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FRAGMENT FROM NATURE examines the complex construction of bacteriophages (phages) that prey on bacteria, and how the structure changes dramatically when the phages become infectious. These are truly beautiful, geometrical and remarkable creatures that flip between the chemical and the living world with ease, and cause great consternation for (mostly) older taxonomists and biologists who assert that they are not living. And that they are simple. View in LinkedIn

CONSERVATION AND COMPLEXITY. "During the last nine years, homologues of genes involved in the regulation of programmed cell death in Caenorhabditis elegans have been identified in sponge, in Hydra vulgaris, in the fruitfly Drosophila melanogaster, in zebrafish, in mice and in humans. As frequently occurs during evolution, however, this striking conservation in both sequences and functional properties has been associated with a great level of diversification." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

PERMANENT REPRIEVE. "This very frailty, this permanent reprieve and the interdependence they generate between our cells, are one of the bases of our perennity and our plasticity, allowing our bodies to build themselves, to constantly reconstruct, and to adapt to ever changing environments." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

SOCIAL COUPLING. "The coupling of the fate of each cell to the nature of the interactions it can establish with other cells has led to the concept of 'social control' of cell survival and cell death, allowing a stringent regulation of cell numbers, of their geographic localization, and a constant adjustment of the different cell types that constitute our organs and tissues." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

DUAL FUNCTIONS. "Molecular effectors of cell suicide may also perform other functions unrelated to cell death induction and crucial to cell survival. In this review, I will argue that this new level of complexity, implying that there may be no such thing as a 'bona fide' genetic death program in our cells, might be better understood when considered in an evolutionary context." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

PRE-MITOCHONDRIAL. These findings "also suggest that the caspase cystein proteinases may have represented the initial, ancestral core of executioners that allowed the emergence of programmed cell death, prior to the recruitment of mitochondria as essential effectors of the cell death machinery." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

ENERGY SOURCE. "Biological machines require energy that can be provided by catalyzing a chemical reaction of high-energy molecules such as ATP, or by using the energy stored when macromolecules fold and assemble." http://www.pnas.org/content/113/10/2654.full View in LinkedIn

DIVERSIFICATION, COMPLEXITY AND VARIATION. "These findings suggest that the recruitment of caspases and mitochondrial effectors to the cell death machinery may have been subjected not only to increased diversification and complexity, but also to phylogenic variation during the evolution of metazoans." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

NEUTRALIZING DEATH. "The death repressors (Bcl-2/Bcl-XL ¼ ) and their antagonists (Bax/Bak/Bid ¼ ) share the capacity to homodimerize and to neutralize each others through heterodimerization, and, for some of them, to insert through a carboxyterminal hydrophobic transmembrane domain into the outer membrane of intracellular organelles such as the nucleus, endoplasmic reticulum and mitochondria." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn

DEATH REPRESSOR AND ANTAGONIST. "In humans and mice, around twenty gene products that are homologues of the cell death repressor Ced-9 and its antagonist Egl-1 (the Bcl-2 family) have been identified, as well as more than ten homologues of the executioner Ced-3 (the caspase family) and at least one homologue of Ced-4 (Apaf-1, or apoptotic protease-activating factor 1)." http://www.nature.com/cdd/journal/v9/n4/full/4400950a.html View in LinkedIn