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Showing results 83 to 87 of 87
  • OER000002355.pdf.jpg
  • Journal Article

  • Ubiquitin-derived artificial binding proteins targeting oncofetal fibronectin reveal scaffold plasticity by β-strand slippage

    • Authors :  Katzschmann, Anja (2023)

  • Affilin proteins (artificial binding proteins based on the ubiquitin scaffold) were generated using directed protein evolution to yield de‐novo variants that bind the extra‐domain B (EDB) of oncofetal fibronectin, an abundant tumor marker in fetal and neoplastic tissues. Structures of two EDB‐specific Affilin molecules reveal striking structural plasticity of the ubiquitin scaffold, characterized by β‐strand slippage, leading to diverse register shifts of ...
  • OER000002298.pdf.jpg
  • Journal Article

  • Urine-HILIC: Automated sample preparation for bottom-up urinary proteome profiling in clinical proteomics

    • Authors : Govender, Ireshyn (2023)

  • The study of the human urinary proteome is becoming increasingly popular in clinical proteomics studies. Large volumes of samples are readily available with minimal invasiveness, and, in addition, soluble proteins and peptides de- rived from various tissues and organs are also filtered in urine, which can reflect more general health problems [1]. Plasma was long considered the best biofluid choice for biomarker discovery studies. However, the main ...
  • OER000002377.pdf.jpg
  • Journal Article

  • USP16 is an ISG15 cross-reactive deubiquitinase targeting a subset of metabolic pathway-related proteins

    • Authors : Gan, Jin (2023)

  • The ubiquitin-like modifier ISG15 can modulate host and viral proteins to restrict viral and microbial infections, and act as a cytokine. Its expression and conjugation are strongly upregulated by type I interferons. Here we identify the deubiquitinating enzyme USP16 as an ISG15 cross-reactive protease. Ubiquitin-specific protease 16 (USP16) was found to react with an ISG15 activity-based probe in pull-down experiments using chronic myeloid leu...
  • OER000002496.pdf.jpg
  • Journal Article

  • Vibrio cholerae’s ToxRS Bile Sensing System

    • Authors : Gubensäk, N.  (2023)

  • Cholera represents a diarrheal disease caused by the Gram-negative bacterium Vibrio cholerae. Its environmental persistence causing recurring sudden outbreaks is enabled by V. cholerae’s rapid adaption to changing environments involving sensory proteins like ToxR and ToxS. Located at the inner membrane, ToxR and ToxS react to environmental stimuli like bile acid, thereby inducing survival strategies e.g. bile resistance and virulence regulation. Currently, transcript...
  • OER000003028.pdf.jpg
  • Journal article

  • αB-crystallin affects the morphology of Aβ(1-40) aggregates

    • Authors : Müller, Henrik (2021)

  • αB-crystallin (ABC) is a human small heat shock protein that is strongly linked to Alzheimer’s disease (AD). In vitro, it can inhibit the aggregation and amyloid formation of a range of proteins including Aβ(1-40), a primary component of AD amyloid plaques. Despite the strong links, the mechanism by which ABC inhibits amyloid formation has remained elusive, in part due to the notorious irreproducibility of aggregation assays involving&...