Jonca, Nathalie; Caubet, Cécile; Leclerc, Emilie A; Guerrin, Marina; Simon, Michel; Serre, Guy Protease sensitivity of corneodesmosin variants encoded by the six more common CDSN haplotypes. Journal Article In: The journal of investigative dermatology, vol. 131, no. 6, pp. 1381–1384, 2011, ISSN: 1523-1747 (Electronic). @article{Jonca2011,
title = {Protease sensitivity of corneodesmosin variants encoded by the six more common CDSN haplotypes.},
author = {Jonca, Nathalie and Caubet, Cécile and Leclerc, Emilie A and Guerrin, Marina and Simon, Michel and Serre, Guy},
doi = {10.1038/jid.2011.7},
issn = {1523-1747 (Electronic)},
year = {2011},
date = {2011-06-01},
booktitle = {The Journal of investigative dermatology},
journal = {The journal of investigative dermatology},
volume = {131},
number = {6},
pages = {1381--1384},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Viret, C.; Leung-Theung-Long, S.; Serre, L.; C.and Vignali Lamare, D. A. and Malissen; Carrier, A.; Guerder, S. Thymus-specific serine protease controls autoreactive CD4 T cell development and autoimmune diabetes in mice. Journal Article In: J Clin Invest , vol. 121, no. 5, pp. 1810-1821, 2011. @article{Viret2011,
title = { Thymus-specific serine protease controls autoreactive CD4 T cell development and autoimmune diabetes in mice.},
author = {Viret, C. and Leung-Theung-Long, S. and Serre, L. and Lamare, C.and Vignali, D.A.and Malissen, B. and Carrier, A. and Guerder, S. },
url = {https://www.ncbi.nlm.nih.gov/pubmed/?term=Thymus-specific+serine+protease+controls+autoreactive+CD4+T+cell+development+and+autoimmune+diabetes+in+mice.},
doi = { 10.1172/JCI43314},
year = {2011},
date = {2011-05-01},
journal = {J Clin Invest },
volume = {121},
number = {5},
pages = {1810-1821},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Henry, Julie; Hsu, Chiung-Yueh; Haftek, Marek; Nachat, Rachida; de Koning, Heleen D; Gardinal-Galera, Isabelle; Hitomi, Kiyotaka; Balica, Stéfana; Jean-Decoster, Catherine; Schmitt, Anne-Marie; Paul, Carle; Serre, Guy; Simon, Michel Hornerin is a component of the epidermal cornified cell envelopes. Journal Article In: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, vol. 25, no. 5, pp. 1567–1576, 2011, ISSN: 1530-6860 (Electronic). @article{Henry2011,
title = {Hornerin is a component of the epidermal cornified cell envelopes.},
author = {Henry, Julie and Hsu, Chiung-Yueh and Haftek, Marek and Nachat, Rachida and de Koning, Heleen D and Gardinal-Galera, Isabelle and Hitomi, Kiyotaka and Balica, Stéfana and Jean-Decoster, Catherine and Schmitt, Anne-Marie and Paul, Carle and Serre, Guy and Simon, Michel},
doi = {10.1096/fj.10-168658},
issn = {1530-6860 (Electronic)},
year = {2011},
date = {2011-05-01},
journal = {FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
volume = {25},
number = {5},
pages = {1567--1576},
abstract = {A single-nucleotide polymorphism within the gene encoding hornerin (HRNR) has recently been linked with atopic dermatitis (AD) susceptibility. HRNR shares features with filaggrin, a key protein for keratinocyte differentiation, but conflicting reports have been published concerning its expression in the epidermis, and its role is still unknown. To analyze HRNR expression and function in the epidermis, anti-HRNR antibodies were produced and used in Western blot analysis and immunohistochemical, confocal, and immunoelectron microscopy analyses of human skin and of cornified cell envelopes purified from plantar stratum corneum. We also tested whether HRNR was a substrate of transglutaminases. In the epidermis, HRNR was detected at the periphery of keratohyalin granules in the upper granular layer and at the corneocyte periphery in the whole cornified layer. Detected in Western blot analysis as numerous bands, HRNR was relatively insoluble and only extracted from epidermis with urea and/or reducing agents. The presence of HRNR in the purified envelopes was confirmed by immunoelectron microscopy and by Western blot analysis after V8-protease digestion. HRNR was shown to be a substrate of transglutaminase 3. These data demonstrate that HRNR is a component of cornified cell envelopes of human epidermis. Its reduced expression in AD may contribute to the epidermal barrier defect observed in the disease.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A single-nucleotide polymorphism within the gene encoding hornerin (HRNR) has recently been linked with atopic dermatitis (AD) susceptibility. HRNR shares features with filaggrin, a key protein for keratinocyte differentiation, but conflicting reports have been published concerning its expression in the epidermis, and its role is still unknown. To analyze HRNR expression and function in the epidermis, anti-HRNR antibodies were produced and used in Western blot analysis and immunohistochemical, confocal, and immunoelectron microscopy analyses of human skin and of cornified cell envelopes purified from plantar stratum corneum. We also tested whether HRNR was a substrate of transglutaminases. In the epidermis, HRNR was detected at the periphery of keratohyalin granules in the upper granular layer and at the corneocyte periphery in the whole cornified layer. Detected in Western blot analysis as numerous bands, HRNR was relatively insoluble and only extracted from epidermis with urea and/or reducing agents. The presence of HRNR in the purified envelopes was confirmed by immunoelectron microscopy and by Western blot analysis after V8-protease digestion. HRNR was shown to be a substrate of transglutaminase 3. These data demonstrate that HRNR is a component of cornified cell envelopes of human epidermis. Its reduced expression in AD may contribute to the epidermal barrier defect observed in the disease. |
Jonca, Nathalie; Leclerc, Emilie A; Caubet, Cécile; Simon, Michel; Guerrin, Marina; Serre, Guy Corneodesmosomes and corneodesmosin: from the stratum corneum cohesion to the pathophysiology of genodermatoses. Journal Article In: European journal of dermatology : EJD, vol. 21 Suppl 2, pp. 35–42, 2011, ISSN: 1167-1122 (Print). @article{Jonca2011b,
title = {Corneodesmosomes and corneodesmosin: from the stratum corneum cohesion to the pathophysiology of genodermatoses.},
author = {Jonca, Nathalie and Leclerc, Emilie A and Caubet, Cécile and Simon, Michel and Guerrin, Marina and Serre, Guy},
doi = {10.1684/ejd.2011.1264},
issn = {1167-1122 (Print)},
year = {2011},
date = {2011-05-01},
journal = {European journal of dermatology : EJD},
volume = {21 Suppl 2},
pages = {35--42},
abstract = {Corneodesmosin (CDSN) was identified 20 years ago by raising monoclonal antibodies against human plantar stratum corneum. The protein is specific to corneodesmosomes, cell-junction structures that, in humans, are found in the epidermis, the hard palate epithelium, and the inner root sheath of the hair follicles. Synthesized by the granular keratinocytes and secreted via the lamellar bodies, CDSN is incorporated into the desmoglea of the desmosomes, shortly before their transformation into corneodesmosomes during cornification. CDSN displays adhesive properties, mostly attributable to its N-terminal glycine-rich domain, and is sequentially proteolyzed as corneocytes migrate towards the skin surface prior to desquamation. The recent inactivation of Cdsn in mice induced a lethal epidermal barrier disruption and hair follicle degeneration, related to corneodesmosome dysfunction. That confirmed the essential role of the protein in maintaining integrity of the epidermis and the hair follicle. The CDSN gene is located in PSORS1, the major psoriasis susceptibility locus on the chromosome 6, but to date its involvement in the disease pathophysiology is not clear. By contrast, two different monogenic diseases associated with nonsense mutations in CDSN, were recently identified. First, hypotrichosis simplex of the scalp in which mutated CDSN accumulates in the dermis and forms amyloid deposits; then, peeling skin disease in which the genetic defect induces dyscohesion of the stratum corneum, responsible for abnormal desquamation and increased skin penetration of allergens.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Corneodesmosin (CDSN) was identified 20 years ago by raising monoclonal antibodies against human plantar stratum corneum. The protein is specific to corneodesmosomes, cell-junction structures that, in humans, are found in the epidermis, the hard palate epithelium, and the inner root sheath of the hair follicles. Synthesized by the granular keratinocytes and secreted via the lamellar bodies, CDSN is incorporated into the desmoglea of the desmosomes, shortly before their transformation into corneodesmosomes during cornification. CDSN displays adhesive properties, mostly attributable to its N-terminal glycine-rich domain, and is sequentially proteolyzed as corneocytes migrate towards the skin surface prior to desquamation. The recent inactivation of Cdsn in mice induced a lethal epidermal barrier disruption and hair follicle degeneration, related to corneodesmosome dysfunction. That confirmed the essential role of the protein in maintaining integrity of the epidermis and the hair follicle. The CDSN gene is located in PSORS1, the major psoriasis susceptibility locus on the chromosome 6, but to date its involvement in the disease pathophysiology is not clear. By contrast, two different monogenic diseases associated with nonsense mutations in CDSN, were recently identified. First, hypotrichosis simplex of the scalp in which mutated CDSN accumulates in the dermis and forms amyloid deposits; then, peeling skin disease in which the genetic defect induces dyscohesion of the stratum corneum, responsible for abnormal desquamation and increased skin penetration of allergens. |
Brasse-Lagnel, Carole; Karim, Zoubida; Letteron, Philippe; Bekri, Soumeya; Bado, André; Beaumont, Carole Intestinal DMT1 cotransporter is down-regulated by hepcidin via proteasome internalization and degradation Journal Article In: Gastroenterology, vol. 140, no. 4, pp. 1261–1271.e1, 2011, ISSN: 1528-0012. @article{brasse-lagnel_intestinal_2011,
title = {Intestinal DMT1 cotransporter is down-regulated by hepcidin via proteasome internalization and degradation},
author = {Brasse-Lagnel, Carole and Karim, Zoubida and Letteron, Philippe and Bekri, Soumeya and Bado, André and Beaumont, Carole},
doi = {10.1053/j.gastro.2010.12.037},
issn = {1528-0012},
year = {2011},
date = {2011-04-01},
journal = {Gastroenterology},
volume = {140},
number = {4},
pages = {1261--1271.e1},
abstract = {BACKGROUNDS & AIMS: The mechanism by which hepcidin regulates iron export from macrophages has been well established and is believed to involve degradation of ferroportin. However, in the small intestine, hepcidin's mechanisms of action are not known. We studied human polarized intestinal (Caco-2/TC7) cells and mouse duodenal segments, ex vivo, to investigate the molecular mechanisms by which hepcidin down-regulates intestinal transepithelial iron transport.
METHODS: Iron transport was analyzed using ⁵⁵FeNTA. Expression of Divalent Metal Transporter 1 (DMT1) and ferroportin was evaluated by reverse-transcription quantitative polymerase chain reaction and immunoblotting. Videomicroscopy analysis was performed on live cells that expressed either DMT1 or ferroportin fused to green fluorescent protein.
RESULTS: In Caco-2/TC7 cells, physiologic doses of hepcidin (50-1000 nmol/L) inhibited transport of ⁵⁵Fe in a dose-dependent manner; a half-maximum effect was observed at 75-100 nmol/L. However, 200 nmol/L hepcidin induced a significant decrease in DMT1 protein expression but no change in ferroportin protein levels, unlike macrophages. This result was confirmed ex vivo in isolated duodenal segments: 200 nmol/L hepcidin induced a significant reduction in iron transport and DMT1 protein levels but no change in ferroportin levels. In Caco-2/TC7 cells, the effect of hepcidin on the DMT1 protein level was completely abolished in the presence of a proteasome inhibitor (MG-132); DMT1 ubiquitination was induced by the addition of hepcidin.
CONCLUSIONS: An acute increase in hepcidin concentration reduces intestinal iron absorption through ubiquitin-dependent proteasome degradation of DMT1.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
BACKGROUNDS & AIMS: The mechanism by which hepcidin regulates iron export from macrophages has been well established and is believed to involve degradation of ferroportin. However, in the small intestine, hepcidin's mechanisms of action are not known. We studied human polarized intestinal (Caco-2/TC7) cells and mouse duodenal segments, ex vivo, to investigate the molecular mechanisms by which hepcidin down-regulates intestinal transepithelial iron transport.
METHODS: Iron transport was analyzed using ⁵⁵FeNTA. Expression of Divalent Metal Transporter 1 (DMT1) and ferroportin was evaluated by reverse-transcription quantitative polymerase chain reaction and immunoblotting. Videomicroscopy analysis was performed on live cells that expressed either DMT1 or ferroportin fused to green fluorescent protein.
RESULTS: In Caco-2/TC7 cells, physiologic doses of hepcidin (50-1000 nmol/L) inhibited transport of ⁵⁵Fe in a dose-dependent manner; a half-maximum effect was observed at 75-100 nmol/L. However, 200 nmol/L hepcidin induced a significant decrease in DMT1 protein expression but no change in ferroportin protein levels, unlike macrophages. This result was confirmed ex vivo in isolated duodenal segments: 200 nmol/L hepcidin induced a significant reduction in iron transport and DMT1 protein levels but no change in ferroportin levels. In Caco-2/TC7 cells, the effect of hepcidin on the DMT1 protein level was completely abolished in the presence of a proteasome inhibitor (MG-132); DMT1 ubiquitination was induced by the addition of hepcidin.
CONCLUSIONS: An acute increase in hepcidin concentration reduces intestinal iron absorption through ubiquitin-dependent proteasome degradation of DMT1. |
Leclerc, Emilie A; Gazeilles, Leila; Serre, Guy; Guerrin, Marina; Jonca, Nathalie The ubiquitous dermokine delta activates Rab5 function in the early endocytic pathway. Journal Article In: PloS one, vol. 6, no. 3, pp. e17816, 2011, ISSN: 1932-6203 (Electronic). @article{Leclerc2011,
title = {The ubiquitous dermokine delta activates Rab5 function in the early endocytic pathway.},
author = {Leclerc, Emilie A and Gazeilles, Leila and Serre, Guy and Guerrin, Marina and Jonca, Nathalie},
doi = {10.1371/journal.pone.0017816},
issn = {1932-6203 (Electronic)},
year = {2011},
date = {2011-03-01},
journal = {PloS one},
volume = {6},
number = {3},
pages = {e17816},
abstract = {The expression of the recently identified dermokine (Dmkn) gene leads to four families of proteins with as yet unknown functions. The secreted $alpha$, $beta$ and $gamma$ isoforms share an epidermis-restricted expression pattern, whereas the $delta$ isoform is intracellular and ubiquitous. To get an insight into Dmkn$delta$ function, we performed yeast two-hybrid screening and identified the small GTPases Rab5 as partners for Dmkn$delta$. The Rab5 proteins are known to regulate membrane docking and fusion in the early endocytic pathway. GST pull-down assays confirmed the direct interaction between Rab5 and Dmkn$delta$. Transient expression of Dmkn$delta$ in HeLa cells led to the formation of punctate structures colocalized with endogenous Rab5 and clathrin, indicating Dmkn$delta$ involvement in the early steps of endocytosis. Dmkn$delta$ indeed colocalized with transferrin at early stages of endocytosis, but did not modulate its endocytosis or recycling kinetics. We also showed that Dmkn$delta$ was able to bind both inactive (GDP-bound) and active (GTP-bound) forms of Rab5 in vitro but preferentially targeted GDP-bound form in HeLa cells. Interestingly, Dmkn$delta$ expression rescued the Rab5S34N-mediated inhibition of endosome fusion. Moreover, Dmkn$delta$ caused the enlargement of vesicles positive for Rab5 by promoting GTP loading onto the small GTPase. Together our data reveal that Dmkn$delta$ activates Rab5 function and thus is involved in the early endosomal trafficking.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The expression of the recently identified dermokine (Dmkn) gene leads to four families of proteins with as yet unknown functions. The secreted $alpha$, $beta$ and $gamma$ isoforms share an epidermis-restricted expression pattern, whereas the $delta$ isoform is intracellular and ubiquitous. To get an insight into Dmkn$delta$ function, we performed yeast two-hybrid screening and identified the small GTPases Rab5 as partners for Dmkn$delta$. The Rab5 proteins are known to regulate membrane docking and fusion in the early endocytic pathway. GST pull-down assays confirmed the direct interaction between Rab5 and Dmkn$delta$. Transient expression of Dmkn$delta$ in HeLa cells led to the formation of punctate structures colocalized with endogenous Rab5 and clathrin, indicating Dmkn$delta$ involvement in the early steps of endocytosis. Dmkn$delta$ indeed colocalized with transferrin at early stages of endocytosis, but did not modulate its endocytosis or recycling kinetics. We also showed that Dmkn$delta$ was able to bind both inactive (GDP-bound) and active (GTP-bound) forms of Rab5 in vitro but preferentially targeted GDP-bound form in HeLa cells. Interestingly, Dmkn$delta$ expression rescued the Rab5S34N-mediated inhibition of endosome fusion. Moreover, Dmkn$delta$ caused the enlargement of vesicles positive for Rab5 by promoting GTP loading onto the small GTPase. Together our data reveal that Dmkn$delta$ activates Rab5 function and thus is involved in the early endosomal trafficking. |
Mattiuzzo, Nicolas R; Toulza, Eve; Jonca, Nathalie; Serre, Guy; Guerrin, Marina A large-scale multi-technique approach identifies forty-nine new players of keratinocyte terminal differentiation in human epidermis. Journal Article In: Experimental dermatology, vol. 20, no. 2, pp. 113–118, 2011, ISSN: 1600-0625 (Electronic). @article{Mattiuzzo2011,
title = {A large-scale multi-technique approach identifies forty-nine new players of keratinocyte terminal differentiation in human epidermis.},
author = {Mattiuzzo, Nicolas R and Toulza, Eve and Jonca, Nathalie and Serre, Guy and Guerrin, Marina},
doi = {10.1111/j.1600-0625.2010.01188.x},
issn = {1600-0625 (Electronic)},
year = {2011},
date = {2011-02-01},
journal = {Experimental dermatology},
volume = {20},
number = {2},
pages = {113--118},
abstract = {At the latest stage of terminal differentiation in the epidermis, granular keratinocytes (GKs) undergo cornification, a programmed cell death required for the establishment of a functional skin barrier. A complex genetic regulatory network orchestrates the underlying biochemical modifications, but very few transcription factors specific to this programme have been identified to date. Here, we describe a large-scale, multi-technique approach performed on cells purified from normal human epidermis, primarily focusing on the identification of regulators. We combined data from microarray analysis of cell fractions enriched in GKs or basal keratinocytes, from an expressed sequence tag (EST) library built from GKs and from an in silico promoter analysis of 52 differentiation-associated genes. Among 3576 genes potentially expressed in GK, 298 candidates were selected, and half were directly profiled for the first time in the different layers of the epidermis by quantitative real-time PCR. Forty-nine genes upregulated during terminal differentiation, associated with numerous function of GK including lipid synthesis and secretion, were identified. Of 94 transcription factors detected, 37 were found to be either positively or negatively regulated, suggesting their involvement as regulators of gene expression in the GKs. These results largely extend the number of genes known as involved in the latest step of the terminal differentiation of human epidermis as well as the number of transcription factors known to control the expression of these genes.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
At the latest stage of terminal differentiation in the epidermis, granular keratinocytes (GKs) undergo cornification, a programmed cell death required for the establishment of a functional skin barrier. A complex genetic regulatory network orchestrates the underlying biochemical modifications, but very few transcription factors specific to this programme have been identified to date. Here, we describe a large-scale, multi-technique approach performed on cells purified from normal human epidermis, primarily focusing on the identification of regulators. We combined data from microarray analysis of cell fractions enriched in GKs or basal keratinocytes, from an expressed sequence tag (EST) library built from GKs and from an in silico promoter analysis of 52 differentiation-associated genes. Among 3576 genes potentially expressed in GK, 298 candidates were selected, and half were directly profiled for the first time in the different layers of the epidermis by quantitative real-time PCR. Forty-nine genes upregulated during terminal differentiation, associated with numerous function of GK including lipid synthesis and secretion, were identified. Of 94 transcription factors detected, 37 were found to be either positively or negatively regulated, suggesting their involvement as regulators of gene expression in the GKs. These results largely extend the number of genes known as involved in the latest step of the terminal differentiation of human epidermis as well as the number of transcription factors known to control the expression of these genes. |
Vasilopoulos, Yiannis; Sharaf, Nazar; di Giovine, Franco; Simon, Michel; Cork, Michael J; Duff, Gordon W; Tazi-Ahnini, Rachid The 3'-UTR AACCins5874 in the stratum corneum chymotryptic enzyme gene (SCCE/KLK7), associated with atopic dermatitis; causes an increased mRNA expression without altering its stability. Journal Article In: Journal of dermatological science, vol. 61, no. 2, pp. 131–133, 2011, ISSN: 1873-569X (Electronic). @article{Vasilopoulos2011,
title = {The 3'-UTR AACCins5874 in the stratum corneum chymotryptic enzyme gene (SCCE/KLK7), associated with atopic dermatitis; causes an increased mRNA expression without altering its stability.},
author = {Vasilopoulos, Yiannis and Sharaf, Nazar and di Giovine, Franco and Simon, Michel and Cork, Michael J and Duff, Gordon W and Tazi-Ahnini, Rachid},
doi = {10.1016/j.jdermsci.2010.11.013},
issn = {1873-569X (Electronic)},
year = {2011},
date = {2011-02-01},
booktitle = {Journal of dermatological science},
journal = {Journal of dermatological science},
volume = {61},
number = {2},
pages = {131--133},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Viret, C.; Lamare, C.; Guiraud, M.; Fazilleau, N.; Bour, A.; Malissen, B.; Carrier, A.; Guerder, S. Thymus-specific serine protease contributes to the diversification of the functional endogenous CD4 T cell receptor repertoire. Journal Article In: J Exp Med., vol. 208, pp. 3-11, 2011. @article{Viret2011b,
title = {Thymus-specific serine protease contributes to the diversification of the functional endogenous CD4 T cell receptor repertoire. },
author = {Viret, C. and Lamare, C. and Guiraud, M. and Fazilleau, N. and Bour, A. and Malissen, B. and Carrier, A. and Guerder, S. },
url = {https://www.ncbi.nlm.nih.gov/pubmed/21173102},
doi = {10.1084/jem.20100027},
year = {2011},
date = {2011-01-17},
journal = {J Exp Med.},
volume = {208},
pages = {3-11},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Gennero, I.; Laurencin-Dalicieux, S.; Conte-Auriol, F.; Briand-Mesange, F.; Laurencin, D.; Rue, J.; Beton, N.; Malet, N.; Mus, M.; Tokumura, A.; Bourin, P.; Vico, L.; Brunel, G.; Oreffo, R. O.; Chun, J.; Salles, J. P. Absence of the lysophosphatidic acid receptor LPA1 results in abnormal bone development and decreased bone mass Journal Article In: Bone, vol. 49, no. 3, pp. 395-403, 2011, ISSN: 1873-2763 (Electronic)
1873-2763 (Linking). @article{RN21b,
title = {Absence of the lysophosphatidic acid receptor LPA1 results in abnormal bone development and decreased bone mass},
author = {Gennero, I. and Laurencin-Dalicieux, S. and Conte-Auriol, F. and Briand-Mesange, F. and Laurencin, D. and Rue, J. and Beton, N. and Malet, N. and Mus, M. and Tokumura, A. and Bourin, P. and Vico, L. and Brunel, G. and Oreffo, R. O. and Chun, J. and Salles, J. P.},
url = {https://www.ncbi.nlm.nih.gov/pubmed/21569876},
doi = {10.1016/j.bone.2011.04.018},
issn = {1873-2763 (Electronic)
1873-2763 (Linking)},
year = {2011},
date = {2011-01-01},
journal = {Bone},
volume = {49},
number = {3},
pages = {395-403},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Boyer, J. F.; Gourraud, P. A.; Cantagrel, A.; Davignon, J. L.; Constantin, A. Traditional cardiovascular risk factors in rheumatoid arthritis: a meta-analysis Journal Article In: Joint Bone Spine, vol. 78, no. 2, pp. 179-83, 2011, ISSN: 1778-7254 (Electronic)
1297-319X (Linking). @article{RN27,
title = {Traditional cardiovascular risk factors in rheumatoid arthritis: a meta-analysis},
author = {Boyer, J. F. and Gourraud, P. A. and Cantagrel, A. and Davignon, J. L. and Constantin, A.},
url = {https://www.ncbi.nlm.nih.gov/pubmed/20851020},
doi = {10.1016/j.jbspin.2010.07.016},
issn = {1778-7254 (Electronic)
1297-319X (Linking)},
year = {2011},
date = {2011-01-01},
journal = {Joint Bone Spine},
volume = {78},
number = {2},
pages = {179-83},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Courties, G.; Baron, M.; Presumey, J.; Escriou, V.; van Lent, P.; Scherman, D.; Cantagrel, A.; van den Berg, W. B.; Jorgensen, C.; Apparailly, F.; Davignon, J. L. Cytosolic phospholipase A2alpha gene silencing in the myeloid lineage alters development of Th1 responses and reduces disease severity in collagen-induced arthritis Journal Article In: Arthritis Rheum, vol. 63, no. 3, pp. 681-90, 2011, ISSN: 1529-0131 (Electronic)
0004-3591 (Linking). @article{RN13b,
title = {Cytosolic phospholipase A2alpha gene silencing in the myeloid lineage alters development of Th1 responses and reduces disease severity in collagen-induced arthritis},
author = {Courties, G. and Baron, M. and Presumey, J. and Escriou, V. and van Lent, P. and Scherman, D. and Cantagrel, A. and van den Berg, W. B. and Jorgensen, C. and Apparailly, F. and Davignon, J. L.},
url = {https://www.ncbi.nlm.nih.gov/pubmed/21360497},
doi = {10.1002/art.30174},
issn = {1529-0131 (Electronic)
0004-3591 (Linking)},
year = {2011},
date = {2011-01-01},
journal = {Arthritis Rheum},
volume = {63},
number = {3},
pages = {681-90},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Hayder, Myriam; Poupot, Mary; Baron, Michel; Nigon, Delphine; Turrin, Cédric-Olivier; Caminade, Anne-Marie; Majoral, Jean-Pierre; Eisenberg, Robert A.; Fournié, Jean-Jacques; Cantagrel, Alain; Poupot, Rémy; Davignon, Jean-Luc A Phosphorus-Based Dendrimer Targets Inflammation
and Osteoclastogenesis in Experimental Arthritis Journal Article In: Sci. Transl. Med, vol. 3, no. 81 81ra35, 2011. @article{RN34,
title = {A Phosphorus-Based Dendrimer Targets Inflammation
and Osteoclastogenesis in Experimental Arthritis},
author = {Myriam Hayder and Mary Poupot and Michel Baron and Delphine Nigon and Cédric-Olivier Turrin and Anne-Marie Caminade and Jean-Pierre Majoral and Robert A. Eisenberg and Jean-Jacques Fournié and Alain Cantagrel and Rémy Poupot and Davignon, Jean-Luc},
year = {2011},
date = {2011-01-01},
journal = {Sci. Transl. Med},
volume = {3},
number = {81 81ra35},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Hayder, Myriam; Poupot, Mary; Baron, Michel; Nigon, Delphine; Turrin, Cédric-Olivier; Caminade, Anne-Marie; Majoral, Jean-Pierre; Eisenberg, Robert A.; Fournié, Jean-Jacques; Cantagrel, Alain; Poupot, Rémy; Davignon, Jean-Luc A Phosphorus-Based Dendrimer Targets Inflammation
and Osteoclastogenesis in Experimental Arthritis Journal Article In: Sci. Transl. Med, vol. 3, no. 81 81ra35, 2011. @article{RN34b,
title = {A Phosphorus-Based Dendrimer Targets Inflammation
and Osteoclastogenesis in Experimental Arthritis},
author = {Myriam Hayder and Mary Poupot and Michel Baron and Delphine Nigon and Cédric-Olivier Turrin and Anne-Marie Caminade and Jean-Pierre Majoral and Robert A. Eisenberg and Jean-Jacques Fournié and Alain Cantagrel and Rémy Poupot and Davignon, Jean-Luc},
year = {2011},
date = {2011-01-01},
journal = {Sci. Transl. Med},
volume = {3},
number = {81 81ra35},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
|
Nouzé, C.; Pasquet, L.; van Meerwijk, J. P. M. In vitro expansion of alloantigen-specific regulatory T cells and their use in prevention of allograft-rejection Book Chapter In: Kassiotis, G.; Liston, A. (Ed.): Regulatory T-Cells: Methods and Protocols, vol. 707, pp. 187-196, Springer, 2011. @inbook{RN157,
title = {In vitro expansion of alloantigen-specific regulatory T cells and their use in prevention of allograft-rejection},
author = {Nouzé, C. and Pasquet, L. and van Meerwijk, J. P. M.},
editor = {Kassiotis, G. and Liston, A.},
year = {2011},
date = {2011-01-01},
booktitle = {Regulatory T-Cells: Methods and Protocols},
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Pasquet, Lise; Joffre, Olivier; Santolaria, Thibault; van Meerwijk, Joost Hematopoietic chimerism and transplantation tolerance: a role for regulatory T cells Journal Article In: Frontiers in Immunology, vol. 2, 2011, ISSN: 1664-3224. @article{RN163,
title = {Hematopoietic chimerism and transplantation tolerance: a role for regulatory T cells},
author = {Pasquet, Lise and Joffre, Olivier and Santolaria, Thibault and van Meerwijk, Joost},
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Pomie, C.; Vicente, R.; Vuddamalay, Y.; Ardesjö Lundgren, B.; van der Hoek, M.; Enault, G.; Kagan, J.; Fazilleau, N; Scott, H. S.; Romagnoli, P.; van Meerwijk, J. P. M. AIRE-deficient CD8+CD28low regulatory T lymphocytes fail to control experimental colitis Journal Article In: Proceedings of the National Academy of Sciences of the U.S.A., vol. 108, no. 30, pp. 12437-12442, 2011. @article{RN162,
title = {AIRE-deficient CD8+CD28low regulatory T lymphocytes fail to control experimental colitis},
author = {Pomie, C. and Vicente, R. and Vuddamalay, Y. and Ardesjö Lundgren, B. and van der Hoek, M. and Enault, G. and Kagan, J. and Fazilleau, N and Scott, H. S. and Romagnoli, P. and van Meerwijk, J.P.M.},
year = {2011},
date = {2011-01-01},
journal = {Proceedings of the National Academy of Sciences of the U.S.A.},
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Colacios, C.; Casemayou, A.; Dejean, A. S.; Gaits-Iacovoni, F.; Pedros, C.; Bernard, I.; Lagrange, D.; Deckert, M.; Lamouroux, L.; Jagodic, M.; Olsson, T.; Liblau, R. S.; Fournie, G. J.; Saoudi, A. The p.Arg63Trp polymorphism controls Vav1 functions and Foxp3 regulatory T cell development Journal Article In: J Exp Med, vol. 208, no. 11, pp. 2183-91, 2011, ISSN: 1540-9538 (Electronic)
0022-1007 (Linking). @article{RN14b,
title = {The p.Arg63Trp polymorphism controls Vav1 functions and Foxp3 regulatory T cell development},
author = {Colacios, C. and Casemayou, A. and Dejean, A. S. and Gaits-Iacovoni, F. and Pedros, C. and Bernard, I. and Lagrange, D. and Deckert, M. and Lamouroux, L. and Jagodic, M. and Olsson, T. and Liblau, R. S. and Fournie, G. J. and Saoudi, A.},
url = {http://www.ncbi.nlm.nih.gov/pubmed/21948080},
doi = {10.1084/jem.20102191},
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year = {2011},
date = {2011-01-01},
journal = {J Exp Med},
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Couturier, N.; Bucciarelli, F.; Nurtdinov, R. N.; Debouverie, M.; Lebrun-Frenay, C.; Defer, G.; Moreau, T.; Confavreux, C.; Vukusic, S.; Cournu-Rebeix, I.; Goertsches, R. H.; Zettl, U. K.; Comabella, M.; Montalban, X.; Rieckmann, P.; Weber, F.; Muller-Myhsok, B.; Edan, G.; Fontaine, B.; Mars, L. T.; Saoudi, A.; Oksenberg, J. R.; Clanet, M.; Liblau, R. S.; Brassat, D. Tyrosine kinase 2 variant influences T lymphocyte polarization and multiple sclerosis susceptibility Journal Article In: Brain, vol. 134, no. Pt 3, pp. 693-703, 2011, ISSN: 1460-2156 (Electronic)
0006-8950 (Linking). @article{RN8b,
title = {Tyrosine kinase 2 variant influences T lymphocyte polarization and multiple sclerosis susceptibility},
author = {Couturier, N. and Bucciarelli, F. and Nurtdinov, R. N. and Debouverie, M. and Lebrun-Frenay, C. and Defer, G. and Moreau, T. and Confavreux, C. and Vukusic, S. and Cournu-Rebeix, I. and Goertsches, R. H. and Zettl, U. K. and Comabella, M. and Montalban, X. and Rieckmann, P. and Weber, F. and Muller-Myhsok, B. and Edan, G. and Fontaine, B. and Mars, L. T. and Saoudi, A. and Oksenberg, J. R. and Clanet, M. and Liblau, R. S. and Brassat, D.},
url = {http://www.ncbi.nlm.nih.gov/pubmed/21354972},
doi = {10.1093/brain/awr010},
issn = {1460-2156 (Electronic)
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year = {2011},
date = {2011-01-01},
journal = {Brain},
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Dejean, A. S.; Hedrick, S. M.; Kerdiles, Y. M. Highly specialized role of Forkhead box O transcription factors in the immune system Journal Article In: Antioxid Redox Signal, vol. 14, no. 4, pp. 663-74, 2011, ISSN: 1557-7716 (Electronic)
1523-0864 (Linking). @article{RN18b,
title = {Highly specialized role of Forkhead box O transcription factors in the immune system},
author = {Dejean, A. S. and Hedrick, S. M. and Kerdiles, Y. M.},
url = {http://www.ncbi.nlm.nih.gov/pubmed/20673126},
doi = {10.1089/ars.2010.3414},
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year = {2011},
date = {2011-01-01},
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