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Geneva, Switzerland

The University of Geneva is a public research university located in Geneva, Switzerland. It was founded in 1559 by John Calvin, as a theological seminary and law school. It remained focused on theology until the 17th century, when it became a center for Enlightenment scholarship. In 1873, it dropped its religious affiliations and became officially secular. Today, the university is the second-largest university in Switzerland by number of students. In 2009, the University of Geneva celebrated the 450th anniversary of its founding.UNIGE has programs in various fields but has academic and research programs in international relations , law, astrophysics, astronomy, genetics . The university holds and actively pursues teaching, research, and community service as its primary objectives. In 2011, it was ranked 73rd worldwide by the Academic Ranking of World Universities, and 69th in the QS World University Rankings.UNIGE is a member of the League of European Research Universities, the Coimbra Group and the European University Association. Wikipedia.


Bender T.,University of Geneva
Cold Spring Harbor perspectives in biology | Year: 2013

Although mitochondria are usually considered as supporters of life, they are also involved in cellular death. Mitochondrial outer membrane permeabilization (MOMP) is a crucial event during apoptosis because it causes the release of proapoptotic factors from the mitochondrial intermembrane space to the cytosol. MOMP is mainly controlled by the Bcl-2 family of proteins, which consists of both proapoptotic and antiapoptotic members. We discuss the current understanding of how activating and inhibitory interactions within this family lead to the activation and oligomerization of MOMP effectors Bax and Bak, which result in membrane permeabilization. The order of events leading to MOMP is then highlighted step by step, emphasizing recent discoveries regarding the formation of Bax/Bak pores on the outer mitochondrial membrane. Besides the Bcl-2 proteins, the mitochondrial organelle contributes to and possibly regulates MOMP, because mitochondrial resident proteins and membrane lipids are prominently involved in the process. Source


Wehrle-Haller B.,University of Geneva
Current Opinion in Cell Biology | Year: 2012

Integrin-dependent cell adhesions come in different shapes and serve in different cell types for tasks ranging from cell-adhesion, migration, and the remodeling of the extracellular matrix to the formation and stabilization of immunological and chemical synapses. A major challenge consists in the identification of adhesion-specific as well as common regulatory mechanisms, motivating the need for a deeper analysis of protein-protein interactions in the context of intact focal adhesions. Specifically, it is critical to understand how small differences in binding of integrins to extracellular ligands and/or cytoplasmic adapter proteins affect the assembly and function of an entire focal adhesion. By using the talin-integrin pair as a starting point, I would like to discuss how specific protein-protein and protein-lipid interactions can control the behavior and function of focal adhesions. By responding to chemical and mechanical cues several allosterically regulated proteins create a dynamic multifunctional protein network that provides both adhesion to the extracellular matrix as well as intracellular signaling in response to mechanical changes in the cellular environment. © 2011 Elsevier Ltd. Source


Rochaix J.-D.,University of Geneva
Annual Review of Plant Biology | Year: 2014

Photosynthetic organisms are continuously subjected to changes in light quantity and quality, and must adjust their photosynthetic machinery so that it maintains optimal performance under limiting light and minimizes photodamage under excess light. To achieve this goal, these organisms use two main strategies in which light-harvesting complex II (LHCII), the light-harvesting system of photosystem II (PSII), plays a key role both for the collection of light energy and for photoprotection. The first is energy-dependent nonphotochemical quenching, whereby the high-light-induced proton gradient across the thylakoid membrane triggers a process in which excess excitation energy is harmlessly dissipated as heat. The second involves a redistribution of the mobile LHCII between the two photosystems in response to changes in the redox poise of the electron transport chain sensed through a signaling chain. These two processes strongly diminish the production of damaging reactive oxygen species, but photodamage of PSII is unavoidable, and it is repaired efficiently. Copyright © 2014 by Annual Reviews. Source


Wehrle-Haller B.,University of Geneva
Current Opinion in Cell Biology | Year: 2012

The formation of tissues and organs requires cells to adhere to each other and/or to migrate and polarize in contact with components of the extracellular matrix. The connection between the cytoskeleton and the extracellular environment is provided by heterodimeric transmembrane receptors of the integrin family. In response to extracellular ligand binding, integrins undergo a conformational switch that permits the recruitment of cytoplasmic adapter proteins, eventually linking the integrin receptors to the actin cytoskeleton, progressively forming highly complex cell-matrix adhesions. A major challenge in the field consists in identifying the regulatory mechanisms, which drive the assembly of cell-matrix adhesions as they are based on posttranslational modifications as well as allosteric conformational changes caused by protein-protein as well as protein-lipid interactions. In response to mechanical tension, generated either by intra-cellular acto-myosin contraction, shear stress or mechanical strain on the extracellular scaffold, the composition and signaling of cell-matrix adhesion changes, leading either to increased anchorage or controlled disassembly of cell matrix adhesions, both processes critically involved in cell migration. The aim of this review is to provide insight into the mechanisms leading to the progressive assembly of focal adhesions, how they are modulated in response to mechanical challenges and which mechanisms are used for their disassembly. © 2012 Elsevier Ltd. Source


Rizzoli R.,University of Geneva
American Journal of Clinical Nutrition | Year: 2014

Fracture risk is determined by bone mass, geometry, and microstructure, which result from peak bone mass (the amount attained at the end of pubertal growth) and from the amount of bone lost subsequently. Nutritional intakes are an important environmental factor that influence both bone mass accumulation during childhood and adolescence and bone loss that occurs in later life. Bone growth is influenced by dietary intake, particularly of calcium and protein. Adequate dietary calcium and protein are essential to achieve optimal peak bone mass during skeletal growth and to prevent bone loss in the elderly. Dairy products are rich in nutrients that are essential for good bone health, including calcium, protein, vitamin D, potassium, phosphorus, and other micronutrients and macronutrients. Studies supporting the beneficial effects of milk or dairy products on bone health show a significant inverse association between dairy food intake and bone turnover markers and a positive association with bone mineral content. Fortified dairy products induce more favorable changes in biochemical indexes of bone metabolism than does calcium supplementation alone. The associations between the consumption of dairy products and the risk of hip fracture are less well established, although yogurt intake shows a weakly positive protective trend for hip fracture. By consuming 3 servings of dairy products per day, the recommended daily intakes of nutrients essential for good bone health may be readily achieved. Dairy products could therefore improve bone health and reduce the risk of fractures in later life. © 2014 American Society for Nutrition. Source

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