| 1. |
- Andersson, Sören, 1957-, et al.
(författare)
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CHIMERIC MOMP ANTIGEN
- 2015
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Patent (populärvet., debatt m.m.)
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| 2. |
- Andersson, Sören, 1957-, et al.
(författare)
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Chimeric MOMP antigen
- 2014
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Patent (populärvet., debatt m.m.)abstract
- The present invention regards polypeptides capable of eliciting an immunological response that is protective against Chlamydia trachomatis. The polypeptide comprises a first amino acid sequence which has at least 90% homology with the amino acid sequence according to SEQ ID NO: 1 and a second amino acid sequence which has at least 90% homology with the amino acid sequence according to SEQ ID NO: 2. Furthermore, production of these polypeptides and pharmaceutical compositions comprising them are also provided.
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| 3. |
- Jirle, Erling, et al.
(författare)
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Förändringar i Tk:s lista : Rapport 12 från Taxonomikommittén
- 2022
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Ingår i: Vår Fågelvärld. - 0042-2649. ; 2022:1, s. 28-32
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Tidskriftsartikel (populärvet., debatt m.m.)abstract
- Här presenteras några av de senaste besluten inom BirdLife Sveriges Taxonomikommitté. Den fullständiga rapporten, inklusive referenser, finns på birdlife.se/tk, liksom en uppdaterad Västpalearktislista (VP7).
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| 4. |
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| 5. |
- Chumnarnsilpa, Sakesit, 1967-, et al.
(författare)
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The crystal structure of the C-terminus of adseverin: Implications for actin binding
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Annan publikation (populärvet., debatt m.m.)abstract
- Adseverin is a member of the calcium-regulated gelsolin superfamily of actin severing and capping proteins. Adseverin comprises six homologous domains (A1-A6) which share 60% homology with the six domains from gelsolin (G1-G6). Adseverin is truncated in comparison to gelsolin, lacking the C-terminal extension which masks the F-actin binding site in calcium-free gelsolin. Biochemical assays have indicated differences in the interaction of the C-terminus halves of adseverin and gelsolin with actin. Gelsolin contacts actin through a major site on G4 and a minor site on G6, while adseverin uses a site on A5. Here we present the X-ray structure of the activated C-terminal half of adseverin (A4-A6). This structure is highly similar to that of the activated form of the C-terminal half of gelsolin (G4-G6), both in arrangement of domains and in the three bound calcium ions. Comparative analysis of the actin-binding surfaces observed in the G4-G6/actin structure suggests that adseverin in this conformation will also be able to interact with actin through A4 and A6, while the A5 surface is obscured. A model of calcium-free adseverin constructed from the structure of gelsolin predicts that the interaction between A2 and A6 provides sterric inhibition to prevent interaction with F-actin in the absence of calcium. Actin-binding assays reveal that the minimal stoichiometry of adseverin to calcium needed to disassemble actin filaments is 1:1 as compared to the 1:2 that was previously observed for gelsolin. We propose that the absence of a gelsolin-like C-terminal extension in adseverin reduces the calcium requirement for activation.
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| 6. |
- Ellervik, Ulf
(författare)
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Vem ska rädda oss från palmoljan?
- 2023
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Ingår i: Svenska Dagbladet, - Under strecket. - 1101-2412.
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Tidskriftsartikel (populärvet., debatt m.m.)
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| 7. |
- Eriksson, Leif A., 1964-, et al.
(författare)
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Tetrazole derivatives as cytochrome p450 inhibitors
- 2019
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Patent (populärvet., debatt m.m.)abstract
- According to the invention there is provided a compound of formula I, wherein R1 and R2 have meanings given in the description, which compounds are useful in the treatment of skin disorders and other diseases.
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| 8. |
- Strand, Malin, et al.
(författare)
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Slemmaskens hemlighet
- 2016
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Ingår i: Forskning & Framsteg. - Stockholm : Stiftelsen Forskning & Framsteg. - 0015-7937. ; :2, s. 26-33
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Tidskriftsartikel (populärvet., debatt m.m.)abstract
- Nyckeln till framtidens mediciner kan gömma sig hos slemmiga, giftiga maskar som lever på havets botten. Här berättar marinbiologen Malin Strand och biokemisten Håkan Andersson om jakten som ledde till en oväntad upptäckt – och som tog slemmasken från det marinbiologiska laboratoriet på Tjärnö och Sveriges västkust till kemilaboratoriet i Uppsala.
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| 9. |
- Bakshi, Arindam, et al.
(författare)
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Interaction of the intrinsically disordered C-terminal domain of the sesbania mosaic virus RNA-dependent RNA polymerase with the viral protein P10 in vitro: modulation of the oligomeric state and polymerase activity
- 2019
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Ingår i: Archives of Virology. - : Springer Science and Business Media LLC. - 0304-8608 .- 1432-8798. ; 164:4, s. 971-982
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Tidskriftsartikel (populärvet., debatt m.m.)abstract
- The RNA-dependent RNA polymerase (RdRp) of sesbania mosaic virus (SeMV) was previously shown to interact with the viral protein P10, which led to enhanced polymerase activity. In the present investigation, the equilibrium dissociation constant for the interaction between the two proteins was determined to be 0.09 mu M using surface plasmon resonance, and the disordered C-terminal domain of RdRp was shown to be essential for binding to P10. The association with P10 brought about a change in the oligomeric state of RdRp, resulting in reduced aggregation and increased polymerase activity. Interestingly, unlike the wild-type RdRp, C-terminal deletion mutants (C del 43 and C del 72) were found to exist predominantly as monomers and were as active as the RdRp-P10 complex. Thus, either the deletion of the C-terminal disordered domain or its masking by binding to P10 results in the activation of polymerase activity. Further, deletion of the C-terminal 85 residues of RdRp resulted in complete loss of activity. Mutation of a conserved tyrosine (RdRp Y480) within motif E, located between 72 and 85 residues from the C-terminus of RdRp, rendered the protein inactive, demonstrating the importance of motif E in RNA synthesis in vitro.
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| 10. |
- Barany, George, et al.
(författare)
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Poly(ethylene glycol)-containing supports for solid-phase synthesis of peptides and combinatorial organic libraries.
- 1997
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Ingår i: Poly(ethylene glycol): Chemistry and Biological Applications, ACS Symp. Series. - Washington, DC : American Chemical Society. - 9780841235373 ; 680, s. 239-264
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Bokkapitel (populärvet., debatt m.m.)abstract
- The choice of a polymeric support is a key factor for the success of solid-phase methods for syntheses of organic compounds and biomolecules such as peptides and oligonucleotides. Classical Merrifield solid-phase peptide synthesis, performed on low cross-linked hydrophobic polystyrene (PS) beads, sometimes suffers from sequence-dependent coupling difficulties. The concept of incorporating PEG into supports for solid-phase synthesis represents a successful approach to alleviating such problems. This chapter reviews the preparation of families of poly(ethylene glycol)-polystyrene (PEG-PS)graft as well as (highly) Cross-Linked Ethoxylate Acrylate Resin (CLEAR) supports developed in our laboratories, and demonstrates their applications to the syntheses of a wide range of targets in connection with numerous research objectives.
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