Evidence map›Paper›PMID 17449671›Full record

ArticleBiophysical journal2007

Two-step mechanism of homogeneous nucleation of sickle cell hemoglobin polymers.

Oleg Galkin, Weichun Pan, Luis Filobelo, Rhoda Elison Hirsch, Ronald L Nagel, Peter G Vekilov

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
  2. Classical and Nonclassical Nucleation Mechanisms of Biomolecules.Advances in biochemical engineering/biotechnology · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Protein conformation and biomolecular condensates.Current research in structural biology · 2022
    Review
  7. Article
  8. Mesoscopic protein-rich clusters host the nucleation of mutant p53 amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Do protein crystals nucleate within dense liquid clusters?Acta crystallographica. Section F, Structural biology communications · 2015
    Article
  19. Crucial role of nonspecific interactions in amyloid nucleation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  20. Nucleation precursors in protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2014
    Review
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 at 3 institutions in 1 country.

Oleg GalkinDepartment of Chemical and Biomolecular Engineering, University of Houston, Houston, Texas 77204-4004, USA.
Weichun Pan
Luis Filobelo
Rhoda Elison Hirsch
Ronald L Nagel
Peter G Vekilov
University of Houston · USAlbert Einstein College of Medicine · USThe Bronx Defenders · US

Funding

PHS HHS G091474
6 · The paper itself

Abstract

Sickle cell anemia is a debilitating genetic disease that affects hundreds of thousands of babies born each year worldwide. Its primary pathogenic event is the polymerization of a mutant, sickle cell, hemoglobin (HbS); and this is one of a line of diseases (Alzheimer's, Huntington's, prion, etc.) in which nucleation initiates pathophysiology. We show that the homogeneous nucleation of HbS polymers follows a two-step mechanism with metastable dense liquid clusters serving as precursor to the ordered nuclei of the HbS polymer. The evidence comes from data on the rates of fiber nucleation and growth and nucleation delay times, the interaction of fibers with polarized light, and mesoscopic metastable HbS clusters in solution. The presence of a precursor in the HbS nucleation mechanism potentially allows low-concentration solution components to strongly affect the nucleation kinetics. The variations of these concentrations in patients might account for the high variability of the disease in genetically identical patients. In addition, these components can potentially be utilized for control of HbS polymerization and treatment of the disease.

Indexed as

Anemia, Sickle CellErythrocytesHemoglobin, SickleHumansKineticsMacromolecular SubstancesModels, MolecularProtein ConformationHemoglobin, SickleMacromolecular Substances

Identifiers

PMID17449671
PMCPMC1913141
OpenAlexW1993176534

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.