Evidence map›Paper›PMID 24442723›Full record

ReviewProtein science : a publication of the Protein Society2014

Sequence variation and structural conservation allows development of novel function and immune evasion in parasite surface protein families.

Matthew K Higgins, Mark Carrington

Open access · hybridAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Evasive mechanisms of human VSG and PfEMP1 antigens with link to Vaccine scenario: a review.Journal of parasitic diseases : official organ of the Indian Society for Parasitology · 2025
    Review
  6. Antibody levels to variant and conservedFrontiers in immunology · 2025
    Article
  7. A Study of Cross-Protection betweenPathogens (Basel, Switzerland) · 2024
    Article
  8. Intracellular Pathogens: Infection, Immunity, and Intervention.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Structure of theProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Structural insights into diverse modes of ICAM-1 binding byProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Matthew K HigginsDepartment of Biochemistry, University of Oxford, OX1 3QU, Oxford.
Mark Carrington
University of Oxford · GB

Funding

Medical Research Council G0901062Wellcome Trust 101020
6 · The paper itself

Abstract

Trypanosoma and Plasmodium species are unicellular, eukaryotic pathogens that have evolved the capacity to survive and proliferate within a human host, causing sleeping sickness and malaria, respectively. They have very different survival strategies. African trypanosomes divide in blood and extracellular spaces, whereas Plasmodium species invade and proliferate within host cells. Interaction with host macromolecules is central to establishment and maintenance of an infection by both parasites. Proteins that mediate these interactions are under selection pressure to bind host ligands without compromising immune avoidance strategies. In both parasites, the expansion of genes encoding a small number of protein folds has established large protein families. This has permitted both diversification to form novel ligand binding sites and variation in sequence that contributes to avoidance of immune recognition. In this review we consider two such parasite surface protein families, one from each species. In each case, known structures demonstrate how extensive sequence variation around a conserved molecular architecture provides an adaptable protein scaffold that the parasites can mobilise to mediate interactions with their hosts.

Indexed as

Amino Acid SequenceGenetic VariationModels, MolecularMolecular Sequence DataPlasmodiumProtein ConformationProtozoan ProteinsSequence AlignmentTrypanosomaProtozoan Proteinsantigenic variationmalariaPfEMP1surface proteinstrypanosomesVSG

Identifiers

PMID24442723
PMCPMC3970887
OpenAlexW2111236962

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.