Evidence map›Paper›PMID 22842973›Full record

ArticleNature chemical biology2012

Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in tissue genesis.

Gautam Bhave, Christopher F Cummings, Roberto M Vanacore, Chino Kumagai-Cresse, Isi A Ero-Tolliver, Mohamed Rafi, Jeong-Suk Kang, Vadim Pedchenko, Liselotte I Fessler, John H Fessler and 1 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

142 citing papers in PubMed, 256 citations in OpenAlex.

  1. Article
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  7. Lactoperoxidase is a candidate for mediating neuromelanin formation in the human substantia nigra.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Basement membrane structure and function: Relating biology to mechanics.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  16. Collagen IV in Gould syndrome and Alport syndrome.Nature reviews. Nephrology · 2025
    Review
  17. Article
  18. The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  19. Article
  20. 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

82 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 2 countries.

Gautam BhaveDivision of Nephrology and Hypertension, Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.
Christopher F Cummings
Roberto M Vanacore
Chino Kumagai-Cresse
Isi A Ero-Tolliver
Mohamed Rafi
Jeong-Suk Kang
Vadim Pedchenko
Liselotte I Fessler
John H Fessler
Billy G Hudson
Vanderbilt University Medical Center · USUniversity of California, Los Angeles · USKorea National Institute of Health · KRMount Desert Island Biological Laboratory · US

Funding

TYPE IV COLLAGEN, LAMININS, AND INTEGRINS IN NORMAL AND DISEASED GLOMERULIP01DK065123 · NIDDK · VANDERBILT UNIVERSITY · PI HUDSON, BILLY GERALD · 2003 to 2012
$12.9M
STUDIES ON THE STRUCTURE OF BASEMENT MEMBRANESR01DK018381 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Sergey Petrovich Budko, BILLY GERALD HUDSON · 1986 to 2026
$12.4M
VANDERBILT NEPHROLOGY TRAINING PROGRAMT32DK007569 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI HARRIS, RAYMOND C., IKIZLER, TALAT ALP · 1988 to 2024
$5.8M
STUDIES ON THE STRUCTURE OF BASEMENT MEMBRANESR37DK018381 · NIDDK · VANDERBILT UNIVERSITY · PI HUDSON, BILLY GERALD · 2000 to 2009
$4.5M
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 2P01 DK065123NIDDK NIH HHS DK18381-38S1NIDDK NIH HHS P01 DK065123NIDDK NIH HHS R01 DK018381NIDDK NIH HHS R01 DK099467NIDDK NIH HHS R01 DK18381NIDDK NIH HHS T32 DK007569
6 · The paper itself

Abstract

Collagen IV comprises the predominant protein network of basement membranes, a specialized extracellular matrix, which underlie epithelia and endothelia. These networks assemble through oligomerization and covalent crosslinking to endow mechanical strength and shape cell behavior through interactions with cell-surface receptors. A recently discovered sulfilimine (S=N) bond between a methionine sulfur and hydroxylysine nitrogen reinforces the collagen IV network. We demonstrate that peroxidasin, an enzyme found in basement membranes, catalyzes formation of the sulfilimine bond. Drosophila peroxidasin mutants have disorganized collagen IV networks and torn visceral muscle basement membranes, pointing to a critical role for the enzyme in tissue biogenesis. Peroxidasin generates hypohalous acids as reaction intermediates, suggesting a paradoxically anabolic role for these usually destructive oxidants. This work highlights sulfilimine bond formation as what is to our knowledge the first known physiologic function for peroxidasin, a role for hypohalous oxidants in tissue biogenesis, and a possible role for peroxidasin in inflammatory diseases.

Indexed as

AcidsAnimalsCatalysisCollagen Type IVDrosophilaExtracellular Matrix ProteinsIminesPeroxidasePeroxidasinAcidsCollagen Type IVExtracellular Matrix ProteinsIminesPeroxidasePeroxidasin

Identifiers

PMID22842973
PMCPMC4128002
OpenAlexW2081781085

What OpenQuestion holds

Textmetadata
LicenceTDM
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.