summarizes studies on the structure-activity relationship of rotenoids, piericidins, capsaicins, pyridinium-type inhibitors and modern synthetic agrochemicals acting at mitochondrial complex I. Copyright 1998 Elsevier Science B.V.

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Year:  1998        PMID: 9593914     DOI: 10.1016/s0005-2728(98)00030-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  21 in total

Review 1.  The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: comparisons of phylogenetically related enzymes.

Authors:  T Yano; T Ohnishi
Journal:  J Bioenerg Biomembr       Date:  2001-06       Impact factor: 2.945

2.  Impairment of Atg5-dependent autophagic flux promotes paraquat- and MPP⁺-induced apoptosis but not rotenone or 6-hydroxydopamine toxicity.

Authors:  Aracely Garcia-Garcia; Annandurai Anandhan; Michaela Burns; Han Chen; You Zhou; Rodrigo Franco
Journal:  Toxicol Sci       Date:  2013-08-31       Impact factor: 4.849

Review 3.  Probing the ubiquinone reduction site in bovine mitochondrial complex I using a series of synthetic ubiquinones and inhibitors.

Authors:  H Miyoshi
Journal:  J Bioenerg Biomembr       Date:  2001-06       Impact factor: 2.945

4.  Inhibitory effect of palmitate on the mitochondrial NADH:ubiquinone oxidoreductase (complex I) as related to the active-de-active enzyme transition.

Authors:  Maria V Loskovich; Vera G Grivennikova; Gary Cecchini; Andrei D Vinogradov
Journal:  Biochem J       Date:  2005-05-01       Impact factor: 3.857

5.  EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ.

Authors:  Sergey Magnitsky; Larisa Toulokhonova; Takahiro Yano; Vladimir D Sled; Cecilia Hägerhäll; Vera G Grivennikova; Doshimjan S Burbaev; Andrei D Vinogradov; Tomoko Ohnishi
Journal:  J Bioenerg Biomembr       Date:  2002-06       Impact factor: 2.945

6.  Anaerobic NADH-fumarate reductase system is predominant in the respiratory chain of Echinococcus multilocularis, providing a novel target for the chemotherapy of alveolar echinococcosis.

Authors:  Jun Matsumoto; Kimitoshi Sakamoto; Noriko Shinjyo; Yasutoshi Kido; Nao Yamamoto; Kinpei Yagi; Hideto Miyoshi; Nariaki Nonaka; Ken Katakura; Kiyoshi Kita; Yuzaburo Oku
Journal:  Antimicrob Agents Chemother       Date:  2007-10-22       Impact factor: 5.191

7.  Synthesis and characterization of new piperazine-type inhibitors for mitochondrial NADH-ubiquinone oxidoreductase (complex I).

Authors:  Naoya Ichimaru; Masatoshi Murai; Nobuyuki Kakutani; Junko Kako; Atsushi Ishihara; Yoshiaki Nakagawa; Takaaki Nishioka; Takao Yagi; Hideto Miyoshi
Journal:  Biochemistry       Date:  2008-09-10       Impact factor: 3.162

Review 8.  Mitochondrial respiratory complex I: structure, function and implication in human diseases.

Authors:  Lokendra K Sharma; Jianxin Lu; Yidong Bai
Journal:  Curr Med Chem       Date:  2009       Impact factor: 4.530

Review 9.  Mechanism targeted discovery of antitumor marine natural products.

Authors:  Dale G Nagle; Yu-Dong Zhou; Flor D Mora; Kaleem A Mohammed; Yong-Pil Kim
Journal:  Curr Med Chem       Date:  2004-07       Impact factor: 4.530

10.  Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (Complex I) and production of reactive oxygen species.

Authors:  Martin S King; Mark S Sharpley; Judy Hirst
Journal:  Biochemistry       Date:  2009-03-10       Impact factor: 3.162

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