Evidence map›Paper›PMID 11032800›Full record

ArticleThe EMBO journal2000

Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo.

A C Gill, M A Ritchie, L G Hunt, S E Steane, K G Davies, S P Bocking, A G Rhie, A D Bennett, J Hope

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Structural changes of TasA in biofilm formation ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Article
  5. Physiological Functions of the Cellular Prion Protein.Frontiers in molecular biosciences · 2017
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Prolyl 4-hydroxylase.Critical reviews in biochemistry and molecular biology · 2010
    Review
  11. Review
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

A C GillInstitute for Animal Health, Compton, Newbury, Berkshire, RG20 7NN, UK.
M A Ritchie
L G Hunt
S E Steane
K G Davies
S P Bocking
A G Rhie
A D Bennett
J Hope
Organic Research Centre · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmissible spongiform encephalopathies are characterized by conversion of a host protein, PrP(C) (cellular prion protein), to a protease-resistant isoform, PrP(Sc) (prion protein scrapie isoform). The importance of the highly flexible, N-terminal region of PrP has recently become more widely appreciated, particularly the biological activities associated with its metal ion-binding domain and its potential to form a poly(L-proline) II (PPII) helix. Circular dichroism spectroscopy of an N-terminal peptide, PrP(37-53), showed that the PPII helix is formed in aqueous buffer; as it also contains an Xaa-Pro-Gly consensus sequence, it may act as a substrate for the collagen-modifying enzyme prolyl 4-hydroxylase. Direct evidence for this modification was obtained by mass spectrometry and Edman sequencing in recombinant mouse PrP secreted from stably transfected Chinese hamster ovary cells. Almost complete conversion of proline to 4-hydroxyproline occurs specifically at residue Pro44 of this murine protein; the same hydroxylated residue was detected, at lower levels, in PrP(Sc) from the brains of scrapie-infected mice. Cation binding and/or post-translational hydroxylation of this region of PrP may regulate its role in the physiology and pathobiology of the cell.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCHO CellsCircular DichroismCricetinaeGuanidineHydroxylationMiceMolecular Sequence DataOsmolar ConcentrationOxidation-ReductionPeptide FragmentsPeptidesPrionsProlineGuanidinePeptide FragmentsPeptidespolyprolinePrionsProlinePrPSc ProteinsRecombinant Proteins

Identifiers

PMID11032800
PMCPMC314005
OpenAlexW2063984339

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.