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Search: WFRF:(Stewart P) > RISE

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1.
  • Regmi, P., et al. (author)
  • The future of WRRF modelling - Outlook and challenges
  • 2019
  • In: Water Science and Technology. - : IWA Publishing. - 0273-1223 .- 1996-9732. ; 79:1, s. 3-14
  • Journal article (peer-reviewed)abstract
    • The wastewater industry is currently facing dramatic changes, shifting away from energy-intensive wastewater treatment towards low-energy, sustainable technologies capable of achieving energy positive operation and resource recovery. The latter will shift the focus of the wastewater industry to how one could manage and extract resources from the wastewater, as opposed to the conventional paradigm of treatment. Debatable questions arise: Can the more complex models be calibrated, or will additional unknowns be introduced? After almost 30 years using well-known International Water Association (IWA) models, should the community move to other components, processes, or model structures like 'black box' models, computational fluid dynamics techniques, etc.? Can new data sources - e.g. on-line sensor data, chemical and molecular analyses, new analytical techniques, off-gas analysis - keep up with the increasing process complexity? Are different methods for data management, data reconciliation, and fault detection mature enough for coping with such a large amount of information? Are the available calibration techniques able to cope with such complex models? This paper describes the thoughts and opinions collected during the closing session of the 6th IWA/WEF Water Resource Recovery Modelling Seminar 2018. It presents a concerted and collective effort by individuals from many different sectors of the wastewater industry to offer past and present insights, as well as an outlook into the future of wastewater modelling.
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2.
  • Michel, M., et al. (author)
  • Small-molecule activation of OGG1 increases oxidative DNA damage repair by gaining a new function
  • 2022
  • In: Science. - Stockholm : American Association for the Advancement of Science. - 0036-8075 .- 1095-9203. ; 376:6600, s. 1471-1476
  • Journal article (peer-reviewed)abstract
    • Oxidative DNA damage is recognized by 8-oxoguanine (8-oxoG) DNA glycosylase 1 (OGG1), which excises 8-oxoG, leaving a substrate for apurinic endonuclease 1 (APE1) and initiating repair. Here, we describe a small molecule (TH10785) that interacts with the phenylalanine-319 and glycine-42 amino acids of OGG1, increases the enzyme activity 10-fold, and generates a previously undescribed b,d-lyase enzymatic function. TH10785 controls the catalytic activity mediated by a nitrogen base within its molecular structure. In cells, TH10785 increases OGG1 recruitment to and repair of oxidative DNA damage. This alters the repair process, which no longer requires APE1 but instead is dependent on polynucleotide kinase phosphatase (PNKP1) activity. The increased repair of oxidative DNA lesions with a small molecule may have therapeutic applications in various diseases and aging. © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works
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