Evidence map›Paper›PMID 31152061›Full record

ArticleThe Journal of biological chemistry2019

Differential cleavage of lysyl oxidase by the metalloproteinases BMP1 and ADAMTS2/14 regulates collagen binding through a tyrosine sulfate domain.

Tamara Rosell-García, Alberto Paradela, Gema Bravo, Laura Dupont, Mourad Bekhouche, Alain Colige, Fernando Rodriguez-Pascual

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 58 citations in OpenAlex.

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  18. Multifunctional Lysyl Oxidases.International journal of molecular sciences · 2023
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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

7 authors at 2 institutions in 2 countries.

Tamara Rosell-GarcíaCentro de Biología Molecular "Severo Ochoa," Consejo Superior de Investigaciones Científicas (C.S.I.C.), Universidad Autónoma de Madrid, 28049 Madrid, Spain.ORCID 0000-0001-8784-2769
Alberto ParadelaProteomics Facility, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (C.S.I.C.), 28049 Madrid, Spain.
Gema BravoProteomics Facility, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas (C.S.I.C.), 28049 Madrid, Spain.
Laura DupontLaboratory of Connective Tissues Biology, GIGA, University of Liège, 4000 Sart Tilman, Belgium.
Mourad BekhoucheLaboratory of Connective Tissues Biology, GIGA, University of Liège, 4000 Sart Tilman, Belgium.
Alain ColigeLaboratory of Connective Tissues Biology, GIGA, University of Liège, 4000 Sart Tilman, Belgium.
Fernando Rodriguez-PascualCentro de Biología Molecular "Severo Ochoa," Consejo Superior de Investigaciones Científicas (C.S.I.C.), Universidad Autónoma de Madrid, 28049 Madrid, Spain frodriguez@cbm.csic.es.ORCID 0000-0002-9765-9578
Consejo Superior de Investigaciones Científicas · ESUniversity of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagens are the main structural component of the extracellular matrix and provide biomechanical properties to connective tissues. A critical step in collagen fibril formation is the proteolytic removal of N- and C-terminal propeptides from procollagens by metalloproteinases of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) and BMP1 (bone morphogenetic protein 1)/Tolloid-like families, respectively. BMP1 also cleaves and activates the lysyl oxidase (LOX) precursor, the enzyme catalyzing the initial step in the formation of covalent collagen cross-links, an essential process for fibril stabilization. In this study, using murine skin fibroblasts and HEK293 cells, along with immunoprecipitation, LOX enzymatic activity, solid-phase binding assays, and proteomics analyses, we report that the LOX precursor is proteolytically processed by the procollagen N-proteinases ADAMTS2 and ADAMTS14 between Asp-218 and Tyr-219, 50 amino acids downstream of the BMP1 cleavage site. We noted that the LOX sequence between the BMP1- and ADAMTS-processing sites contains several conserved tyrosine residues, of which some are post-translationally modified by tyrosine

Indexed as

ADAMTS ProteinsAnimalsBinding SitesBone Morphogenetic Protein 1CattleCells, CulturedCollagenHEK293 CellsHumansMiceProtein BindingProtein-Lysine 6-OxidaseProtein Processing, Post-TranslationalProteolysisTyrosineADAMTS ProteinsBone Morphogenetic Protein 1CollagenProtein-Lysine 6-OxidaseTyrosinetyrosine O-sulfateADAMTScollagenconnective tissueextracellular matrixlysyl oxidasemetalloproteinasepost-translational modification (PTM)proteolysistyrosine sulfation

Identifiers

PMID31152061
PMCPMC6643040
OpenAlexW2947176488

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.