The Experts below are selected from a list of 90 Experts worldwide ranked by ideXlab platform
Miska Luoto - One of the best experts on this subject based on the ideXlab platform.
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Appendix F. Response shapes (Partial Dependency plots) for the zooplankton Daphnia galeata based on GBM models.
2016Co-Authors: Janne Soininen, Jenni J. Korhonen, Miska LuotoAbstract:Response shapes (Partial Dependency plots) for the zooplankton Daphnia galeata based on GBM models
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Appendix E. Response shapes (Partial Dependency plots) for the phytoplankton Staurastrum sp. based on GBM models.
2016Co-Authors: Janne Soininen, Jenni J. Korhonen, Miska LuotoAbstract:Response shapes (Partial Dependency plots) for the phytoplankton Staurastrum sp. based on GBM models
Janne Soininen - One of the best experts on this subject based on the ideXlab platform.
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Appendix F. Response shapes (Partial Dependency plots) for the zooplankton Daphnia galeata based on GBM models.
2016Co-Authors: Janne Soininen, Jenni J. Korhonen, Miska LuotoAbstract:Response shapes (Partial Dependency plots) for the zooplankton Daphnia galeata based on GBM models
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Appendix E. Response shapes (Partial Dependency plots) for the phytoplankton Staurastrum sp. based on GBM models.
2016Co-Authors: Janne Soininen, Jenni J. Korhonen, Miska LuotoAbstract:Response shapes (Partial Dependency plots) for the phytoplankton Staurastrum sp. based on GBM models
Jenni J. Korhonen - One of the best experts on this subject based on the ideXlab platform.
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Appendix F. Response shapes (Partial Dependency plots) for the zooplankton Daphnia galeata based on GBM models.
2016Co-Authors: Janne Soininen, Jenni J. Korhonen, Miska LuotoAbstract:Response shapes (Partial Dependency plots) for the zooplankton Daphnia galeata based on GBM models
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Appendix E. Response shapes (Partial Dependency plots) for the phytoplankton Staurastrum sp. based on GBM models.
2016Co-Authors: Janne Soininen, Jenni J. Korhonen, Miska LuotoAbstract:Response shapes (Partial Dependency plots) for the phytoplankton Staurastrum sp. based on GBM models
Debyser Zeger - One of the best experts on this subject based on the ideXlab platform.
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Interplay between HIV entry and transportin-SR2 Dependency
'Springer Science and Business Media LLC', 2011Co-Authors: Thys Wannes, De Houwer Stéphanie, Demeulemeester Jonas, Taltynov Oliver, Vancraenenbroeck Renée, Gérard Melanie, De Rijck Jan, Gijsbers Rik, Christ Frauke, Debyser ZegerAbstract:BACKGROUND: Transportin-SR2 (TRN-SR2, TNPO3, transportin 3) was previously identified as an interaction partner of human immunodeficiency virus type 1 (HIV-1) integrase and functions as a nuclear import factor of HIV-1. A possible role of capsid in transportin-SR2-mediated nuclear import was recently suggested by the findings that a chimeric HIV virus, carrying the murine leukemia virus (MLV) capsid and matrix proteins, displayed a transportin-SR2 independent phenotype, and that the HIV-1 N74D capsid mutant proved insensitive to transportin-SR2 knockdown. RESULTS: Our present analysis of viral specificity reveals that TRN-SR2 is not used to the same extent by all lentiviruses. The DNA flap does not determine the TRN-SR2 requirement of HIV-1. We corroborate the TRN-SR2 independent phenotype of the chimeric HIV virus carrying the MLV capsid and matrix proteins. We reanalyzed the HIV-1 N74D capsid mutant in cells transiently or stably depleted of transportin-SR2 and confirm that the N74D capsid mutant is independent of TRN-SR2 when pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G). Remarkably, although somewhat less dependent on TRN-SR2 than wild type virus, the N74D capsid mutant carrying the wild type HIV-1 envelope required TRN-SR2 for efficient replication. By pseudotyping with envelopes that mediate pH-independent viral uptake including HIV-1, measles virus and amphotropic MLV envelopes, we demonstrate that HIV-1 N74D capsid mutant viruses retain Partial Dependency on TRN-SR2. However, this Dependency on TRN-SR2 is lost when the HIV N74D capsid mutant is pseudotyped with envelopes mediating pH-dependent endocytosis, such as the VSV-G and Ebola virus envelopes. CONCLUSION: Here we discover a link between the viral entry of HIV and its interaction with TRN-SR2. Our data confirm the importance of TRN-SR2 in HIV-1 replication and argue for careful interpretation of experiments performed with VSV-G pseudotyped viruses in studies on early steps of HIV replication including the role of capsid therein.status: publishe
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Interplay between HIV Entry and Transportin-SR2 Dependency
BMC, 2011Co-Authors: Gijsbers Rik, Thys Wannes, De Houwer Stéphanie, Demeulemeester Jonas, Taltynov Oliver, Vancraenenbroeck Renée, Gérard Melanie, De Rijck Jan, Christ Frauke, Debyser ZegerAbstract:Abstract Background Transportin-SR2 (TRN-SR2, TNPO3, transportin 3) was previously identified as an interaction partner of human immunodeficiency virus type 1 (HIV-1) integrase and functions as a nuclear import factor of HIV-1. A possible role of capsid in transportin-SR2-mediated nuclear import was recently suggested by the findings that a chimeric HIV virus, carrying the murine leukemia virus (MLV) capsid and matrix proteins, displayed a transportin-SR2 independent phenotype, and that the HIV-1 N74D capsid mutant proved insensitive to transportin-SR2 knockdown. Results Our present analysis of viral specificity reveals that TRN-SR2 is not used to the same extent by all lentiviruses. The DNA flap does not determine the TRN-SR2 requirement of HIV-1. We corroborate the TRN-SR2 independent phenotype of the chimeric HIV virus carrying the MLV capsid and matrix proteins. We reanalyzed the HIV-1 N74D capsid mutant in cells transiently or stably depleted of transportin-SR2 and confirm that the N74D capsid mutant is independent of TRN-SR2 when pseudotyped with the vesicular stomatitis virus glycoprotein (VSV-G). Remarkably, although somewhat less dependent on TRN-SR2 than wild type virus, the N74D capsid mutant carrying the wild type HIV-1 envelope required TRN-SR2 for efficient replication. By pseudotyping with envelopes that mediate pH-independent viral uptake including HIV-1, measles virus and amphotropic MLV envelopes, we demonstrate that HIV-1 N74D capsid mutant viruses retain Partial Dependency on TRN-SR2. However, this Dependency on TRN-SR2 is lost when the HIV N74D capsid mutant is pseudotyped with envelopes mediating pH-dependent endocytosis, such as the VSV-G and Ebola virus envelopes. Conclusion Here we discover a link between the viral entry of HIV and its interaction with TRN-SR2. Our data confirm the importance of TRN-SR2 in HIV-1 replication and argue for careful interpretation of experiments performed with VSV-G pseudotyped viruses in studies on early steps of HIV replication including the role of capsid therein.
Xinyu Wang - One of the best experts on this subject based on the ideXlab platform.
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epistemic logic with Partial Dependency operator
International Workshop on Logic Rationality and Interaction, 2019Co-Authors: Xinyu WangAbstract:In this paper, we introduce Partial Dependency modality \(\mathcal {D}\) into epistemic logic so as to reason about Partial Dependency relationship in Kripke models. The resulted dependence epistemic logic possesses decent expressivity and beautiful properties. Several interesting examples are provided, which highlight this logic’s practical usage. The logic’s bisimulation is then discussed, and we give a sound and strongly complete axiomatization for a sub-language of the logic.
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epistemic logic with Partial Dependency operator
arXiv: Logic, 2019Co-Authors: Xinyu WangAbstract:In this paper, we introduce $\textit{Partial}$ Dependency modality $\mathcal{D}$ into epistemic logic so as to reason about $\textit{Partial}$ Dependency relationship in Kripke models. The resulted dependence epistemic logic possesses decent expressivity and beautiful properties. Several interesting examples are provided, which highlight this logic's practical usage. The logic's bisimulation is then discussed, and we give a sound and strongly complete axiomatization for a sub-language of the logic.