Evidence map›Paper›PMID 30165816›Full record

ReviewMolecular medicine (Cambridge, Mass.)2018

Serum amyloid A - a review.

George H Sack

Open access · goldAbstract readReview
In one paragraph

Review in Molecular medicine (Cambridge, Mass.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 284 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
284citing papers in PubMed, 1 pooled it
15.3field-weighted citation impact, top 1% 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

284 citing papers in PubMed, 1 synthesis or guideline pooled it, 484 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Article
  4. Article
  5. Article
  6. Blood-Based Biomarkers for Post-Stroke Cognitive Impairment.Current issues in molecular biology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. SAA4: An Underdog Within the Serum Amyloid a Superfamily?International journal of molecular sciences · 2026
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Effects of crowberry (Food & nutrition research · 2026
    Article
  18. Article
  19. Article
  20. Article

224 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

George H SackDepartments of Biological Chemistry and Medicine, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Physiology 615, Baltimore, MD, 21205, USA. gsack@jhmi.edu.ORCID 0000-0001-9307-6263
Johns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serum amyloid A (SAA) proteins were isolated and named over 50 years ago. They are small (104 amino acids) and have a striking relationship to the acute phase response with serum levels rising as much as 1000-fold in 24 hours. SAA proteins are encoded in a family of closely-related genes and have been remarkably conserved throughout vertebrate evolution. Amino-terminal fragments of SAA can form highly organized, insoluble fibrils that accumulate in "secondary" amyloid disease. Despite their evolutionary preservation and dynamic synthesis pattern SAA proteins have lacked well-defined physiologic roles. However, considering an array of many, often unrelated, reports now permits a more coordinated perspective. Protein studies have elucidated basic SAA structure and fibril formation. Appreciating SAA's lipophilicity helps relate it to lipid transport and metabolism as well as atherosclerosis. SAA's function as a cytokine-like protein has become recognized in cell-cell communication as well as feedback in inflammatory, immunologic, neoplastic and protective pathways. SAA likely has a critical role in control and possibly propagation of the primordial acute phase response. Appreciating the many cellular and molecular interactions for SAA suggests possibilities for improved understanding of pathophysiology as well as treatment and disease prevention.

Indexed as

Acute-Phase ReactionAnimalsAtherosclerosisCollagenasesHumansLipid MetabolismMammary Glands, HumanMaternal HealthMatrix MetalloproteinasesNeoplasmsSarcoidosis, PulmonarySerum Amyloid A ProteinCollagenasesMatrix MetalloproteinasesSerum Amyloid A Proteinacute phase response (APR)amyloidosisapolipoproteinarthritisatherosclerosiscytokineinflammationlipopolysaccharide (LPS)livermyeloid-derived suppressor cells (MDSC)SAASerum amyloid A

Identifiers

PMID30165816
PMCPMC6117975
OpenAlexW2889145334

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.