Evidence map›Paper›PMID 28864775›Full record

ArticleThe Journal of biological chemistry2017

Proteolytic processing of lysyl oxidase-like-2 in the extracellular matrix is required for crosslinking of basement membrane collagen IV.

Alberto J López-Jiménez, Trayambak Basak, Roberto M Vanacore

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

36 citing papers in PubMed, 54 citations in OpenAlex.

  1. Enzymatic and non-enzymatic oxidation of fibrillar collagen.Redox report : communications in free radical research · 2026
    Review
  2. Review
  3. Glycocalyx and basal lamina in neurological disorders.Matrix biology : journal of the International Society for Matrix Biology · 2026
    Review
  4. Article
  5. Review
  6. Collagen IV in Gould syndrome and Alport syndrome.Nature reviews. Nephrology · 2025
    Review
  7. Basement membranes at a glance.Journal of cell science · 2025
    Review
  8. The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  9. Beyond classical collagen: basement membrane collagen IV in age-associated lung diseases.European respiratory review : an official journal of the European Respiratory Society · 2025
    Review
  10. Review
  11. Article
  12. Article
  13. LOXL2 in Cancer: A Two-Decade Perspective.International journal of molecular sciences · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. An in situ activity assay for lysyl oxidases.Communications biology · 2021
    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

3 authors at 1 institution in 1 country.

Alberto J López-JiménezFrom the Department of Medicine, Division of Nephrology and Hypertension and.ORCID 0000-0002-4992-631X
Trayambak BasakFrom the Department of Medicine, Division of Nephrology and Hypertension and.ORCID 0000-0001-7683-3189
Roberto M VanacoreFrom the Department of Medicine, Division of Nephrology and Hypertension and roberto.vanacore@vanderbilt.edu.ORCID 0000-0002-2886-0606
Hypertension Institute · US

Funding

The role of lysyl oxidase like-2 in chronic kidney diseaseR01DK099467 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI VANACORE, ROBERTO MARCELO · 2013 to 2023
$3.8M
NIDDK NIH HHS R01 DK099467
6 · The paper itself

Abstract

Lysyl oxidase-like-2 (LOXL2) is an enzyme secreted into the extracellular matrix that crosslinks collagens by mediating oxidative deamination of lysine residues. Our previous work demonstrated that this enzyme crosslinks the 7S domain, a structural domain that stabilizes collagen IV scaffolds in the basement membrane. Despite its relevant role in extracellular matrix biosynthesis, little is known about the structural requirements of LOXL2 that enable collagen IV crosslinking. In this study, we demonstrate that LOXL2 is processed extracellularly by serine proteases, generating a 65-kDa form lacking the first two scavenger receptor cysteine-rich domains. Site-specific mutagenesis to prevent proteolytic processing generated a full-length enzyme that is active

Indexed as

ProteolysisAmino Acid OxidoreductasesBasement MembraneCollagen Type IVExtracellular MatrixHEK293 CellsHumansMutagenesis, Site-DirectedProtein DomainsProtein Processing, Post-TranslationalAmino Acid OxidoreductasesCollagen Type IVLOXL2 protein, humanbasement membranecollagenenzyme processingextracellular matrixLOXL2lysyl oxidaseposttranslational modification (PTM)protein crosslinkingproteolytic processing

Identifiers

PMID28864775
PMCPMC5641870
OpenAlexW2751877422

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.