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Träfflista för sökning "L773:1545 9985 OR L773:1545 9993 srt2:(2005-2009)"

Sökning: L773:1545 9985 OR L773:1545 9993 > (2005-2009)

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1.
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2.
  • Banci, L, et al. (författare)
  • Structural proteomics: from the molecule to the system
  • 2007
  • Ingår i: Nature structural & molecular biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 14:1, s. 3-4
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)
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3.
  • Ekwall, Karl (författare)
  • 'Arc' escorts siRNAs in heterochromatin assembly
  • 2007
  • Ingår i: Nature Structural & Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 14:3, s. 178-179
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • RNA interference (RNAi) is important in directing heterochromatin assembly at centromeres in fission yeast, which is crucial for maintaining a stable genome through mitotic and meiotic divisions. In this issue, Buker et al. describe a new Argonaute siRNA chaperone (ARC) that converts duplex RNA to single-stranded RNA. This is a previously unknown step in the RNAi-directed heterochromatin-formation pathway.
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4.
  • Fong, Nova, et al. (författare)
  • Fast ribozyme cleavage releases transcripts from RNA polymerase II and aborts co-transcriptional pre-mRNA processing
  • 2009
  • Ingår i: Nature Structural & Molecular Biology. - : Nature America Inc. - 1545-9993 .- 1545-9985. ; 16:9, s. 916-923
  • Tidskriftsartikel (refereegranskat)abstract
    • Adenosine-to-inosine (A-to-I) editing has been shown to be an important mechanism that increases protein diversity in the brain of organisms from human to fly. The family of ADAR enzymes converts some adenosines of RNA duplexes to inosines through hydrolytic deamination. The adenosine recognition mechanism is still largely unknown. Here, to investigate it, we analyzed a set of selectively edited substrates with a cluster of edited sites. We used a large set of individual transcripts sequenced by the 454 sequencing technique. On average, we analyzed 570 single transcripts per edited region at four different developmental stages from embryogenesis to adulthood. To our knowledge, this is the first time, large-scale sequencing has been used to determine synchronous editing events. We demonstrate that edited sites are only coupled within specific distances from each other. Furthermore, our results show that the coupled sites of editing are positioned on the same side of a helix, indicating that the three-dimensional structure is key in ADAR enzyme substrate recognition. Finally, we propose that editing by the ADAR enzymes is initiated by their attraction to one principal site in the substrate.
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5.
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7.
  • Macao, Bertil, 1969, et al. (författare)
  • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin.
  • 2006
  • Ingår i: Nature structural & molecular biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 13:1, s. 71-6
  • Tidskriftsartikel (refereegranskat)abstract
    • The single cell layer of the lungs and the gastrointestinal tract is protected by the mucus formed by large glycoproteins called mucins. Transmembrane mucins typically contain 110-residue SEA domains located next to the membrane. These domains undergo post-translational cleavage between glycine and serine in a characteristic GSVVV sequence, but the two peptides remain tightly associated. We show that the SEA domain of the human MUC1 transmembrane mucin undergoes a novel type of autoproteolysis, which is catalyzed by conformational stress and the conserved serine hydroxyl. We propose that self-cleaving SEA domains have evolved to dissociate as a result of mechanical rather than chemical stress at the apical cell membrane and that this protects epithelial cells from rupture. We further suggest that the cell can register mechanical shear at the mucosal surface if the dissociation is signaled via loss of a SEA-binding protein.
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8.
  • Paeschke, Katrin, et al. (författare)
  • Telomerase recruitment by the telomere end binding protein-beta facilitates G-quadruplex DNA unfolding in ciliates.
  • 2008
  • Ingår i: Nature structural & molecular biology. - : Springer Science and Business Media LLC. - 1545-9985 .- 1545-9993. ; 15:6, s. 598-604
  • Tidskriftsartikel (refereegranskat)abstract
    • The telomeric G-overhangs of the ciliate Stylonychia lemnae fold into a G-quadruplex DNA structure in vivo. Telomeric G-quadruplex formation requires the presence of two telomere end binding proteins, TEBPalpha and TEBPbeta, and is regulated in a cell-cycle dependent manner. Unfolding of this structure in S phase is dependent on the phosphorylation of TEBPbeta. Here we show that TEBPbeta phosphorylation is necessary but not sufficient for a G-quadruplex unfolding rate compatible with telomere synthesis. The telomerase seems to be actively involved in telomeric G-quadruplex DNA structure unfolding in vivo. Significantly, the telomerase is recruited to telomeres by phosphorylated TEBPbeta, and hence telomerase recruitment is cell-cycle regulated through phosphorylation. These observations allow us to propose a model for the regulation of G-quadruplex unfolding and telomere synthesis during the cell cycle.
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10.
  • Persson, B David, et al. (författare)
  • Adenovirus type 11 binding alters the conformation of its receptor CD46.
  • 2007
  • Ingår i: Nature Structural & Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 14:2, s. 164-166
  • Tidskriftsartikel (refereegranskat)abstract
    • Adenoviruses (Ads) are important human pathogens and valuable gene delivery vehicles. We report here the crystal structure of the species B Ad11 knob complexed with the Ad11-binding region of its receptor CD46. The conformation of bound CD46 differs profoundly from its unbound state, with the bent surface structure straightened into an elongated rod. This mechanism of interaction is likely to be conserved among many pathogens that target CD46 or related molecules.
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11.
  • Rapp, Mikaela, et al. (författare)
  • Identification and evolution of dual-topology membrane proteins
  • 2006
  • Ingår i: Nature Structural & Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 13:2, s. 112-116
  • Tidskriftsartikel (refereegranskat)abstract
    • Integral membrane proteins are generally believed to have unique membrane topologies. However, it has been suggested that dual-topology proteins that adopt a mixture of two opposite orientations in the membrane may exist. Here we show that the membrane orientations of five dual-topology candidates identified in Escherichia coli are highly sensitive to changes in the distribution of positively charged residues, that genes in families containing dual-topology candidates occur in genomes either as pairs or as singletons and that gene pairs encode two oppositely oriented proteins whereas singletons encode dual-topology candidates. Our results provide strong support for the existence of dual-topology proteins and shed new light on the evolution of membrane-protein topology and structure.
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12.
  • Sheng, Yi, et al. (författare)
  • Molecular basis of Pirh2-mediated p53 ubiquitylation
  • 2008
  • Ingår i: NATURE STRUCTURAL and MOLECULAR BIOLOGY. - : Springer Science and Business Media LLC. - 1545-9985 .- 1545-9993. ; 15:12, s. 1334-1342
  • Tidskriftsartikel (refereegranskat)abstract
    • Pirh2 (p53-induced RING-H2 domain protein; also known as Rchy1) is an E3 ubiquitin ligase involved in a negative-feedback loop with p53. Using NMR spectroscopy, we show that Pirh2 is a unique cysteine-rich protein comprising three modular domains. The protein binds nine zinc ions using a variety of zinc coordination schemes, including a RING domain and a left-handed beta-spiral in which three zinc ions align three consecutive small beta-sheets in an interleaved fashion. We show that Pirh2-p53 interaction is dependent on the C-terminal zinc binding module of Pirh2, which binds to the tetramerization domain of p53. As a result, Pirh2 preferentially ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting that Pirh2 regulates protein turnover of the transcriptionally active form of p53.
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13.
  • Wagner, Gerhart E. H. (författare)
  • Kill the messenger : bacterial antisense RNA promotes mRNA decay.
  • 2009
  • Ingår i: Nature Structural & Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 16:8, s. 804-806
  • Tidskriftsartikel (refereegranskat)abstract
    • Bacterial antisense RNAs target translation initiation regions (TIR s) to compete with ribosome binding, thus repressing translation and—secondarily—causing degradation of the naked mRNA. A new study reports on an antisense RNA that directly accelerates mRNA decay by targeting a sequence deep within the coding region, far downstream of the TIR.
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14.
  • Weixlbaumer, Albert, et al. (författare)
  • Crystal structure of the ribosome recycling factor bound to the ribosome
  • 2007
  • Ingår i: Nature Structural & Molecular Biology. - : Springer Science and Business Media LLC. - 1545-9993 .- 1545-9985. ; 14:8, s. 733-737
  • Tidskriftsartikel (refereegranskat)abstract
    • In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNAfMet in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.
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15.
  • von Heijne, Gunnar (författare)
  • Helices on the move.
  • 2005
  • Ingår i: Nat Struct Mol Biol. - 1545-9993. ; 12:10, s. 834-5
  • Tidskriftsartikel (refereegranskat)
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