Institution
University of Lausanne
Education•Lausanne, Switzerland•
About: University of Lausanne is a education organization based out in Lausanne, Switzerland. It is known for research contribution in the topics: Population & Poison control. The organization has 20508 authors who have published 46458 publications receiving 1996655 citations. The organization is also known as: Université de Lausanne & UNIL.
Topics: Population, Poison control, Immune system, Cytotoxic T cell, T cell
Papers published on a yearly basis
Papers
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TL;DR: The BAFF system provides not only potential insight into the development of autoreactive B cells but a relatively simple paradigm to begin considering the balancing act between survival, growth, and death that affects all cells.
Abstract: BAFF, a member of the TNF family, is a fundamental survival factor for transitional and mature B cells. BAFF overexpression leads to an expanded B cell compartment and autoimmunity in mice, and elevated amounts of BAFF can be found in the serum of autoimmune patients. APRIL is a related factor that shares receptors with BAFF yet appears to play a different biological role. The BAFF system provides not only potential insight into the development of autoreactive B cells but a relatively simple paradigm to begin considering the balancing act between survival, growth, and death that affects all cells.
944 citations
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University of Vienna1, Austrian Academy of Sciences2, Ilia State University3, Slovak Academy of Sciences4, University of Innsbruck5, University of Granada6, Mediterranean Agronomic Institute of Chania7, Norwegian University of Science and Technology8, Russian Academy of Sciences9, University of Molise10, Babeș-Bolyai University11, University of Pavia12, University of Geneva13, University of Parma14, University of Lausanne15, Open University of Cyprus16
TL;DR: In this article, the authors used 867 vegetation samples above the treeline from 60 summit sites in all major European mountain systems to show that ongoing climate change gradually transforms mountain plant communities.
Abstract: Climate impact studies have indicated ecological fingerprints of recent global warming across a wide range of habitats1, 2. Although these studies have shown responses from various local case studies, a coherent large-scale account on temperature-driven changes of biotic communities has been lacking3, 4. Here we use 867 vegetation samples above the treeline from 60 summit sites in all major European mountain systems to show that ongoing climate change gradually transforms mountain plant communities. We provide evidence that the more cold-adapted species decline and the more warm-adapted species increase, a process described here as thermophilization. At the scale of individual mountains this general trend may not be apparent, but at the larger, continental scale we observed a significantly higher abundance of thermophilic species in 2008, compared with 2001. Thermophilization of mountain plant communities mirrors the degree of recent warming and is more pronounced in areas where the temperature increase has been higher. In view of the projected climate change5, 6 the observed transformation suggests a progressive decline of cold mountain habitats and their biota.
943 citations
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TL;DR: BAFF-R appears to be the principal receptor for BAFF-mediated mature B cell survival and is disrupted in A/WySnJ mice, which display a B cell phenotype qualitatively similar to that of the BAff-deficient mice.
Abstract: B cell homeostasis has been shown to critically depend on BAFF, the B cell activation factor from the tumor necrosis factor (TNF) family Although BAFF is already known to bind two receptors, BCMA and TACI, we have identified a third receptor for BAFF that we have termed BAFF-R BAFF-R binding appears to be highly specific for BAFF, suggesting a unique role for this ligand-receptor interaction Consistent with this, the BAFF-R locus is disrupted in A/WySnJ mice, which display a B cell phenotype qualitatively similar to that of the BAFF-deficient mice Thus, BAFF-R appears to be the principal receptor for BAFF-mediated mature B cell survival
942 citations
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TL;DR: Mutations in one of the scaffold proteins of the inflammasome, NALP3/Cryopyrin, are associated with autoinflammatory disorders underscoring the importance of regulating inflammatory caspase activation.
942 citations
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University of Lausanne1, University of Strasbourg2, Merck & Co.3, University of Cambridge4, University of California, Los Angeles5, National Institutes of Health6, University of Nice Sophia Antipolis7, University of Tokyo8, University of Pennsylvania9, University of Dundee10, Brigham and Women's Hospital11, Harvard University12, French Institute of Health and Medical Research13
TL;DR: The three peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors of the nuclear hormone receptor superfamily as discussed by the authors, which share a high degree of structural homology with all members of the superfamily, particularly in the DNA-binding domain and ligand and cofactor binding domain.
Abstract: The three peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors of the nuclear hormone receptor superfamily. They share a high degree of structural homology with all members of the superfamily, particularly in the DNA-binding domain and ligand- and cofactor-binding domain. Many cellular and systemic roles have been attributed to these receptors, reaching far beyond the stimulation of peroxisome proliferation in rodents after which they were initially named. PPARs exhibit broad, isotype-specific tissue expression patterns. PPARalpha is expressed at high levels in organs with significant catabolism of fatty acids. PPARbeta/delta has the broadest expression pattern, and the levels of expression in certain tissues depend on the extent of cell proliferation and differentiation. PPARgamma is expressed as two isoforms, of which PPARgamma2 is found at high levels in the adipose tissues, whereas PPARgamma1 has a broader expression pattern. Transcriptional regulation by PPARs requires heterodimerization with the retinoid X receptor (RXR). When activated by a ligand, the dimer modulates transcription via binding to a specific DNA sequence element called a peroxisome proliferator response element (PPRE) in the promoter region of target genes. A wide variety of natural or synthetic compounds was identified as PPAR ligands. Among the synthetic ligands, the lipid-lowering drugs, fibrates, and the insulin sensitizers, thiazolidinediones, are PPARalpha and PPARgamma agonists, respectively, which underscores the important role of PPARs as therapeutic targets. Transcriptional control by PPAR/RXR heterodimers also requires interaction with coregulator complexes. Thus, selective action of PPARs in vivo results from the interplay at a given time point between expression levels of each of the three PPAR and RXR isotypes, affinity for a specific promoter PPRE, and ligand and cofactor availabilities.
932 citations
Authors
Showing all 20911 results
Name | H-index | Papers | Citations |
---|---|---|---|
Peer Bork | 206 | 697 | 245427 |
Aaron R. Folsom | 181 | 1118 | 134044 |
Kari Alitalo | 174 | 817 | 114231 |
Ralph A. DeFronzo | 160 | 759 | 132993 |
Johan Auwerx | 158 | 653 | 95779 |
Silvia Franceschi | 155 | 1340 | 112504 |
Matthias Egger | 152 | 901 | 184176 |
Bart Staels | 152 | 824 | 86638 |
Fernando Rivadeneira | 146 | 628 | 86582 |
Christopher George Tully | 142 | 1843 | 111669 |
Richard S. J. Frackowiak | 142 | 309 | 100726 |
Peter Timothy Cox | 140 | 1267 | 95584 |
Jürg Tschopp | 140 | 328 | 86900 |
Stylianos E. Antonarakis | 138 | 746 | 93605 |
Michael Weller | 134 | 1105 | 91874 |