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Träfflista för sökning "L773:0264 6021 srt2:(2010-2019);mspu:(researchreview)"

Sökning: L773:0264 6021 > (2010-2019) > Forskningsöversikt

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2.
  • Birkholtz, Lyn-Marie, et al. (författare)
  • Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities
  • 2011
  • Ingår i: Biochemical Journal. - London : The Biochemical Society. - 0264-6021 .- 1470-8728. ; 438, s. 229-244
  • Forskningsöversikt (refereegranskat)abstract
    • New drugs are urgently needed for the treatment of tropical and subtropical parasitic diseases, such as African sleeping sickness. Chagas' disease, leishmaniasis and malaria. Enzymes in polyamine biosynthesis and thiol metabolism, as well as polyamine transporters, are potential drug targets within these organisms. In the present review, the current knowledge of unique properties of polyamine metabolism in these parasites is outlined. These properties include prozyme regulation of AdoMetDC (S-adenosylmethionine decarboxylase) activity in trypanosomatids, co-expression of ODC (ornithine decarboxylase) and AdoMetDC activities in a single protein in plasmodia, and formation of trypanothione, a unique compound linking polyamine and thiol metabolism in trypanosomatids. Particularly interesting features within polyamine metabolism in these parasites are highlighted for their potential in selective therapeutic strategies.
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3.
  • Johansson, Jan, et al. (författare)
  • Control of amyloid assembly by autoregulation
  • 2012
  • Ingår i: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 447, s. 185-192
  • Forskningsöversikt (refereegranskat)abstract
    • The assembly of proteins into amyloid fibrils can be an element of both protein aggregation diseases and a functional unit in healthy biological pathways. In both cases, it must be kept under tight control to prevent undesired aggregation. In normophysiology, proteins can self-chaperone amyloidogenic segments by restricting their conformational flexibility in an overall stabilizing protein fold. However, some aggregation-prone segments cannot be controlled in this manner and require additional regulatory elements to limit fibrillation. The present review summarizes different molecular mechanisms that proteins use to control their own assembly into fibrils, such as the inclusion of a chaperoning domain or a blocking segment in the proform, the controlled release of an amyloidogenic region from the folded protein, or the adjustment of fibrillation propensity according to pH. Autoregulatory elements can control disease-related as well as functional fibrillar protein assemblies and distinguish a group of self-regulating amyloids across a wide range of biological functions and organisms.
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4.
  • Koch, Sina, et al. (författare)
  • Signal transduction by vascular endothelial growth factor receptors
  • 2011
  • Ingår i: Biochemical Journal. - 0264-6021 .- 1470-8728. ; 437, s. 169-183
  • Forskningsöversikt (refereegranskat)abstract
    • VEGFs (vascular endothelial growth factors) control vascular development during embryogenesis and the function of blood vessels and lymphatic vessels in the adult. There are five related mammalian ligands, which act through three receptor tyrosine kinases. Signalling is modulated through neuropilins, which act as VEGF co-receptors. Heparan sulfate and integrins are also important modulators of VEGF signalling. Therapeutic agents that interfere with VEGF signalling have been developed with the aim of decreasing angiogenesis in diseases that involve tissue growth and inflammation, such as cancer. The present review will outline the current understanding and consequent biology of VEGF receptor signalling.
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  • Resultat 1-4 av 4

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