Evidence map›Paper›PMID 11707399›Full record

ArticleThe EMBO journal2001

Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca(2+) stabilization.

C D Chen, M E Huff, J Matteson, L Page, R Phillips, J W Kelly, W E Balch

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

48 citing papers in PubMed, 137 citations in OpenAlex.

  1. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
  3. Plant Hormone Cytokinin as Aggregation Modulator of Gelsolin Amyloidosis.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
  4. Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  5. Journal of neurology, neurosurgery, and psychiatry · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. The role of gelsolin domain 3 in familial amyloidosis (Finnish type).Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  20. 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

7 authors at 1 institution in 1 country.

C D ChenDepartments of Molecular and Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Road, La Jolla, CA 92037, USA.
M E Huff
J Matteson
L Page
R Phillips
J W Kelly
W E Balch
Scripps Research Institute · US

Funding

Probing the Biochemical Mechanisms of Amyloid DiseaseR01DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 1998 to 2025
$8.8M
Probing the biochemical mechanism of amyloid diseaseR37DK046335 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2006 to 2015
$5.9M
ROLE OF RAB PROTEINS AND CA2+ IN VESICULAR TRANSPORTR01GM042336 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD · 1990 to 2011
$4.8M
Structure and Function of Guanine Nucleotide Dissociation InhibitorR01GM033301 · NIGMS · YALE UNIVERSITY · PI BALCH, WILLIAM EDWARD · 1985 to 2012
$4.6M
BIOCHEMICAL MECHANISM OF AMYLOID DISEASER29DK046335 · NIDDK · TEXAS A&M UNIVERSITY SYSTEM · PI KELLY, JEFFERY W · 1993 to 1997
–
NIDDK NIH HHS DK46335NIDDK NIH HHS R01 DK046335NIDDK NIH HHS R37 DK046335NIGMS NIH HHS GM33301NIGMS NIH HHS GM42336NIGMS NIH HHS R01 GM033301NIGMS NIH HHS R01 GM042336
6 · The paper itself

Abstract

Hereditary familial amyloidosis of Finnish type (FAF) leading to amyloid in the peripheral and central nervous systems stems from deposition of a 71 residue fragment generated from the D187N/Y variants of plasma gelsolin by two sequential endoproteolytic events. We identify the protease accomplishing the first cleavage as furin, a proprotein convertase. Endoproteolysis of plasma gelsolin occurs in the trans-Golgi network due to the inability of the FAF variants to bind and be stabilized by Ca(2+). Secretion and processing of the FAF variants by furin can be uncoupled by blocking the convergence of the exocytic pathway transporting plasma gelsolin and the endocytic recycling of furin. We propose that coincidence of membrane trafficking pathways contributes to the development of proteolysis-initiated amyloid disease.

Indexed as

Amyloidosis, FamilialAnimalsCalciumCalorimetryCell LineCell MembraneCricetinaeDose-Response Relationship, DrugEndocytosisFurinGelsolinGenetic VariationGolgi ApparatusProtein BindingProtein Structure, TertiarySubtilisinsCalciumFurinGelsolinSubtilisins

Identifiers

PMID11707399
PMCPMC125307
OpenAlexW1975624408

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.