Evidence map›Paper›PMID 21811627›Full record

ArticlePloS one2011

Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis.

Nahuel A Ramella, Omar J Rimoldi, Eduardo D Prieto, Guillermo R Schinella, Susana A Sanchez, María S Jaureguiberry, María E Vela, Sergio T Ferreira, M Alejandra Tricerri

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

34 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. A Study on Multiple Facets of Apolipoprotein A1 Milano.Applied biochemistry and biotechnology · 2023
    Review
  7. On the Aggregation of Apolipoprotein A-I.International journal of molecular sciences · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

9 authors at 5 institutions in 4 countries.

Nahuel A RamellaInstituto de Investigaciones Bioquímicas La Plata (INIBIOLP), CCT-CONICET, La Plata, Argentina.
Omar J Rimoldi
Eduardo D Prieto
Guillermo R Schinella
Susana A Sanchez
María S Jaureguiberry
María E Vela
Sergio T Ferreira
M Alejandra Tricerri
Universidad Nacional de La Plata · ARBiochemistry Research Institute of La Plata · ARConsejo Nacional de Investigaciones Científicas y Técnicas · ARFluor (United States) · USUniversidade Federal do Rio de Janeiro · BR

Funding

YEAST RIBOSOMAL STALK COMPOSITION IN VIVO BY TWO-PHOTON FCS AND PCH ANALYSISP41RR003155 · NCRR · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GRATTON, ENRICO · 1986 to 2011
$14.9M
NCRR NIH HHS 5 P41 RR-03155NCRR NIH HHS P41 RR003155
6 · The paper itself

Abstract

Amyloidoses constitute a group of diseases in which soluble proteins aggregate and deposit extracellularly in tissues. Nonhereditary apolipoprotein A-I (apoA-I) amyloid is characterized by deposits of nonvariant protein in atherosclerotic arteries. Despite being common, little is known about the pathogenesis and significance of apoA-I deposition. In this work we investigated by fluorescence and biochemical approaches the impact of a cellular microenvironment associated with chronic inflammation on the folding and pro-amyloidogenic processing of apoA-I. Results showed that mildly acidic pH promotes misfolding, aggregation, and increased binding of apoA-I to extracellular matrix elements, thus favoring protein deposition as amyloid like-complexes. In addition, activated neutrophils and oxidative/proteolytic cleavage of the protein give rise to pro amyloidogenic products. We conclude that, even though apoA-I is not inherently amyloidogenic, it may produce non hereditary amyloidosis as a consequence of the pro-inflammatory microenvironment associated to atherogenesis.

Indexed as

AmyloidAnilino NaphthalenesulfonatesAnimalsApolipoprotein A-IAtherosclerosisBenzothiazolesCHO CellsCholesterolCricetinaeCricetulusHeparinHumansHydrogen-Ion ConcentrationHypochlorous AcidMatrix Metalloproteinase 12Neutrophil Activation5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)AmyloidAnilino NaphthalenesulfonatesAPOA1 protein, humanApolipoprotein A-IBenzothiazolesCholesterolHeparinHypochlorous AcidMatrix Metalloproteinase 12SolventsTetradecanoylphorbol AcetateThiazolesthioflavin TTryptophan

Identifiers

PMID21811627
PMCPMC3139661
OpenAlexW2085498526

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.