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Showing results 1 to 5 of 5
  • OER000002396.pdf.jpg
  • Journal Article

  • Borrelia PeptideAtlas: A proteome resource of common Borrelia burgdorferi isolates for Lyme research

    • Authors : Reddy, Panga Jaipal. (2023)

  • Lyme disease , caused by an infection with the spirochete Borrelia burgdorferi, is the most common 36 vector-borne disease in North America. B. burgdorferi strains harbor extensive genomic and 37 proteomic variability and further comparison is key to understanding the spirochetes infectivity and 38 biological impacts of identified sequence variants. To achieve this goal, both transcript and mass 39 spectrometry (MS)-based proteomics was applied to assemble pe...
  • OER000002280.pdf.jpg
  • Journal Article

  • Dynamic inter-domain transformations mediate the allosteric regulation of human 5, 10-methylenetetrahydrofolate reductase

    • Authors : Linnea Klara Maryann Blomgren (2023)

  • One-carbon metabolism drives an extensive network of signalling and biosynthetic pathways 17 essential for cell growth and redox regulation. In all domains of life, 5,10-18 methylenetetrahydrofolate reductase (MTHFR) signals the commitment of folate-derived one-19 carbon units into biosynthesis of the global donor of trans-methylation, S-adenosyl-L-methionine 20 (SAM). Eukaryotic MTHFR appends to its conserved TIM-barrel catalytic domain (CD) a unique 21 regulatory domain (RD)&#...
  • OER000002472.pdf.jpg
  • Journal Article

  • Factors influencing the detergent-free membrane protein isolation using synthetic nanodisc-forming polymers

    • Authors : Krishnarjuna, Bankala (2023)

  • The detergent-free isolation of membrane proteins using synthetic polymers is becoming the desired approach for functional and structural studies of membrane proteins. Since the expression levels for many membrane proteins are low and a high yield of functionalized reconstituted membrane proteins is essential for in vitro studies, it is crucial to optimize the experimental conditions for a given polymer to effectively solubilize target membranes/...