Evidence map›Paper›PMID 32617419›Full record

ArticleBiochemistry and biophysics reports2020

Structural features and oligomeric nature of human podocin domain.

Sandeep K N Mulukala, Shivkumar S Irukuvajjula, Krishan Kumar, Kanchan Garai, Pannuru Venkatesu, Ramakrishna Vadrevu, Anil K Pasupulati

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry and biophysics reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Kidney international reports · 2026
    Article
  2. Biophysical characterization and insights into the oligomeric nature of CD2-associated protein.International journal of biochemistry and molecular biology · 2024
    Article
  3. Article
  4. Review
  5. Biomarkers of Kidney Disease in Horses: A Review of the Current Literature.Animals : an open access journal from MDPI · 2022
    Review
  6. Article
  7. 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 4 institutions in 1 country.

Sandeep K N MulukalaDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, 500046, India.
Shivkumar S IrukuvajjulaDepartment of Biological Sciences, Birla Institute of Technology and Sciences, Pilani Hyderabad Campus, Hyderabad, 500078, India.
Krishan KumarDepartment of Chemistry, University of Delhi, New Delhi, 110 007, India.
Kanchan GaraiTata Institute of Fundamental Research, Hyderabad, 500019, India.
Pannuru VenkatesuDepartment of Chemistry, University of Delhi, New Delhi, 110 007, India.
Ramakrishna VadrevuDepartment of Biological Sciences, Birla Institute of Technology and Sciences, Pilani Hyderabad Campus, Hyderabad, 500078, India.
Anil K PasupulatiDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, 500046, India.
Birla Institute of Technology and Science - Hyderabad Campus · INUniversity of Delhi · INUniversity of Hyderabad · INTata Institute of Fundamental Research · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Podocytes are crucial cells of the glomerular filtration unit and plays a vital role at the interface of the blood-urine barrier. Podocyte slit-diaphragm is a modified tight junction that facilitates size and charge-dependent permselectivity. Several proteins including podocin, nephrin, CD2AP, and TRPC6 form a macromolecular assembly and constitute the slit-diaphragm. Podocin is an integral membrane protein attached to the inner membrane of the podocyte via a short transmembrane region (101-125). The cytosolic N- and C-terminus help podocin to attain a hook-like structure. Podocin shares 44% homology with stomatin family proteins and similar to the stomatin proteins, podocin was shown to associate into higher-order oligomers at the site of slit-diaphragm. However, the stoichiometry of the homo-oligomers and how it partakes in the macromolecular assemblies with other slit-diaphragm proteins remains elusive. Here we investigated the oligomeric propensity of a truncated podocin construct (residues:126-350). We show that the podocin domain majorly homo-oligomerizes into a 16-mer. Circular dichroism and fluorescence spectroscopy suggest that the 16-mer oligomer has considerable secondary structure and moderate tertiary packing.

Indexed as

CD2AP, CD-2 associated proteinCD, Circular dichroismGFB, Glomerular filtration barrierIDRs, Intrinsically disordered regionsMALS, multi-angle light scatteringNEPH, Nephrin-like proteinNephrotic syndromeNPHS1 & 2, Nephrotic syndrome-type I and type IINS, Nephrotic syndromePodocinPodocyteProteinuriaSD, slit-diaphragmSEC, Size-exclusion chromatographySlit-diaphragmSRNS, steroid-resistant NSTRPC6, Transient receptor potential cation channel subfamily C member 6ZO-1, Zonula occludens-1

Identifiers

PMID32617419
PMCPMC7322680
OpenAlexW3037819287

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.