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Sökning: WFRF:(Figueroa J) > Stockholms universitet

  • Resultat 1-7 av 7
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1.
  • Nielsen, K. S., et al. (författare)
  • Improving Climate Change Mitigation Analysis : A Framework for Examining Feasibility
  • 2020
  • Ingår i: One Earth. - : Elsevier BV. - 2590-3330 .- 2590-3322. ; 3:3, s. 325-336
  • Tidskriftsartikel (refereegranskat)abstract
    • Limiting global warming to 2°C or less compared with pre-industrial temperatures will require unprecedented rates of decarbonization globally. The scale and scope of transformational change required across sectors and actors in society raises critical questions of feasibility. Much of the literature on mitigation pathways addresses technological and economic aspects of feasibility, but overlooks the behavioral, cultural, and social factors that affect theoretical and practical mitigation pathways. We present a tripartite framework that “unpacks” the concept of mitigation pathways by distinguishing three factors that together determine actual mitigation: technical potential, initiative feasibility, and behavioral plasticity. The framework aims to integrate and streamline heterogeneous disciplinary research traditions toward a more comprehensive and transparent approach that will facilitate learning across disciplines and enable mitigation pathways to more fully reflect available knowledge. We offer three suggestions for integrating the tripartite framework into current research on climate change mitigation.
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2.
  • Jafferali, Mohammed Hakim, et al. (författare)
  • MCLIP, an effective method to detect interactions of transmembrane proteins of the nuclear envelope in live cells
  • 2014
  • Ingår i: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier BV. - 0005-2736 .- 1879-2642 .- 0006-3002. ; 1838:10, s. 2399-2403
  • Tidskriftsartikel (refereegranskat)abstract
    • Investigating interactions of proteins in the nuclear envelope (NE) using co-immunoprecipitation (Co-IP) has previously been difficult or even impossible due to their inherent resistance to extraction. We have developed a novel method, MCLIP (Membrane protein Cross-Link ImmunoPrecipitation), which takes advantage of a cell permeable crosslinker to enable effective detection and analysis of specific interactions of NE proteins in live cells using Western blot. Using MCLIP we show that, in U2OS cells, the integral inner nuclear membrane protein Samp1 interacts with Lamin B1, the LINC (Linker of nucleoskeleton and cytoskeleton) complex protein, Sun1 and the soluble small GTPase Ran. The results show that the previously detected in vitro interaction between Samp1 and Emerin also takes place in live cells. In vitro pull down experiments show, that the nucleoplasmic domains of Samp1 and Emerin can bind directly to each other. We also, show that MCLIP is suitable to coprecipitate protein interactions in different stages of the cell cycle.
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  • Larsson, Veronica J., et al. (författare)
  • Mitotic spindle assembly and γ-tubulin localisation depend on the integral nuclear membrane protein, Samp1
  • 2018
  • Ingår i: Journal of Cell Science. - : The Company of Biologists. - 0021-9533 .- 1477-9137. ; 131:8
  • Tidskriftsartikel (refereegranskat)abstract
    • We have investigated a possible role of the inner nuclear membrane protein, Samp1, in the mitotic machinery. Live cell imaging showed that Samp1aYFP distributed as filamentous structures in the mitotic spindle, partially co-localising with ß-tubulin. Samp1 depletion resulted in an increased frequency of cells with signs of chromosomal mis-segregation and prolonged metaphase, indicating problems with spindle assembly and/or chromosomal alignment. Consistently, mitotic spindles in Samp1 depleted cells contained significantly lower levels of ß-tubulin and γ-tubulin, phenotypes which were rescued by overexpression of Samp1aYFP. We found that Samp1 can bind directly to γ-tubulin and that Samp1 co-precipitated with γ-tubulin and HAUS6 of the Augmin complex in live cells. The levels of Haus6, in the mitotic spindle also decreased after Samp1 depletion. We show that Samp1 is involved in the recruitment of Haus6 and γ-tubulin to the mitotic spindle. Samp1 is the first inner nuclear membrane protein shown to have a function in mitotic spindle assembly.
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  • Vijayaraghavan, Balaje, et al. (författare)
  • RanGTPase regulates the interaction between the inner nuclear membrane proteins, Samp1 and Emerin
  • 2018
  • Ingår i: Biochimica et Biophysica Acta - Biomembranes. - : Elsevier BV. - 0005-2736 .- 1879-2642. ; 1860:6, s. 1326-1334
  • Tidskriftsartikel (refereegranskat)abstract
    • Samp1, spindle associated membrane protein 1, is a type II integral membrane protein localized in the inner nuclear membrane. Recent studies have shown that the inner nuclear membrane protein, Emerin and the small monomeric GTPase, Ran are direct binding partners of Samp1. Here we addressed the question whether Ran could regulate the interaction between Samp1 and Emerin in the inner nuclear membrane. To investigate the interaction between Samp1 and Emerin in live cells, we performed FRAP experiments in cells overexpressing YFP-Emerin. We compared the mobility of YFP-Emerin in Samp1 knock out cells and cells overexpressing Samp1. The results showed that the mobility of YFP-Emerin was higher in Samp1 knock out cells and lower in cells overexpressing Samp1, suggesting that Samp1 significantly attenuates the mobility of Emerin in the nuclear envelope. FRAP experiments using tsBN2 cells showed that the mobility of Emerin depends on RanGTP. Consistently, in vitro binding experiments showed that the affinity between Samp1 and Emerin is decreased in the presence of Ran, suggesting that Ran attenuates the interaction between Samp1 and Emerin. This is the first demonstration that Ran can regulate the interaction between two proteins in the nuclear envelope.
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  • Resultat 1-7 av 7

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