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Institution

University of Lausanne

EducationLausanne, 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.


Papers
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Journal ArticleDOI
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

Journal ArticleDOI
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

Journal ArticleDOI
14 Sep 2001-Science
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

Journal ArticleDOI
28 May 2004-Cell
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

Journal ArticleDOI
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

NameH-indexPapersCitations
Peer Bork206697245427
Aaron R. Folsom1811118134044
Kari Alitalo174817114231
Ralph A. DeFronzo160759132993
Johan Auwerx15865395779
Silvia Franceschi1551340112504
Matthias Egger152901184176
Bart Staels15282486638
Fernando Rivadeneira14662886582
Christopher George Tully1421843111669
Richard S. J. Frackowiak142309100726
Peter Timothy Cox140126795584
Jürg Tschopp14032886900
Stylianos E. Antonarakis13874693605
Michael Weller134110591874
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023249
2022635
20213,969
20203,508
20193,091
20182,776