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Träfflista för sökning "WFRF:(Gulati S.) srt2:(2020-2024)"

Sökning: WFRF:(Gulati S.) > (2020-2024)

  • Resultat 1-10 av 14
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  • Kanai, M, et al. (författare)
  • 2023
  • swepub:Mat__t
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  • Niemi, MEK, et al. (författare)
  • 2021
  • swepub:Mat__t
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  • 2021
  • swepub:Mat__t
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  • Carlsten, C., et al. (författare)
  • COVID-19 as an occupational disease
  • 2021
  • Ingår i: American Journal of Industrial Medicine. - : Wiley. - 0271-3586 .- 1097-0274. ; 64:4, s. 227-237
  • Tidskriftsartikel (refereegranskat)abstract
    • The impact of coronavirus disease 2019 (COVID-19) caused by the severe acute respiratory syndrome coronavirus 2 permeates all aspects of society worldwide. Initial medical reports and media coverage have increased awareness of the risk imposed on healthcare workers in particular, during this pandemic. However, the health implications of COVID-19 for the global workforce are multifaceted and complex, warranting careful reflection and consideration to mitigate the adverse effects on workers worldwide. Accordingly, our review offers a framework for considering this topic, highlighting key issues, with the aim to prompt and inform action, including research, to minimize the occupational hazards imposed by this ongoing challenge. We address respiratory disease as a primary concern, while recognizing the multisystem spectrum of COVID-19-related disease and how clinical aspects are interwoven with broader socioeconomic forces.
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10.
  • Currie, Michael J., et al. (författare)
  • Structural and biophysical analysis of a Haemophilus influenzae tripartite ATP-independent periplasmic (TRAP) transporter
  • 2024
  • Ingår i: ELIFE. - 2050-084X. ; 12
  • Tidskriftsartikel (refereegranskat)abstract
    • Tripartite ATP-independent periplasmic (TRAP) transporters are secondary-active transporters that receive their substrates via a soluble-binding protein to move bioorganic acids across bacterial or archaeal cell membranes. Recent cryo-electron microscopy (cryo-EM) structures of TRAP transporters provide a broad framework to understand how they work, but the mechanistic details of transport are not yet defined. Here we report the cryo-EM structure of the Haemophilus influenzae N-acetylneuraminate TRAP transporter (HiSiaQM) at 2.99 & Aring; resolution (extending to 2.2 & Aring; at the core), revealing new features. The improved resolution (the previous HiSiaQM structure is 4.7 & Aring; resolution) permits accurate assignment of two Na+ sites and the architecture of the substrate-binding site, consistent with mutagenic and functional data. Moreover, rather than a monomer, the HiSiaQM structure is a homodimer. We observe lipids at the dimer interface, as well as a lipid trapped within the fusion that links the SiaQ and SiaM subunits. We show that the affinity (K-D) for the complex between the soluble HiSiaP protein and HiSiaQM is in the micromolar range and that a related SiaP can bind HiSiaQM. This work provides key data that enhances our understanding of the 'elevator-with-an-operator' mechanism of TRAP transporters.
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