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S. Yokoyama

Bio: S. Yokoyama is an academic researcher from Fujita Health University. The author has contributed to research in topics: Domain (software engineering) & Thermus thermophilus. The author has an hindex of 5, co-authored 171 publications receiving 254 citations.


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Journal ArticleDOI
TL;DR: The mevalonate pathway is essential in plants, many eubacteria and apicomplexan parasites, but not in archaea and animals, and detailed knowledge about the mechanisms may benefit the development of novel antibiotics, antimalarials and herbicides.
Abstract: The mevalonate pathway for the biosynthesis of the universal terpenoid precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), is known in considerable detail. Only recently, the existence of a second mevalonate-independent pathway for the biosynthesis of IPP and DMAPP was detected in plants and certain eubacteria. Experiments with 13C and/or 2H-labelled precursors were crucial in the elucidation of this novel route. The pathway is essential in plants, many eubacteria and apicomplexan parasites, but not in archaea and animals. The genes, enzymes and intermediates of this pathway were rapidly unravelled over the past few years. Detailed knowledge about the mechanisms of this novel route may benefit the development of novel antibiotics, antimalarials and herbicides.

601 citations

Journal ArticleDOI
TL;DR: The existence of specific types of protein-defined microdomains which are sculpt by the clustering of individual SPFH proteins is proposed, similar to caveolae, which provide platforms for the recruitment of multiprotein complexes.
Abstract: Reggie/flotillin proteins are considered to be components of lipid rafts and are commonly used as marker proteins for lipid microdomains. Yet almost a decade after their discovery, the function of reggies/ flotillins is still enigmatic. In this review we summarize the present state of knowledge on reggie/flotillin structure, localization and function, and discuss the role of the proteins in development and disease. Based on insights into reggie/flotillin function and by comparison with related proteins of the so-called SPFH (Stomatin/Prohibitin/Flotillin/HflK/C) protein family, including stomatin, podocin and prohibitin, we propose the existence of specific types of protein-defined microdomains which are sculpt by the clustering of individual SPFH proteins. As 'specialized rafts' similar to caveolae, these membrane domains provide platforms for the recruitment of multiprotein complexes. Since, under certain circumstances, reggie-2/flotillin-1 translocates to the nucleus, reggie/ flotillin microdomains are not only stable scaffolds but also dynamic units with their own regulatory functions.

304 citations

Journal ArticleDOI
TL;DR: Structural and biochemical advances that contribute new insights into three central facets of canonical Notch signal transduction, including ligand recognition, autoinhibition and the switch from protease resistance to protease sensitivity, and the mechanism of nuclear-complex assembly and the induction of target-gene transcription are summarized.
Abstract: The Notch signaling pathway constitutes an ancient and conserved mechanism for cell-cell communication in metazoan organisms, and has a central role both in development and in adult tissue homeostasis. Here, we summarize structural and biochemical advances that contribute new insights into three central facets of canonical Notch signal transduction: (1) ligand recognition, (2) autoinhibition and the switch from protease resistance to protease sensitivity, and (3) the mechanism of nuclear-complex assembly and the induction of target-gene transcription. These advances set the stage for future mechanistic studies investigating ligand-dependent activation of Notch receptors, and serve as a foundation for the development of mechanism-based inhibitors of signaling in the treatment of cancer and other diseases.

264 citations

Journal ArticleDOI
TL;DR: I greatly appreciate interacting with Peter Schultz, Scott Lesley and Marc Nasoff at the Genomics Institute for the Novartis Research Foundation and Mark Knuth and Ron Swanson at Syrrx, Inc., where much of this work is currently being pursued.

262 citations

Journal ArticleDOI
TL;DR: This review aims to integrate structural, biochemical, and functional aspects of this bewildering and ancient family of glycan-binding proteins and discuss their implications in physiologic and pathologic settings.
Abstract: In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes occurring on the cell surface during fundamental biological processes such as cellular communication, inflammation, development, and differentiation. Their highly conserved structures, exquisite carbohydrate specificity, and ability to modulate a broad spectrum of biological processes have captivated a wide range of scientists from a wide spectrum of disciplines, including biochemistry, biophysics, cell biology, and physiology. However, in spite of enormous efforts to dissect the functions and properties of these glycan-binding proteins, limited information about how structural and biochemical aspects of these proteins can influence biological functions is available. In this review, we aim to integrate structura...

247 citations