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Sökning: WFRF:(Olsen JV)

  • Resultat 1-21 av 21
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  • Haselmann, KF, et al. (författare)
  • Electronic excitation gives informative fragmentation of polypeptide cations and anions
  • 2002
  • Ingår i: EUROPEAN JOURNAL OF MASS SPECTROMETRY. - : SAGE Publications. - 1469-0667 .- 1751-6838. ; 8:2, s. 117-121
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • A Fourier transform mass spectrometer is a versatile instrument with a range of available fragmentation techniques. Comparison of polypeptide fragmentation patterns revealed that the techniques involving electronic excitation, such as hot-electron-capture dissociation (HECD) and electron-detachment dissociation (EDD), are even more informative than vibrational excitation (VE) techniques such as collisional activation. For dications of the peptide KIMHASELMANN, 11 eV HECD cleaved all inter-residue links in at least two places, with up to five fragments characterizing each link. For dianions of the same molecule, VE produced only one backbone cleavage whereas EDD gave ten, including five internal cleavage fragments. This is consistent with the general postulate that homogeneous electronic excitation yields more types of cleavage than near-equilibrium processes such as VE.
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  • Paul, I, et al. (författare)
  • The ubiquitin ligase Cullin5SOCS2 regulates NDR1/STK38 stability and NF-κB transactivation
  • 2017
  • Ingår i: Scientific reports. - : Springer Science and Business Media LLC. - 2045-2322. ; 7, s. 42800-
  • Tidskriftsartikel (refereegranskat)abstract
    • SOCS2 is a pleiotropic E3 ligase. Its deficiency is associated with gigantism and organismal lethality upon inflammatory challenge. However, mechanistic understanding of SOCS2 function is dismal due to our unawareness of its protein substrates. We performed a mass spectrometry based proteomic profiling upon SOCS2 depletion and yield quantitative data for ~4200 proteins. Through this screen we identify a novel target of SOCS2, the serine-threonine kinase NDR1. Over-expression of SOCS2 accelerates turnover, while its knockdown stabilizes, endogenous NDR1 protein. SOCS2 interacts with NDR1 and promotes its degradation through K48-linked ubiquitination. Functionally, over-expression of SOCS2 antagonizes NDR1-induced TNFα-stimulated NF-κB activity. Conversely, depletion of NDR1 rescues the effect of SOCS2-deficiency on TNFα-induced NF-κB transactivation. Using a SOCS2−/− mice model of colitis we show that SOCS2-deficiency is pro-inflammatory and negatively correlates with NDR1 and nuclear p65 levels. Lastly, we provide evidence to suggest that NDR1 acts as an oncogene in prostate cancer. To the best of our knowledge, this is the first report of an identified E3 ligase for NDR1. These results might explain how SOCS2-deficiency leads to hyper-activation of NF-κB and downstream pathological implications and posits that SOCS2 induced degradation of NDR1 may act as a switch in restricting TNFα-NF-κB pathway.
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  • 2017
  • swepub:Mat__t
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  • Resultat 1-21 av 21

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