Evidence map›Paper›PMID 22733729›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Aligned hemozoin crystals in curved clusters in malarial red blood cells revealed by nanoprobe X-ray Fe fluorescence and diffraction.

Sergey Kapishnikov, Trine Berthing, Lars Hviid, Martin Dierolf, Andreas Menzel, Franz Pfeiffer, Jens Als-Nielsen, Leslie Leiserowitz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 6% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Pooled it
  2. Chemical propulsion of hemozoin crystal motion in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Quinolines block every step of malaria heme crystal growth.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Antimalarials inhibit hematin crystallization by unique drug-surface site interactions.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Mechanisms of hematin crystallization and inhibition by the antimalarial drug chloroquine.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

8 authors at 3 institutions in 4 countries.

Sergey KapishnikovDepartment of Materials and Interfaces, The Weizmann Institute of Science, Rehovot 76100, Israel.
Trine Berthing
Lars Hviid
Martin Dierolf
Andreas Menzel
Franz Pfeiffer
Jens Als-Nielsen
Leslie Leiserowitz
Paul Scherrer Institute · CHUniversity of Copenhagen · DKWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human malaria parasite Plasmodium falciparum detoxifies the heme byproduct of hemoglobin digestion in infected red blood cells by sequestration into submicron-sized hemozoin crystals. The crystal is composed of heme units interlinked to form cyclic dimers via reciprocal Fe─O (propionate) bonds. Templated hemozoin nucleation was envisaged to explain a classic observation by electron microscopy of a cluster of aligned hemozoin crystals within the parasite digestive vacuole. This dovetails with evidence that acylglycerol lipids are involved in hemozoin nucleation in vivo, and nucleation of β-hematin, the synthetic analogue of hemozoin, was consistently induced at an acylglycerol-water interface via their {100} crystal faces. In order to ascertain the nature of hemozoin nucleation in vivo, we probed the mutual orientations of hemozoin crystals in situ within RBCs using synchrotron-based X-ray nanoprobe Fe fluorescence and diffraction. The X-ray patterns indicated the presence of hemozoin clusters, each comprising several crystals aligned along their needle c axes and exposing {100} side faces to an approximately cylindrical surface, suggestive of nucleation via a common lipid layer. This experimental finding, and the associated nucleation model, are difficult to reconcile with recent reports of hemozoin formation within lipid droplets in the digestive vacuole. The diffraction results are verified by a study of the nucleation process using emerging tools of three-dimensional cellular microscopy, described in the companion paper.

Indexed as

AnimalsCrystallography, X-RayErythrocytesHemeHemeproteinsHumansLipidsMalariaMolecular ProbesNanotechnologyOptics and PhotonicsPlasmodiumSynchrotronsWaterX-Ray DiffractionHemeHemeproteinshemozoinLipidsMolecular ProbesWater

Identifiers

PMID22733729
PMCPMC3396539
OpenAlexW1976146170

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.