Evidence map›Paper›PMID 29754827›Full record

ArticleStructure (London, England : 1993)2018

Atomic Structural Models of Fibrin Oligomers.

Artem Zhmurov, Anna D Protopopova, Rustem I Litvinov, Pavel Zhukov, John W Weisel, Valeri Barsegov

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.9field-weighted citation impact, top 9% 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, 46 citations in OpenAlex.

  1. Article
  2. Fibrin as a Versatile Fibrous Biopolymer.Sub-cellular biochemistry · 2026
    Review
  3. Review
  4. Article
  5. Review
  6. Rupture mechanics of blood clot fibrin fibers: A coarse-grained model study.Journal of the mechanics and physics of solids · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Computational Prediction of the Interaction of Ivermectin with Fibrinogen.International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Biomechanical origins of inherent tension in fibrin networks.Journal of the mechanical behavior of biomedical materials · 2022
    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

6 authors at 4 institutions in 2 countries.

Artem ZhmurovMoscow Institute of Physics & Technology, Dolgoprudny, Moscow Region 141700, Russian Federation; Sechenov University, Moscow 119991, Russian Federation.
Anna D ProtopopovaDepartment of Cell & Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Rustem I LitvinovDepartment of Cell & Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA; Institute of Fundamental Medicine and Biology, Kazan Federal University, Kazan 420008, Russian Federation.
Pavel ZhukovMoscow Institute of Physics & Technology, Dolgoprudny, Moscow Region 141700, Russian Federation.
John W WeiselDepartment of Cell & Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA. Electronic address: weisel@pennmedicine.upenn.edu.
Valeri BarsegovMoscow Institute of Physics & Technology, Dolgoprudny, Moscow Region 141700, Russian Federation; Department of Chemistry, University of Massachusetts, Lowell, MA 01854, USA. Electronic address: valeri_barsegov@uml.edu.
Moscow Institute of Physics and Technology · RUUniversity of Pennsylvania · USKazan Federal University · RUSechenov University · RU

Funding

Multiscale modeling and empirical study of a mechanism limiting blood clot growthU01HL116330 · NHLBI · UNIVERSITY OF NOTRE DAME · PI ALBER, MARK · 2014 to 2018
$3.5M
Experiment-based multi-scale modeling of the tensile and compressive deformations of fibrinR01HL135254 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI PUROHIT, PRASHANT KISHORE · 2017 to 2020
$1.6M
NHLBI NIH HHS R01 HL135254NHLBI NIH HHS U01 HL116330
6 · The paper itself

Abstract

The space-filling fibrin network is a major part of clots and thrombi formed in blood. Fibrin polymerization starts when fibrinogen, a plasma protein, is proteolytically converted to fibrin, which self-assembles to form double-stranded protofibrils. When reaching a critical length, these intermediate species aggregate laterally to transform into fibers arranged into branched fibrin network. We combined multiscale modeling in silico with atomic force microscopy (AFM) imaging to reconstruct complete atomic models of double-stranded fibrin protofibrils with γ-γ crosslinking, A:a and B:b knob-hole bonds, and αC regions-all important structural determinants not resolved crystallographically. Structures of fibrin oligomers and protofibrils containing up to 19 monomers were successfully validated by quantitative comparison with high-resolution AFM images. We characterized the protofibril twisting, bending, kinking, and reversibility of A:a knob-hole bonds, and calculated hydrodynamic parameters of fibrin oligomers. Atomic structures of protofibrils provide a basis to understand mechanisms of early stages of fibrin polymerization.

Indexed as

Crystallography, X-RayFibrinMicroscopy, Atomic ForceModels, MolecularProtein ConformationProtein MultimerizationFibrinfibrinfibrinogenfibrin oligomersfibrin polymerizationfibrin protofibrilsGPU computingMD simulationsmultiscale modeling

Identifiers

PMID29754827
PMCPMC6501597
OpenAlexW2800160491

What OpenQuestion holds

Textmetadata
LicenceTDM
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.