The Experts below are selected from a list of 324 Experts worldwide ranked by ideXlab platform
Terry L. Orr-weaver - One of the best experts on this subject based on the ideXlab platform.
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Identification of ORD, a Drosophila Protein essential for sister chromatid cohesion.
The EMBO Journal, 1996Co-Authors: Sharon E. Bickel, Daniel P. Moore, Dudley Wyman, W Y Miyazaki, Terry L. Orr-weaverAbstract:Attachment between the sister chromatids is required for proper chromosome segregation in meiosis and mitosis, but its molecular basis is not understood. Mutations in the Drosophila ord gene result in premature sister chromatid separation in meiosis, indicating that the product of this gene is necessary for sister chromatid cohesion. We isolated the ord gene and found that it encodes a novel 55 kDa Protein. Some of the ord mutations exhibit unusual complementation properties, termed negative complementation, in which particular alleles poison the activity of another allele. Negative complementation predicts that Protein-Protein interactions are critical for ORD function. The position and nature of these unusual ord mutations demonstrate that the C-terminal half of ORD is essential for sister chromatid cohesion and suggest that it mediates Protein binding.
Jack E. Dixon - One of the best experts on this subject based on the ideXlab platform.
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A Drosophila Protein-tyrosine Phosphatase Associates with an Adapter Protein Required for Axonal Guidance
The Journal of biological chemistry, 1996Co-Authors: James C. Clemens, Zenovia Ursuliak, Kristina K. Clemens, James V. Price, Jack E. DixonAbstract:We have used the yeast two-hybrid system to isolate a novel Drosophila adapter Protein, which interacts with the Drosophila Protein-tyrosine phosphatase (PTP) dPTP61F. Absence of this Protein in Drosophila causes the mutant photoreceptor axon phenotype dreadlocks (dock) (Garrity, P. A., Rao, Y., Salecker, I., and Zipursky, S. L. (1996) Cell 85, 639-650). Dock is similar to the mammalian oncoProtein Nck and contains three Src homology 3 (SH3) domains and one Src homology 2 (SH2) domain. The interaction of dPTP61F with Dock was confirmed in vivo by immune precipitation experiments. A sequence containing five PXXP motifs from the non-catalytic domain of the PTP is sufficient for interaction with Dock. This suggests that binding to the PTP is mediated by one or more of the SH3 domains of Dock. Immune precipitations of Dock also co-precipitate two tyrosine-phosphorylated Proteins having molecular masses of 190 and 145 kDa. Interactions between Dock and these tyrosine-phosphorylated Proteins are likely mediated by the Dock SH2 domain. These findings identify potential signal-transducing partners of Dock and propose a role for dPTP61F and the unidentified phosphoProteins in axonal guidance.
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Alternative splicing gives rise to a nuclear Protein tyrosine phosphatase in Drosophila.
The Journal of biological chemistry, 1993Co-Authors: S Mclaughlin, Jack E. DixonAbstract:Abstract A novel Drosophila Protein tyrosine phosphatase gene (dPTP61F) undergoes alternative splicing to encode two non-receptor-like Proteins of 61,000 daltons. This splice selection occurs at the 3' end of the message, altering the carboxyl termini of the encoded Proteins. These carboxyl-terminal sequences govern the targeting of each Protein tyrosine phosphatase either to a cytoplasmic membrane or to the nucleus. The catalytic activity of the two Protein products is indistinguishable, suggesting that substrate specificity is modulated by the Protein's subcellular location.
Daniel P. Moore - One of the best experts on this subject based on the ideXlab platform.
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Identification of ORD, a Drosophila Protein essential for sister chromatid cohesion.
The EMBO Journal, 1996Co-Authors: Sharon E. Bickel, Daniel P. Moore, Dudley Wyman, W Y Miyazaki, Terry L. Orr-weaverAbstract:Attachment between the sister chromatids is required for proper chromosome segregation in meiosis and mitosis, but its molecular basis is not understood. Mutations in the Drosophila ord gene result in premature sister chromatid separation in meiosis, indicating that the product of this gene is necessary for sister chromatid cohesion. We isolated the ord gene and found that it encodes a novel 55 kDa Protein. Some of the ord mutations exhibit unusual complementation properties, termed negative complementation, in which particular alleles poison the activity of another allele. Negative complementation predicts that Protein-Protein interactions are critical for ORD function. The position and nature of these unusual ord mutations demonstrate that the C-terminal half of ORD is essential for sister chromatid cohesion and suggest that it mediates Protein binding.
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mei s332 a Drosophila Protein required for sister chromatid cohesion can localize to meiotic centromere regions
Cell, 1995Co-Authors: Anne W. Kerrebrock, Daniel P. Moore, Jim S Wu, Terry L OrrweaverAbstract:Mutations in the Drosophila mei-S332 gene cause premature separation of the sister chromatids in late anaphase of meiosis I. Therefore, the mei-S332 Protein was postulated to hold the centromere regions of sister chromatids together until anaphase II. The mei-S332 gene encodes a novel 44 kDa Protein. Mutations in mei-S332 that differentially affect function in males or females map to distinct domains of the Protein. A fusion of mei-S332 to the green fluorescent Protein (GFP) is fully functional and localizes specifically to the centromere region of meiotic chromosomes. When sister chromatids separate at anaphase II, mei-S332-GFP disappears from the chromosomes, suggesting that the destruction or release of this Protein is required for sister-chromatid separation.
Terry L Orrweaver - One of the best experts on this subject based on the ideXlab platform.
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developmental control of oocyte maturation and egg activation in metazoan models
Cold Spring Harbor Perspectives in Biology, 2011Co-Authors: Jessica R Von Stetina, Terry L OrrweaverAbstract:Production of functional eggs requires meiosis to be coordinated with developmental signals. Oocytes arrest in prophase I to permit oocyte differentiation, and in most animals, a second meiotic arrest links completion of meiosis to fertilization. Comparison of oocyte maturation and egg activation between mammals, Caenorhabditis elegans, and Drosophila reveal conserved signaling pathways and regulatory mechanisms as well as unique adaptations for reproductive strategies. Recent studies in mammals and C. elegans show the role of signaling between surrounding somatic cells and the oocyte in maintaining the prophase I arrest and controlling maturation. Proteins that regulate levels of active Cdk1/ cyclin B during prophase I arrest have been identified in Drosophila. Protein kinases play crucial roles in the transition from meiosis in the oocyte to mitotic embryonic divisions in C. elegans and Drosophila. Here we will contrast the regulation of key meiotic events in oocytes.
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mei s332 a Drosophila Protein required for sister chromatid cohesion can localize to meiotic centromere regions
Cell, 1995Co-Authors: Anne W. Kerrebrock, Daniel P. Moore, Jim S Wu, Terry L OrrweaverAbstract:Mutations in the Drosophila mei-S332 gene cause premature separation of the sister chromatids in late anaphase of meiosis I. Therefore, the mei-S332 Protein was postulated to hold the centromere regions of sister chromatids together until anaphase II. The mei-S332 gene encodes a novel 44 kDa Protein. Mutations in mei-S332 that differentially affect function in males or females map to distinct domains of the Protein. A fusion of mei-S332 to the green fluorescent Protein (GFP) is fully functional and localizes specifically to the centromere region of meiotic chromosomes. When sister chromatids separate at anaphase II, mei-S332-GFP disappears from the chromosomes, suggesting that the destruction or release of this Protein is required for sister-chromatid separation.
Vincent Mirouse - One of the best experts on this subject based on the ideXlab platform.
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DroPNet: a web portal for integrated analysis of Drosophila Protein-Protein interaction networks
Nucleic Acids Research, 2012Co-Authors: Y. Renaud, A. Baillif, J.-b. Perez, M. Agier, E. Mephu Nguifo, Vincent MirouseAbstract:DroPNet (Drosophila Protein Network) is a Drosophila-dedicated web portal for generating and analyzing Protein–Protein interaction (PPI) networks. This platform integrates users’ experimental data provided as one or two lists of genes with PPI data from Drosophila and other species. These experimental data can, for example, come from RNAi screens, for which this approach is known to be valuable. DroPNet, therefore, provides an essential basis for further biological analysis by linking functional and physical interactions and reinforcing the relevance of each. DroPNet focuses on the search of PPIs between genes of the entry list, and includes the possibility of searching for intermediate genes for which the corresponding Protein indirectly links two entry data. It also offers multiple functions for editing the networks obtained, providing users with interactive possibilities to progressively improve and refine the results. This approach gives a global view of the studied process and makes it possible to highlight specific interactions that have so far been understudied. DroPNet is freely available at http://dropnet.isima.fr.
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DroPNet: a web portal for integrated analysis of Drosophila Protein–Protein interaction networks
Nucleic Acids Research, 2012Co-Authors: Y. Renaud, A. Baillif, J.-b. Perez, M. Agier, Engelbert Mephu Nguifo, Vincent MirouseAbstract:DroPNet (Drosophila Protein Network) is a Drosophila-dedicated web portal for generating and analyzing Protein–Protein interaction (PPI) networks. This platform integrates users’ experimental data provided as one or two lists of genes with PPI data from Drosophila and other species. These experimental data can, for example, come from RNAi screens, for which this approach is known to be valuable. DroPNet, therefore, provides an essential basis for further biological analysis by linking functional and physical interactions and reinforcing the relevance of each. DroPNet focuses on the search of PPIs between genes of the entry list, and includes the possibility of searching for intermediate genes for which the corresponding Protein indirectly links two entry data. It also offers multiple functions for editing the networks obtained, providing users with interactive possibilities to progressively improve and refine the results. This approach gives a global view of the studied process and makes it possible to highlight specific interactions that have so far been understudied. DroPNet is freely available at http://dropnet.isima.fr.
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DroPNet: a web portal for integrated analysis of Drosophila Protein-Protein interaction networks
Nucleic Acids Research, 2012Co-Authors: Y. Renaud, A. Baillif, J.-b. Perez, M. Agier, E. Mephu Nguifo, Vincent MirouseAbstract:International audienceDroPNet (Drosophila Protein Network) is a Drosophila-dedicated web portal for generating and analyzing Protein–Protein interaction (PPI) networks. This platform integrates users’ experimental data provided as one or two lists of genes with PPI data from Drosophila and other species. These experimental data can, for example, come from RNAi screens, for which this approach is known to be valuable. DroPNet, therefore, provides an essential basis for further biological analysis by linking functional and physical interactions and reinforcing the relevance of each. DroPNet focuses on the search of PPIs between genes of the entry list, and includes the possibility of searching for intermediate genes for which the corresponding Protein indirectly links two entry data. It also offers multiple functions for editing the networks obtained, providing users with interactive possibilities to progressively improve and refine the results. This approach gives a global view of the studied process and makes it possible to highlight specific interactions that have so far been understudied. DroPNet is freely available at http://dropnet.isima.fr
