Evidence map›Paper›PMID 37874916›Full record

ReviewBlood2024

Biology of factor XI.

Samantha A Moellmer, Cristina Puy, Owen J T McCarty

Open access · greenAbstract readReview
In one paragraph

Review in Blood, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
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  7. Article
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  11. Review
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  13. Article
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  15. Article
  16. Rare inherited coagulation disorders: no longer orphan and neglected.Research and practice in thrombosis and haemostasis · 2024
    Review
  17. Review
  18. Case Report: Allelic and biallelic variants inFrontiers in cardiovascular medicine · 2024
    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

3 authors at 1 institution in 1 country.

Samantha A MoellmerDepartment of Biomedical Engineering, Oregon Health & Science University, Portland, OR.ORCID 0000-0002-4501-6917
Cristina PuyDepartment of Biomedical Engineering, Oregon Health & Science University, Portland, OR.ORCID 0000-0002-5911-8156
Owen J T McCartyDepartment of Biomedical Engineering, Oregon Health & Science University, Portland, OR.ORCID 0000-0001-9481-0124
Oregon Health & Science University · US

Funding

Characterization of Coagulation Factor-platelet Interactions: Role of FXIR01HL101972 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI Owen J McCarty · 2010 to 2026
$8.5M
Contact Pathway Activation on Vascular DevicesR01HL144113 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI HINDS, MONICA T, MCCARTY, OWEN J · 2018 to 2025
$6.0M
Contact Activation and InfectionR01AI157037 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI LUPU, FLOREA, MCCARTY, OWEN J · 2020 to 2024
$3.3M
NHLBI NIH HHS R01 HL101972NHLBI NIH HHS R01 HL144113NIAID NIH HHS R01 AI157037
6 · The paper itself

Abstract

abstractUnique among coagulation factors, the coagulation factor XI (FXI) arose through a duplication of the gene KLKB1, which encodes plasma prekallikrein. This evolutionary origin sets FXI apart structurally because it is a homodimer with 2 identical subunits composed of 4 apple and 1 catalytic domain. Each domain exhibits unique affinities for binding partners within the coagulation cascade, regulating the conversion of FXI to a serine protease as well as the selectivity of substrates cleaved by the active form of FXI. Beyond serving as the molecular nexus for the extrinsic and contact pathways to propagate thrombin generation by way of activating FIX, the function of FXI extends to contribute to barrier function, platelet activation, inflammation, and the immune response. Herein, we critically review the current understanding of the molecular biology of FXI, touching on some functional consequences at the cell, tissue, and organ level. We conclude each section by highlighting the DNA mutations within each domain that present as FXI deficiency. Together, a narrative review of the structure-function of the domains of FXI is imperative to understand the etiology of hemophilia C as well as to identify regions of FXI to safely inhibit the pathological function of activation or activity of FXI without compromising the physiologic role of FXI.

Indexed as

Factor XIFactor XI DeficiencyBiologyBlood CoagulationCatalytic DomainHumansThrombinFactor XIThrombin

Identifiers

PMID37874916
PMCPMC11033592
OpenAlexW4387900899

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.