Stefan Grimm, 1963–2014, a tragic loss for the scientific community

Al, Mahul-Mellier; L, Huc; Lemarié, Anthony; Irshad, Sheeba; Hwang, Mi Yeong; Datler, Christoph; Pazarentzos, Evangelos

doi:10.1038/cdd.2014.196

Cited by 2 publications

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“…Of note, these quiescent mitochondria would constitute a third mitochondrial state, not described in Figure 9 , since they lack the oxidative phosphorylation complexes and hence a source of superoxide to protect the mitochondrial DNA. This line of research was also unfortunately disrupted at Queen Mary University of London (Allen and Missirlis, 2012 ; Ashworth, 2012 ; Horton, 2012 ); for further insights see (Burrows, 2012 ; Mahul-Mellier et al, 2015 ; Lawrence, 2016 ; Edwards and Roy, 2017 ; Tsimilli-Michael and Haldimann, 2017 ).…”

Section: Physiological Relevance Of Fe-s and Moco Enzymes In Differenmentioning

confidence: 99%

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

2018

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Iron sulfur (Fe-S) clusters and the molybdenum cofactor (Moco) are present at enzyme sites, where the active metal facilitates electron transfer. Such enzyme systems are soluble in the mitochondrial matrix, cytosol and nucleus, or embedded in the inner mitochondrial membrane, but virtually absent from the cell secretory pathway. They are of ancient evolutionary origin supporting respiration, DNA replication, transcription, translation, the biosynthesis of steroids, heme, catabolism of purines, hydroxylation of xenobiotics, and cellular sulfur metabolism. Here, Fe-S cluster and Moco biosynthesis in Drosophila melanogaster is reviewed and the multiple biochemical and physiological functions of known Fe-S and Moco enzymes are described. We show that RNA interference of Mocs3 disrupts Moco biosynthesis and the circadian clock. Fe-S-dependent mitochondrial respiration is discussed in the context of germ line and somatic development, stem cell differentiation and aging. The subcellular compartmentalization of the Fe-S and Moco assembly machinery components and their connections to iron sensing mechanisms and intermediary metabolism are emphasized. A biochemically active Fe-S core complex of heterologously expressed fly Nfs1, Isd11, IscU, and human frataxin is presented. Based on the recent demonstration that copper displaces the Fe-S cluster of yeast and human ferredoxin, an explanation for why high dietary copper leads to cytoplasmic iron deficiency in flies is proposed. Another proposal that exosomes contribute to the transport of xanthine dehydrogenase from peripheral tissues to the eye pigment cells is put forward, where the Vps16a subunit of the HOPS complex may have a specialized role in concentrating this enzyme within pigment granules. Finally, we formulate a hypothesis that (i) mitochondrial superoxide mobilizes iron from the Fe-S clusters in aconitase and succinate dehydrogenase; (ii) increased iron transiently displaces manganese on superoxide dismutase, which may function as a mitochondrial iron sensor since it is inactivated by iron; (iii) with the Krebs cycle thus disrupted, citrate is exported to the cytosol for fatty acid synthesis, while succinyl-CoA and the iron are used for heme biosynthesis; (iv) as iron is used for heme biosynthesis its concentration in the matrix drops allowing for manganese to reactivate superoxide dismutase and Fe-S cluster biosynthesis to reestablish the Krebs cycle.

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Section: Physiological Relevance Of Fe-s and Moco Enzymes In Differenmentioning

confidence: 99%

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

2018

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“…The degree of the pressure varies from country to country but in some cases it is great and has led to grave consequences. For instance, Mahul-Mellier et al (2015) recount the sad story of Stefan Grimm, a professor of toxicology at the Imperial College, London, who committed suicide in September 2014 after his superiors warned him that he had not met his research targets in terms of funding. Although Professor Grimm's publication history was impressive, he apparently failed to achieve the financial targets expected by his superiors.…”

Section: Introductionmentioning

confidence: 99%

Publishing and perishing? Publishing patterns of information science academics in Kenya

Kwanya

2018

Information Development

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This study investigated the publishing patterns of information science academics in Kenya. Using a bibliometric approach, the author conducted an analysis of the quantity, quality and visibility of the publications indexed by Google Scholar. Data for the analysis was collected using Harzing’s “Publish or Perish” software from Google Scholar and presented using VOSviewer software. The findings of the study revealed low quantity, quality and visibility of research publications by information science academics in Kenya. Twenty (22.4%) serving academics are yet to publish any scholarly work. Similarly, 185 (42%) of the published papers have not been cited. This low publishing performance can be attributed to lack of scholarly communication skills; inadequate research funding and facilitation; limited access to scholarly communication channels; and heavy teaching workloads, among other factors. The quantity, quality and visibility of publications by information science academics in Kenya can be enhanced by training the lecturers on scholarly communication; accrediting journals and publishers; increasing research funding; strengthening research collaboration; increasing scholarly forums and platforms; and balancing lecturers’ teaching and research workloads.

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Stefan Grimm, 1963–2014, a tragic loss for the scientific community

Cited by 2 publications

References 0 publications

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

Publishing and perishing? Publishing patterns of information science academics in Kenya

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