Evidence map›Paper›PMID 32482891›Full record

ArticleThe Journal of biological chemistry2020

Mechanisms of aortic carboxypeptidase-like protein secretion and identification of an intracellularly retained variant associated with Ehlers-Danlos syndrome.

Neya Vishwanath, William J Monis, Gwendolyn A Hoffmann, Bhavana Ramachandran, Vincent DiGiacomo, Joyce Y Wong, Michael L Smith, Matthew D Layne

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  11. Case report: further delineation ofFrontiers in genetics · 2023
    Article
  12. Case report: Two individuals withFrontiers in genetics · 2023
    Article
  13. Article
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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

8 authors at 1 institution in 1 country.

Neya VishwanathDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts, USA.
William J MonisDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts, USA.
Gwendolyn A HoffmannDepartment of Biomedical Engineering, Boston University, Boston, Massachusetts, USA.ORCID 0000-0001-7492-4503
Bhavana RamachandranDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts, USA.
Vincent DiGiacomoDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts, USA.
Joyce Y WongDepartment of Biomedical Engineering, Boston University, Boston, Massachusetts, USA.ORCID 0000-0002-3526-6381
Michael L SmithDepartment of Biomedical Engineering, Boston University, Boston, Massachusetts, USA.
Matthew D LayneDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts, USA mlayne@bu.edu.ORCID 0000-0003-0007-4870
Boston University · US

Funding

TRAINING PROGRAM IN QUANTITATIVE BIOLOGY AND PHYSIOLOGYT32GM008764 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI WHITE, JOHN A. · 2001 to 2021
$5.9M
Role of ACLP in Vascular Smooth Muscle BiologyR01HL078869 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI LAYNE, MATTHEW D · 2007 to 2011
$2.2M
Mechanically active extracellular matrix fibers for tissue engineering applicationsF31HL151082 · NHLBI · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI HOFFMANN, GWENDOLYN ANN · 2020 to 2021
$64k
NHLBI NIH HHS F31 HL151082NHLBI NIH HHS R01 HL078869NIGMS NIH HHS T32 GM008764
6 · The paper itself

Abstract

Aortic carboxypeptidase-like protein (ACLP) is a collagen-binding extracellular matrix protein that has important roles in wound healing and fibrosis. ACLP contains thrombospondin repeats, a collagen-binding discoidin domain, and a catalytically inactive metallocarboxypeptidase domain. Recently, mutations in the ACLP-encoding gene, AE-binding protein 1 (

Indexed as

Protein Processing, Post-TranslationalAmino Acid SubstitutionAnimalsCarboxypeptidasesEhlers-Danlos SyndromeExtracellular MatrixGlycosylationMiceMutagenesis, Site-DirectedMutation, MissenseRepressor ProteinsAebp1 protein, mouseCarboxypeptidasesRepressor Proteinsaortic carboxypeptidase-like protein (ACLP)collagenEhlers-Danlos syndromeendoplasmic reticulum stress (ER stress)extracellular matrix (ECM)genetic diseaseglycoprotein secretionglycosylationpost-translational modification (PTM)

Identifiers

PMID32482891
PMCPMC7363150
OpenAlexW3028654748

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.