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(hämtat ur Lunds universitets publikationsdatabas)
- Dual actions of apolipoprotein A-I on glucose-stimulated insulin secretion and insulin-independent peripheral tissue glucose uptake lead to increased heart and skeletal muscle glucose disposal
- Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function
- ApoA-I Milano stimulates lipolysis in adipose cells independently of cAMP/PKA activation.
- Structural and Functional Analysis of the ApolipoproteinA-I A164S Variant.
- ZnT8 autoantibody epitope specificity and affinity examined with recombinant ZnT8 variant proteins in specific ZnT8R and ZnT8W autoantibody positive type 1 diabetes patients.
- Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I
- Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.
- Secondary Structure Changes in ApoA-I Milano (R173C) Are Not Accompanied by a Decrease in Protein Stability or Solubility.
- Single injections of apoA-I acutely improve in vivo glucose tolerance in insulin-resistant mice.
- Superantigen activates the gp130 receptor on adipocytes resulting in altered adipocyte metabolism.
- Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89
- Discoidal HDL and apoA-I-derived peptides improve glucose uptake in skeletal muscle.
- Double Electron-Electron Resonance Probes Ca2+-Induced Conformational Changes and Dimerization of Recoverin
- EPR assessment of protein sites for incorporation of Gd(III) MRI contrast labels.
- The secondary structure of apolipoprotein A-I on 9.6-nm reconstituted high-density lipoprotein determined by EPR spectroscopy
- Postprandial apoE Isoform and Conformational Changes Associated with VLDL Lipolysis Products Modulate Monocyte Inflammation
- The "beta-clasp" model of apolipoprotein A-I - A lipid-free solution structure determined by electron paramagnetic resonance spectroscopy.
- The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
- The intrinsic GTPase activity of the Gtr1 protein from Saccharomyces cerevisiae