The Experts below are selected from a list of 117 Experts worldwide ranked by ideXlab platform
Bernard Moussian - One of the best experts on this subject based on the ideXlab platform.
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The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila.
Scientific reports, 2019Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a putative C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
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The C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila
2018Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
Renata Zuber - One of the best experts on this subject based on the ideXlab platform.
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The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila.
Scientific reports, 2019Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a putative C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
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The C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila
2018Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
Khaleelulla Saheb Shaik - One of the best experts on this subject based on the ideXlab platform.
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The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila.
Scientific reports, 2019Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a putative C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
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The C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila
2018Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
Frauke Meyer - One of the best experts on this subject based on the ideXlab platform.
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The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila.
Scientific reports, 2019Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a putative C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
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The C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila
2018Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
Anna Speidel - One of the best experts on this subject based on the ideXlab platform.
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The putative C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila.
Scientific reports, 2019Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a putative C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.
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The C-type lectin Schlaff ensures epidermal barrier compactness in Drosophila
2018Co-Authors: Renata Zuber, Khaleelulla Saheb Shaik, Frauke Meyer, Anna Speidel, Nicole Gehring, Slawomir Bartoszewski, Heinz Schwarz, Bernard MoussianAbstract:The stability of extracellular matrices is in general ensured by cross-linking of its components. Previously, we had shown that the integrity of the layered Drosophila cuticle relies on the presence of a covalent cuticular dityrosine network. Production and composition of this structure remained unstudied. In this work, we present our analyses of the schlaff (slf) gene coding for a C-type lectin that is needed for the adhesion between the horizontal cuticle layers. The Slf protein mainly localizes between the two layers called Epicuticle and procuticle that separate from each other when the function of Slf is reduced or eliminated paralleling the phenotype of a cuticle with reduced extracellular dityrosine. Localisation of the dityrosinylated protein Resilin to the Epicuticle-procuticle interface suggests that the dityrosine network mediates the adhesion of the Epicuticle to the procuticle. Ultimately, compromised Slf function is associated with massive water loss. In summary, we propose that Slf is implied in the stabilisation of a dityrosine layer especially between the Epicuticle and the procuticle that in turn constitutes an outward barrier against uncontrolled water flow.