Evidence map›Paper›PMID 33775698›Full record

ArticleThe Journal of biological chemistry

Collagen IV

Sergei P Boudko, Ryan Bauer, Sergei V Chetyrkin, Sergey Ivanov, Jarrod Smith, Paul A Voziyan, Billy G Hudson

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. IncreasedWellcome open research · 2025
    Article
  7. Collagen IV of basement membranes: II. Emergence of collagen IVThe Journal of biological chemistry · 2023
    Article
  8. Review
  9. ModelCraft: an advanced automated model-building pipeline using Buccaneer.Acta crystallographica. Section D, Structural biology · 2022
    Article
  10. Article
  11. Article
  12. Collagen IVThe Journal of biological chemistry
    Article
  13. Collagen IVThe Journal of biological chemistry
    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

7 authors at 2 institutions in 1 country.

Sergei P BoudkoDepartment of Medicine, Division of Nephrology and Hypertension, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Department of Biochemistry, Center for Structural Biology, Vanderbilt University, Nashville, Tennessee, USA. Electronic address: Sergey.Budko@vumc.org.
Ryan BauerDepartment of Medicine, Division of Nephrology and Hypertension, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Sergei V ChetyrkinDepartment of Medicine, Division of Nephrology and Hypertension, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Sergey IvanovDepartment of Medicine, Division of Nephrology and Hypertension, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Jarrod SmithDepartment of Biochemistry, Center for Structural Biology, Vanderbilt University, Nashville, Tennessee, USA.
Paul A VoziyanDepartment of Medicine, Division of Nephrology and Hypertension, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Billy G HudsonDepartment of Medicine, Division of Nephrology and Hypertension, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Center for Matrix Biology, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Department of Biochemistry, Center for Structural Biology, Vanderbilt University, Nashville, Tennessee, USA; Aspirnaut, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Department of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, Tennessee, USA; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, Tennessee, USA; Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, Tennessee, USA; Vanderbilt-Ingram Cancer Center, Vanderbilt University, Nashville, Tennessee, USA.
Vanderbilt University Medical Center · USVanderbilt University · US

Funding

STUDIES ON THE STRUCTURE OF BASEMENT MEMBRANESR01DK018381 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Sergey Petrovich Budko, BILLY GERALD HUDSON · 1986 to 2026
$12.4M
Novel Integrated Analyses of Human Diabetic NephropathyR24DK103067 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI CAPRIOLI, RICHARD M, DENNY, JOSHUA C. · 2014 to 2018
$6.5M
Glucose Modifications of Proteins in Diabetic NephropathyR01DK065138 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI HUDSON, BILLY GERALD, VOZIYAN, PAUL A · 2003 to 2020
$6.3M
NIDDK NIH HHS R01 DK018381NIDDK NIH HHS R01 DK065138NIDDK NIH HHS R24 DK103067
6 · The paper itself

Abstract

Our recent work identified a genetic variant of the α345 hexamer of the collagen IV scaffold that is present in patients with glomerular basement membrane diseases, Goodpasture's disease (GP) and Alport syndrome (AS), and phenocopies of AS in knock-in mice. To understand the context of this "Zurich" variant, an 8-amino acid appendage, we developed a construct of the WT α345 hexamer using the single-chain NC1 trimer technology, which allowed us to solve a crystal structure of this key connection module. The α345 hexamer structure revealed a ring of 12 chloride ions at the trimer-trimer interface, analogous to the collagen α121 hexamer, and the location of the 170 AS variants. The hexamer surface is marked by multiple pores and crevices that are potentially accessible to small molecules. Loop-crevice-loop features constitute bioactive sites, where pathogenic pathways converge that are linked to AS and GP, and, potentially, diabetic nephropathy. In Pedchenko et al., we demonstrate that these sites exhibit conformational plasticity, a dynamic property underlying assembly of bioactive sites and hexamer dysfunction. The α345 hexamer structure is a platform to decipher how variants cause AS and how hypoepitopes can be triggered, causing GP. Furthermore, the bioactive sites, along with the pores and crevices on the hexamer surface, are prospective targets for therapeutic interventions.

Indexed as

MutationProtein MultimerizationAnimalsAnti-Glomerular Basement Membrane DiseaseCollagen Type IVCrystallography, X-RayMiceModels, MolecularNephritis, HereditaryProtein Structure, QuaternaryCollagen Type IVatomic force microscopy (AFM)collagenextracellular matrixgenetic diseaseX-ray crystallography

Identifiers

PMID33775698
PMCPMC8093946
OpenAlexW3139165104

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.