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NumreringReferensOmslagsbildHitta
1021.
  • Schmitz, Birger (författare)
  • How a world came to be
  • 2012
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 485:7396, s. 39-39
  • Recension (övrigt vetenskapligt)
  •  
1022.
  • Schmitz, Birger (författare)
  • The cosmological you
  • 2013
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 493:7430, s. 25-25
  • Recension (övrigt vetenskapligt)
  •  
1023.
  •  
1024.
  • Schnadt, Joachim, et al. (författare)
  • Experimental evidence for sub-3-fs charge transfer from an aromatic adsorbate to a semiconductor
  • 2002
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 418:6898, s. 620-623
  • Tidskriftsartikel (refereegranskat)abstract
    • The ultrafast timescale of electron transfer processes is crucial to their role in many biological systems and technological devices. In dye-sensitized solar cells(1-4), the electron transfer from photoexcited dye molecules to nanostructured semiconductor substrates needs to be sufficiently fast to compete effectively against loss processes and thus achieve high solar energy conversion efficiencies(4). Time-resolved laser techniques indicate an upper limit of 20 to 100 femtoseconds(5-9) for the time needed to inject an electron from a dye into a semiconductor, which corresponds to the timescale on which competing processes such as charge redistribution(10,11) and intramolecular thermalization of excited states(12-14) occur. Here we use resonant photoemission spectroscopy, which has previously been used to monitor electron transfer in simple systems with an order-of-magnitude improvement in time resolution(15,16), to show that electron transfer from an aromatic adsorbate to a TiO2 semiconductor surface can occur in less than 3 fs. These results directly confirm that electronic coupling of the aromatic molecule to its substrate is sufficiently strong to suppress competing processes(17).
  •  
1025.
  •  
1026.
  • Schoebel, Stefan, et al. (författare)
  • Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3
  • 2017
  • Ingår i: Nature. - 0028-0836. ; 548:7667, s. 352-
  • Tidskriftsartikel (refereegranskat)abstract
    • Misfolded endoplasmic reticulum proteins are retro-translocated through the membrane into the cytosol, where they are poly-ubiquitinated, extracted from the membrane, and degraded by the proteasome(1-4)-a pathway termed endoplasmic reticulum-associated protein degradation (ERAD). Proteins with misfolded domains in the endoplasmic reticulum lumen or membrane are discarded through the ERAD-L and ERAD-M pathways, respectively. In Saccharomyces cerevisiae, both pathways require the ubiquitin ligase Hrd1, a multi-spanning membrane protein with a cytosolic RING finger domain(5,6). Hrd1 is the crucial membrane component for retro-translocation(7,8), but it is unclear whether it forms a protein-conducting channel. Here we present a cryo-electron microscopy structure of S. cerevisiae Hrd1 in complex with its endoplasmic reticulum luminal binding partner, Hrd3. Hrd1 forms a dimer within the membrane with one or two Hrd3 molecules associated at its luminal side. Each Hrd1 molecule has eight transmembrane segments, five of which form an aqueous cavity extending from the cytosol almost to the endoplasmic reticulum lumen, while a segment of the neighbouring Hrd1 molecule forms a lateral seal. The aqueous cavity and lateral gate are reminiscent of features of protein-conducting conduits that facilitate polypeptide movement in the opposite direction-from the cytosol into or across membranes(9-11). Our results suggest that Hrd1 forms a retro-translocation channel for the movement of misfolded polypeptides through the endoplasmic reticulum membrane.
  •  
1027.
  • Scholze, Marko (författare)
  • Earth network.
  • 2007
  • Ingår i: Nature. - Nature Publishing Group. - 0028-0836. ; 447:7141
  • Tidskriftsartikel (refereegranskat)
  •  
1028.
  •  
1029.
  •  
1030.
  •  
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