Browsing Artikler, rapporter og annet (kjemi) by Author "Rothweiler, Ulli"

Now showing items 1-6 of 6

    • 2.09 Å resolution structure of E. coli HigBA toxin-antitoxin complex reveals an ordered DNA-binding domain and intrinsic dynamics in antitoxin 

      Jadhav, Pankaj; Sinha, Vikrant; Chugh, Saurabh; Kotyada, Chaithanya; Bachhav, Digvijay; Singh, Ramandeep; Rothweiler, Ulli; Singh, Mahavir (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-10-29)
      The toxin–antitoxin (TA) systems are small operon systems that are involved in important physiological processes in bacteria such as stress response and persister cell formation. Escherichia coli HigBA complex belongs to the type II TA systems and consists of a protein toxin called HigB and a protein antitoxin called HigA. The toxin HigB is a ribosome-dependent endoribonuclease that cleaves the ...

    • The crystal structure of haemoglobin from Atlantic cod 

      Helland, Ronny; Bjørkeng, Eva katrin; Rothweiler, Ulli; Sydnes, Magne Olav; Pampanin, Daniela Maria (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-07-16)
      The crystal structure of haemoglobin from Atlantic cod has been solved to 2.54 A˚ resolution. The structure consists of two tetramers in the crystallographic asymmetric unit. The structure of haemoglobin obtained from one individual cod suggests polymorphism in the tetrameric assembly.

    • Enzyme-adenylate structure of a bacterial ATP-dependent DNA ligase with a minimized DNA-binding surface 

      Williamson, Adele Kim; Rothweiler, Ulli; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2014-11-01)
      DNA ligases are a structurally diverse class of enzymes which share a common catalytic core and seal breaks in the phosphodiester backbone of double-stranded DNA via an adenylated intermediate. Here, the structure and activity of a recombinantly produced ATP-dependent DNA ligase from the bacterium Psychromonas sp. strain SP041 is described. This minimal-type ligase, like its close homologues, ...

    • Novel DYRK1A Inhibitor Rescues Learning and Memory Deficits in a Mouse Model of Down Syndrome 

      Stensen, Wenche; Rothweiler, Ulli; Engh, Richard Alan; Stasko, Melissa R.; Bederman, Ilya; Costa, Alberto C. S.; Fugelli, Anders; Svendsen, John Sigurd Mjøen (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-11-17)
      Down syndrome (DS) is a complex genetic disorder associated with substantial physical, cognitive, and behavioral challenges. Due to better treatment options for the physical co-morbidities of DS, the life expectancy of individuals with DS is beginning to approach that of the general population. However, the cognitive deficits seen in individuals with DS still cannot be addressed pharmacologically. ...

    • Structure and function of a CE4 deacetylase isolated from a marine environment 

      Tuveng, Tina Rise; Rothweiler, Ulli; Udatha, D.B.R.K. Gupta; Vaaje-Kolstad, Gustav; Smalås, Arne O.; Eijsink, Vincent (Journal article; Tidsskriftartikkel; Peer reviewed, 2017-11-06)
      Chitin, a polymer of β(1–4)-linked N-acetylglucosamine found in e.g. arthropods, is a valuable resource that may be used to produce chitosan and chitooligosaccharides, two compounds with considerable industrial and biomedical potential. Deacetylating enzymes may be used to tailor the properties of chitin and its derived products. Here, we describe a novel CE4 enzyme originating from a marine ...

    • The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A-PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine 

      Alexeeva, Marina; Åberg, espen; Engh, Richard Alan; Rothweiler, Ulli (Journal article; Tidsskriftartikkel; Peer reviewed, 2015)
      Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) is a protein kinase associated with neuronal development and brain physiology. The DYRK kinases are very unusual with respect to the sequence of the catalytic loop, in which the otherwise highly conserved arginine of the HRD motif is replaced by a cysteine. This replacement, along with the proximity of a potential disulfide-bridge ...