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Träfflista för sökning "L773:0167 7640 OR L773:0968 0004 "

Search: L773:0167 7640 OR L773:0968 0004

  • Result 1-10 of 54
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1.
  • Al-Karadaghi, Salam, et al. (author)
  • Chelatases: distort to select?
  • 2006
  • In: Trends in Biochemical Sciences. - : Elsevier BV. - 0167-7640 .- 0968-0004. ; 31:3, s. 135-142
  • Journal article (other academic/artistic)abstract
    • Chelatases catalyze the insertion of a specific metal ion into porphyrins, a key step in the synthesis of metalated tetrapyrroles that are essential for many cellular processes. Despite apparent common structural features among chelatases, no general reaction mechanism accounting for metal ion specificity has been established. We propose that chelatase-induced distortion of the porphyrin substrate not only enhances the reaction rate by decreasing the activation energy of the reaction but also modulates which divalent metal ion is incorporated into the porphyrin ring. We evaluate the recently recognized interaction between ferrochelatase and frataxin as a way to regulate iron delivery to ferrochelatase, and thus iron and heme metabolism. We postulate that the ferrochelatase-frataxin interaction controls the type of metal ion that is delivered to ferrochelatase.
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2.
  • Massoumi, Ramin (author)
  • Ubiquitin chain cleavage: CYLD at work.
  • 2010
  • In: Trends in Biochemical Sciences. - : Elsevier BV. - 0167-7640 .- 0968-0004. ; 35, s. 392-399
  • Journal article (peer-reviewed)abstract
    • The tumor suppressor CYLD is a deubiquitylating enzyme that negatively regulates different signaling pathways by removing lysine 63-linked polyubiquitin chains from several specific substrates. In various tumor types, CYLD loss can lead to cell survival or cell proliferation. In addition to its loss due to mutations, CYLD expression can also be decreased through transcriptional and post-transcriptional regulatory mechanisms. Moreover, as epigenetic repression of CYLD can affect tumor progression in different cancer types, the activation of the CYLD promoter ensures the tight control of an inflammatory response. Recent work also shows that CYLD activity can be governed by different regulatory mechanisms including phosphorylation, thus providing another layer of control for diverse physiological processes.
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3.
  • Sandrini, Michael, et al. (author)
  • Deoxyribonucleoside kinases: two enzyme families catalyze the same reaction
  • 2005
  • In: Trends in Biochemical Sciences. - : Elsevier BV. - 0167-7640 .- 0968-0004. ; 30:5, s. 225-228
  • Journal article (peer-reviewed)abstract
    • Mammals have four deoxyribonucleoside kinases, the cytoplasmic (TK1) and mitochondrial (TK2) thymidine kinases, and the deoxycytidine (dCK) and deoxyguanosine (dGK) kinases, which salvage the precursors for nucleic acids synthesis. In addition to the native deoxyribonucleoside substrates, the kinases can phosphorylate and thereby activate a variety of anti-cancer and antiviral prodrugs. Recently, the crystal structure of human TK1 has been solved and has revealed that enzymes with fundamentally different origins and folds catalyze similar, crucial cellular reactions.
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4.
  • Akerström, B, et al. (author)
  • An intriguing member of the lipocalin protein family : alpha 1-microglobulin
  • 1990
  • In: Trends in Biochemical Sciences. - 0968-0004. ; 15:6, s. 3-240
  • Research review (peer-reviewed)abstract
    • The plasma protein alpha 1-microglobulin is a member of the lipocalin protein superfamily. In the last few years, the work on alpha 1-microglobulin has given unexpected and promising new results. Of particular interest are its molecular association with immunoglobulin A and with proteinase inhibitors, and its interactions with the immune system.
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  • Result 1-10 of 54
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