| 1. |
- Abercrombie, Daniel, et al.
(författare)
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Dark Matter benchmark models for early LHC Run-2 Searches : Report of the ATLAS/CMS Dark Matter Forum
- 2020
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Ingår i: Physics of the Dark Universe. - : Elsevier BV. - 2212-6864. ; 27
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Tidskriftsartikel (refereegranskat)abstract
- This document is the final report of the ATLAS-CMS Dark Matter Forum, a forum organized by the ATLAS and CMS collaborations with the participation of experts on theories of Dark Matter, to select a minimal basis set of dark matter simplified models that should support the design of the early LHC Run-2 searches. A prioritized, compact set of benchmark models is proposed, accompanied by studies of the parameter space of these models and a repository of generator implementations. This report also addresses how to apply the Effective Field Theory formalism for collider searches and present the results of such interpretations.
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| 2. |
- Shen, Nannan, et al.
(författare)
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Designing Polymorphic Bi3+-Containing Ionic Liquids for Stimuli-Responsive Luminescent Materials
- 2019
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Ingår i: Inorganic Chemistry. - : American Chemical Society (ACS). - 0020-1669 .- 1520-510X. ; 58:12, s. 8079-8085
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Tidskriftsartikel (refereegranskat)abstract
- Solid-state luminescent materials that possess reversible fluorescence changes toward external multistimuli are of immense interest because of their potential applications in data storage and sensors. While the recent developments in this field are mainly focused on the pi-conjugated organic molecules. Herein two polymorphic luminescent ionic liquid (IL)-based stimuli-responsive materials were designed by the supramolecular assemblies of an organic-decorated chlorobismuthate anion and a rotationally flexible imidazolium cation, namely, alpha (1)/beta (2)-[Bmmim][BiCl4(2,2'-bpy)] (Bmmim = 1-butyl-2,3-dimethylimidazolium; 2,2'-bpy = 2,2'-bipyridine). Because of the different conformations of the n-butyl chains on the imidazolium cations, tuning of the supramolecular packing structures as well as luminescent colors for 1 and 2 was realized. Single-crystal X-ray diffraction and Hirshfeld surface analyses disclose that the poly-morphism-dependent emission may be attributed to the different weak interactions, especially to the pi-pi interactions between adjacent [BiCl4(2,2'-bpy)](-) anions in two compounds. Additionally, compound 2 could be transformed into 1 spontaneously at ambient conditions, which could be triggered by the moisture in the air. Both of the title compounds could detect NH(3 )vapor selectively through the luminescence "turn-off" method rapidly and reversibly because of the destruction of intermolecular interactions, indicating their stimuli-responsive property toward NH3.
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| 3. |
- Yu, Guimei, et al.
(författare)
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Structure of Arabidopsis SOQ1 lumenal region unveils C-terminal domain essential for negative regulation of photoprotective qH
- 2022
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Ingår i: Nature Plants. - : Nature Publishing Group. - 2055-0278. ; 8:7, s. 840-855
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Tidskriftsartikel (refereegranskat)abstract
- Non-photochemical quenching (NPQ) plays an important role for phototrophs in decreasing photo-oxidative damage. qH is a sustained form of NPQ and depends on the plastid lipocalin (LCNP). A thylakoid membrane-anchored protein SUPPRESSOR OF QUENCHING1 (SOQ1) prevents qH formation by inhibiting LCNP. SOQ1 suppresses qH with its lumen-located thioredoxin (Trx)-like and NHL domains. Here we report structural data, genetic modification and biochemical characterization of Arabidopsis SOQ1 lumenal domains. Our results show that the Trx-like and NHL domains are associated together, with the cysteine motif located at their interface. Residue E859, required for SOQ1 function, is pivotal for maintaining the Trx–NHL association. Importantly, the C-terminal region of SOQ1 forms an independent β-stranded domain that has structural homology to the N-terminal domain of bacterial disulfide bond protein D and is essential for negative regulation of qH. Furthermore, SOQ1 is susceptible to cleavage at the loops connecting the neighbouring lumenal domains both in vitro and in vivo, which could be a regulatory process for its suppression function of qH.
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| 4. |
- Yu, Guimei, et al.
(författare)
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Structure of SOQ1 lumenal domains identifies potential disulfide exchange for negative regulation of photoprotection, qH
- 2024
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Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
- Non-photochemical quenching (NPQ) plays an important role for phototrophs in decreasing photo-oxidative damage. qH is a sustained component of NPQ and depends on the plastid lipocalin (LCNP). A thylakoid membrane-anchored protein SUPPRESSOR OF QUENCHING1 (SOQ1) prevents qH formation by inhibiting LCNP. SOQ1 suppresses qH with its lumen-located C-terminal Trx-like and NHL domains. Here we report crystal structures and biochemical characterization of SOQ1 lumenal domains. Our results show that the Trx-like and NHL domains are stably associated, with the potential redox-active motif located at their interface. Residue E859 essential for SOQ1 function is pivotal for mediating the inter-domain interaction. Moreover, the C-terminal region of SOQ1 forms an independent β-stranded domain, which possibly interacts with the Trx-like domain through disulfide exchange. Furthermore, SOQ1 is susceptible to cleavage at the loops connecting the neighboring domains both in vitro and in vivo, which could be a regulatory process for its suppression function of qH.
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