Matches in SemOpenAlex for { <https://semopenalex.org/work/W2491105326> ?p ?o ?g. }
- W2491105326 endingPage "394" @default.
- W2491105326 startingPage "375" @default.
- W2491105326 abstract "In addition to heme-copper oxidases, all higher plants, some algae, yeasts, molds, metazoans, and pathogenic microorganisms such as Trypanosoma brucei contain an additional terminal oxidase, the cyanide- and antimycin-insensitive alternative oxidase (AOX). It is a di-iron carboxylate protein that catalyzes the four-electron reduction of dioxygen to water by ubiquinol, short-circuiting the mitochondrial electron-transport chain prior to proton translocation by complexes III and IV, thereby dramatically reducing ATP formation. In plants, it plays a key role in cellular metabolism, thermogenesis, and energy homeostasis and is generally considered to be a major stress-induced protein. In T. brucei, a parasite that causes human African sleeping sickness, AOX plays a critical role in the survival of the parasite in its bloodstream form. Because AOX is absent from mammals, this protein represents a unique and promising therapeutic target. Despite its bioenergetic and medical importance, however, until recently structural features of any AOX were unknown. In this review we describe recent advances in our understanding of this protein’s structure following the recent successful crystallization of the alternative oxidase from T. brucei. We focus on the nature of the active site and ubiquinol-binding channels and describe a mechanism for the reduction of oxygen to water based on these structural insights." @default.
- W2491105326 created "2016-08-23" @default.
- W2491105326 creator A5005158368 @default.
- W2491105326 creator A5021007087 @default.
- W2491105326 creator A5032175320 @default.
- W2491105326 creator A5048380414 @default.
- W2491105326 creator A5060441431 @default.
- W2491105326 creator A5072986768 @default.
- W2491105326 creator A5080734357 @default.
- W2491105326 date "2016-01-01" @default.
- W2491105326 modified "2023-09-30" @default.
- W2491105326 title "Structure and Mechanism of Action of the Alternative Quinol Oxidases" @default.
- W2491105326 cites W185850242 @default.
- W2491105326 cites W1972415605 @default.
- W2491105326 cites W1985573773 @default.
- W2491105326 cites W1987899226 @default.
- W2491105326 cites W1991289955 @default.
- W2491105326 cites W1993000645 @default.
- W2491105326 cites W1998120645 @default.
- W2491105326 cites W2002551641 @default.
- W2491105326 cites W2003038480 @default.
- W2491105326 cites W2004448262 @default.
- W2491105326 cites W2015726498 @default.
- W2491105326 cites W2017256508 @default.
- W2491105326 cites W2021713602 @default.
- W2491105326 cites W2028462347 @default.
- W2491105326 cites W2031658822 @default.
- W2491105326 cites W2032638839 @default.
- W2491105326 cites W2035795675 @default.
- W2491105326 cites W2038873477 @default.
- W2491105326 cites W2042545763 @default.
- W2491105326 cites W2048693286 @default.
- W2491105326 cites W2052746892 @default.
- W2491105326 cites W2052811729 @default.
- W2491105326 cites W2055283831 @default.
- W2491105326 cites W2058856233 @default.
- W2491105326 cites W2058980787 @default.
- W2491105326 cites W2060322429 @default.
- W2491105326 cites W2061711520 @default.
- W2491105326 cites W2062189356 @default.
- W2491105326 cites W2065074542 @default.
- W2491105326 cites W2077749836 @default.
- W2491105326 cites W2078581076 @default.
- W2491105326 cites W2082094306 @default.
- W2491105326 cites W2083280040 @default.
- W2491105326 cites W2087956118 @default.
- W2491105326 cites W2088097288 @default.
- W2491105326 cites W2096136976 @default.
- W2491105326 cites W2098657745 @default.
- W2491105326 cites W2098666291 @default.
- W2491105326 cites W2107918972 @default.
- W2491105326 cites W2112335860 @default.
- W2491105326 cites W2137825366 @default.
- W2491105326 cites W2147873373 @default.
- W2491105326 cites W2148105483 @default.
- W2491105326 cites W2152997175 @default.
- W2491105326 cites W2153968287 @default.
- W2491105326 cites W2160310346 @default.
- W2491105326 cites W2172844043 @default.
- W2491105326 cites W2313673463 @default.
- W2491105326 cites W332328726 @default.
- W2491105326 cites W4252954754 @default.
- W2491105326 doi "https://doi.org/10.1007/978-94-017-7481-9_19" @default.
- W2491105326 hasPublicationYear "2016" @default.
- W2491105326 type Work @default.
- W2491105326 sameAs 2491105326 @default.
- W2491105326 citedByCount "5" @default.
- W2491105326 countsByYear W24911053262017 @default.
- W2491105326 countsByYear W24911053262018 @default.
- W2491105326 countsByYear W24911053262019 @default.
- W2491105326 countsByYear W24911053262020 @default.
- W2491105326 crossrefType "book-chapter" @default.
- W2491105326 hasAuthorship W2491105326A5005158368 @default.
- W2491105326 hasAuthorship W2491105326A5021007087 @default.
- W2491105326 hasAuthorship W2491105326A5032175320 @default.
- W2491105326 hasAuthorship W2491105326A5048380414 @default.
- W2491105326 hasAuthorship W2491105326A5060441431 @default.
- W2491105326 hasAuthorship W2491105326A5072986768 @default.
- W2491105326 hasAuthorship W2491105326A5080734357 @default.
- W2491105326 hasConcept C100206155 @default.
- W2491105326 hasConcept C104317684 @default.
- W2491105326 hasConcept C14471203 @default.
- W2491105326 hasConcept C181199279 @default.
- W2491105326 hasConcept C185592680 @default.
- W2491105326 hasConcept C23265538 @default.
- W2491105326 hasConcept C2778777121 @default.
- W2491105326 hasConcept C2778858093 @default.
- W2491105326 hasConcept C2779134199 @default.
- W2491105326 hasConcept C2779502636 @default.
- W2491105326 hasConcept C28859421 @default.
- W2491105326 hasConcept C29311851 @default.
- W2491105326 hasConcept C38485361 @default.
- W2491105326 hasConcept C55493867 @default.
- W2491105326 hasConcept C86803240 @default.
- W2491105326 hasConcept C95444343 @default.
- W2491105326 hasConceptScore W2491105326C100206155 @default.
- W2491105326 hasConceptScore W2491105326C104317684 @default.
- W2491105326 hasConceptScore W2491105326C14471203 @default.