Evidence map›Paper›PMID 20394753›Full record

ReviewJournal of molecular biology2010

Domain metastability: a molecular basis for immunoglobulin deposition?

Andreas F-P Sonnen, Chao Yu, Edward J Evans, David I Stuart, Simon J Davis, Robert J C Gilbert

Abstract readReview
In one paragraph

Review in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Considering B7-CD28 as a family through sequence and structure.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

6 authors.

Andreas F-P SonnenDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK. andreas@strubi.ox.ac.uk
Chao Yu
Edward J Evans
David I Stuart
Simon J Davis
Robert J C Gilbert

Funding

Wellcome Trust 081894
6 · The paper itself

Abstract

We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis-trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits.

Indexed as

AmyloidAntigens, CDCrystallography, X-RayCTLA-4 AntigenDimerizationHumansImmunoglobulin Light ChainsMacromolecular SubstancesMicroscopy, ElectronModels, MolecularProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryAmyloidAntigens, CDCTLA-4 AntigenCTLA4 protein, humanImmunoglobulin Light ChainsMacromolecular Substances

Identifiers

PMID20394753
PMCPMC2954335

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.