Evidence map›Paper›PMID 10359653›Full record

ArticleThe Biochemical journal1999

N-terminal domains of fibrillin 1 and fibrillin 2 direct the formation of homodimers: a possible first step in microfibril assembly.

T M Trask, T M Ritty, T Broekelmann, C Tisdale, R P Mecham

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly.Matrix biology : journal of the International Society for Matrix Biology · 2019
    Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Biogenesis and function of fibrillin assemblies.Cell and tissue research · 2010
    Review
  11. Fibrillin assembly requires fibronectin.Molecular biology of the cell · 2009
    Article
  12. Article
  13. Extracellular matrix in the trabecular meshwork.Experimental eye research · 2008
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Marfan syndrome in the third Millennium.European journal of human genetics : EJHG · 2002
    Review
  19. Fibrillin: from microfibril assembly to biomechanical function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2002
    Review
  20. Fibrillin-rich microfibrils: elastic biopolymers of the extracellular matrix.Journal of muscle research and cell motility · 2002
    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

5 authors at 1 institution in 1 country.

T M TraskDepartment of Cell Biology and Physiology, Washington University School of Medicine, Box 8228, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
T M Ritty
T Broekelmann
C Tisdale
R P Mecham
Washington University in St. Louis · US

Funding

VASCULAR CELL DIVERSITY IN PULMONARY HYPERTENSIONP01HL029594 · NHLBI · WASHINGTON UNIVERSITY · PI HOLTZMAN, MICHAEL J · 1985 to 2012
$23.8M
ASSEMBLY OF LUNG ELASTINR37HL053325 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 2000 to 2009
$4.1M
ASSEMBLY OF LUNG ELASTINR01HL053325 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 1995 to 2019
$3.6M
ELASTIN/LAMININ RECEPTORR01HL041926 · NHLBI · WASHINGTON UNIVERSITY · PI MECHAM, ROBERT P. · 1989 to 1998
–
NHLBI NIH HHS HL29594NHLBI NIH HHS HL41926NHLBI NIH HHS HL53325
6 · The paper itself

Abstract

Aggregation of fibrillin molecules via disulphide bonds is postulated to be an early step in microfibril assembly. By expressing fragments of fibrillin 1 and fibrillin 2 in a mammalian expression system, we found that the N-terminal region of each protein directs the formation of homodimers and that disulphide bonds stabilize this interaction. A large fragment of fibrillin 1 containing much of the region downstream from the N-terminus remained as a monomer when expressed in the same cell system, indicating that this region of the protein lacks dimerization domains. This finding also confirms that the overexpression of fibrillin fragments does not in itself lead to spurious dimer formation. Pulse-chase analysis demonstrated that dimer formation occurred intracellularly, suggesting that the process of fibrillin aggregation is initiated early after biosynthesis of the molecules. These findings also implicate the N-terminal region of fibrillin 1 and fibrillin 2 in directing the formation of a dimer intermediate that aggregates to form the functional microfibril.

Indexed as

AlkylationAnimalsBlotting, WesternCHO CellsCricetinaeCysteineDimerizationDisulfidesDithiothreitolFibrillinsGlycineMicrofilament ProteinsMolecular WeightPeptide FragmentsPrecipitin TestsProlineCysteineDisulfidesDithiothreitolFibrillinsGlycineMicrofilament ProteinsPeptide FragmentsProline

Identifiers

PMID10359653
PMCPMC1220300
OpenAlexW2130103086

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.