placeholder
and
and

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Language: German
    In: 2015
    Subject(s): Specialist Journals + Scientific Journals (Press) ; Switzerland (Central Europe). Swiss Confederation ; Schweiz (Mitteleuropa). Schweizerische Eidgenossenschaft ; OPEN Access (Scientific Publishing) ; Fachzeitschriften + Wissenschaftliche Zeitschriften (Zeitungswesen) ; OPEN Access (Wissenschaftliches Publizieren) ; Bibliothekswesen + Bibliothekswissenschaften + Bibliotheken ; Librarianship + Library Sciences + Libraries ; Library & Information Sciences
    Source: Research Collection (ETH Zurich)
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Language: English
    In: PLoS Biology, 2005, Vol.3(6), p.e189
    Description: Eukaryotic cells contain several unconventional poly(A) polymerases in addition to the canonical enzymes responsible for the synthesis of poly(A) tails of nuclear messenger RNA precursors. The yeast protein Trf4p has been implicated in a quality control pathway that leads to the polyadenylation and subsequent exosome-mediated degradation of hypomethylated initiator tRNA Met (tRNA i Met ). Here we show that Trf4p is the catalytic subunit of a new poly(A) polymerase complex that contains Air1p or Air2p as potential RNA-binding subunits, as well as the putative RNA helicase Mtr4p. Comparison of native tRNA i Met with its in vitro transcribed unmodified counterpart revealed that the unmodified RNA was preferentially polyadenylated by affinity-purified Trf4 complex from yeast, as well as by complexes reconstituted from recombinant components. These results and additional experiments with other tRNA substrates suggested that the Trf4 complex can discriminate between native tRNAs and molecules that are incorrectly folded. Moreover, the polyadenylation activity of the Trf4 complex stimulated the degradation of unmodified tRNA i Met by nuclear exosome fractions in vitro. Degradation was most efficient when coupled to the polyadenylation activity of the Trf4 complex, indicating that the poly(A) tails serve as signals for the recruitment of the exosome. This polyadenylation-mediated RNA surveillance resembles the role of polyadenylation in bacterial RNA turnover. ; A new molecular surveillance mechanism is uncovered in eukaryotes, in which incorrectly folded tRNAs are polyadenylated and then targeted for degradation.
    Subject(s): Research Article ; Molecular Biology ; Biochemistry ; Saccharomyces
    ISSN: 1544-9173
    E-ISSN: 1545-7885
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Language: English
    In: Journal of neurochemistry, September 2005, Vol.94(5), pp.1351-60
    Description: The pathological role of ApoE4 in Alzheimer's disease (AD) is not fully elucidated yet but there is strong evidence that ApoE is involved in Abeta deposition, which is an early hallmark of AD neuropathology. Overexpression of ApoE in neuroblastoma cells (Neuro2a) leads to the generation of an intracellular 13 kDa carboxy-terminal fragment of ApoE comparable to fragments seen in brains of AD patients. ApoE4 generates more of this fragment than ApoE2 and E3 suggesting a potential pathological role of these fragments in Alzheimer's disease. Analysis of this intracellular ApoE4 fragment by protease digest followed by MALDI-TOF mass spectrometry showed the proteolytic cleavage site close to residue 187 of ApoE. We have engineered and expressed the corresponding ApoE fragments in vitro. The recombinant 13 kDa carboxy-terminal fragment inhibited fibril formation of Abeta; this contrasts with the full-length ApoE and the corresponding amino-terminal ApoE fragment. Moreover, we show that the 13...
    Subject(s): Amyloid Beta-Peptides -- Chemistry ; Apolipoproteins E -- Chemistry
    ISSN: 0022-3042
    Source: MEDLINE/PubMed (U.S. National Library of Medicine)
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    In: Journal of Neurochemistry, September 2005, Vol.94(5), pp.1351-1360
    Description: The pathological role of ApoE4 in Alzheimer's disease (AD) is not fully elucidated yet but there is strong evidence that ApoE is involved in Abeta deposition, which is an early hallmark of AD neuropathology. Overexpression of ApoE in neuroblastoma cells (Neuro2a) leads to the generation of an intracellular 13 kDa carboxy‐terminal fragment of ApoE comparable to fragments seen in brains of AD patients. ApoE4 generates more of this fragment than ApoE2 and E3 suggesting a potential pathological role of these fragments in Alzheimer's disease. Analysis of this intracellular ApoE4 fragment by protease digest followed by MALDI‐TOF mass spectrometry showed the proteolytic cleavage site close to residue 187 of ApoE. We have engineered and expressed the corresponding ApoE fragments . The recombinant 13 kDa carboxy‐terminal fragment inhibited fibril formation of Abeta; this contrasts with the full‐length ApoE and the corresponding amino‐terminal ApoE fragment. Moreover, we show that the 13 kDa carboxy‐terminal fragment of ApoE stabilizes the formation of Abeta hexamers. Complexes of Abeta with the 13 kDa carboxy‐terminal ApoE fragment show toxicity in PC12 cells comparable to Abeta fibrils. These data suggest that cleavage of ApoE, leading to the generation of this fragment, contributes to the pathogenic effect of ApoE4 in AD.
    Subject(s): Abeta ; Alzheimer'S Disease ; Amyloid ; Apoe ; Apoe Fragments
    ISSN: 0022-3042
    E-ISSN: 1471-4159
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...