Evidence map›Paper›PMID 15542552›Full record

ArticleBiophysical journal2005

Understanding the shape of sickled red cells.

Garrott W Christoph, James Hofrichter, William A Eaton

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

49 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. High-throughput quantification of red blood cell deformability and oxygen saturation to probe mechanisms of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Article
  8. Phenotypic screening of the ReFRAME drug repurposing library to discover new drugs for treating sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. Article
  11. Pathologically stiff erythrocytes impede contraction of blood clots.Journal of thrombosis and haemostasis : JTH · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Allosteric control of hemoglobin S fiber formation by oxygen and its relation to the pathophysiology of sickle cell disease.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Review
  17. Review
  18. Article
  19. Review
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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

3 authors at 1 institution in 1 country.

Garrott W ChristophLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.
James Hofrichter
William A Eaton
National Institutes of Health · US

Funding

Ultrafast Protein Folding ZIADK029010 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM · 2009 to 2011
$1.4M
Ultrafast Protein FoldingZ01DK029010 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI EATON, WILLIAM A · 1986 to 2008
$891k
6 · The paper itself

Abstract

To understand the physical basis of the wide variety of shapes of deoxygenated red cells from patients with sickle cell anemia, we have measured the formation rate and volume distribution of the birefringent domains of hemoglobin S fibers. We find that the domain formation rate depends on the approximately 80th power of the protein concentration, compared to approximately 40th power for the concentration dependence of the reciprocal of the delay time that precedes fiber formation. These remarkably high concentration dependences, as well as the exponential distribution of domain volumes, can be explained by the previously proposed double nucleation model in which homogeneous nucleation of a single fiber triggers the formation of an entire domain via heterogeneous nucleation and growth. The enormous sensitivity of the domain formation rate to intracellular hemoglobin S concentration explains the variable cell morphology and why rapid polymerization results in cells that do not appear sickled at all.

Indexed as

Models, ChemicalModels, MolecularAnemia, Sickle CellCells, CulturedCell SizeDimerizationErythrocytesGelsHemoglobin, SickleHumansKineticsMultiprotein ComplexesProtein ConformationProtein Structure, TertiaryGelsHemoglobin, SickleMultiprotein Complexes

Identifiers

PMID15542552
PMCPMC1305139
OpenAlexW2089541065

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.