Evidence map›Paper›PMID 26924944›Full record

ArticleProteome science2016

Label-free proteomic methodology for the analysis of human kidney stone matrix composition.

Frank A Witzmann, Andrew P Evan, Fredric L Coe, Elaine M Worcester, James E Lingeman, James C Williams

Open access · goldAbstract read
In one paragraph

Article in Proteome science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Frank A WitzmannDepartment of Cellular and Integrative Physiology, Indiana University School of Medicine, 635 Barnhill Drive, Room 362A, Indianapolis, IN 46202-5120 USA.
Andrew P EvanDepartment of Anatomy and Cell Biology, Indiana University School of Medicine, Indianapolis, IN USA.
Fredric L CoeDepartment of Medicine, Nephrology Section, University of Chicago, Chicago, IL USA.
Elaine M WorcesterDepartment of Medicine, Nephrology Section, University of Chicago, Chicago, IL USA.
James E LingemanInternational Kidney Stone Institute, Methodist Hospital, Indianapolis, IN USA.
James C WilliamsDepartment of Anatomy and Cell Biology, Indiana University School of Medicine, Indianapolis, IN USA.
Indiana University School of MedicineUniversity of Chicago · USHouston Methodist · US

Funding

SWL AND RENAL INJURY AND STONE COMMINUTIONP01DK043881 · NIDDK · UNIVERSITY OF WASHINGTON · PI LIU, ZIYUE · 1994 to 2023
$33.5M
STONE FORMATION IN GENETIC HYPERCALCIURIAP01DK056788 · NIDDK · UNIVERSITY OF CHICAGO · PI BERGSLAND, KRISTIN J · 2000 to 2021
$22.5M
NIDDK NIH HHS P01 DK043881NIDDK NIH HHS P01 DK056788
6 · The paper itself

Abstract

backgroundKidney stone matrix protein composition is an important yet poorly understood aspect of nephrolithiasis. We hypothesized that this proteome is considerably more complex than previous reports have indicated and that comprehensive proteomic profiling of the kidney stone matrix may demonstrate relevant constitutive differences between stones. We have analyzed the matrices of two unique human calcium oxalate stones (CaOx-Ia and CaOx-Id) using a simple but effective chaotropic reducing solution for extraction/solubilization combined with label-free quantitative mass spectrometry to generate a comprehensive profile of their proteomes, including physicochemical and bioinformatic analysis.`.

resultsWe identified and quantified 1,059 unique protein database entries in the two human kidney stone samples, revealing a more complex proteome than previously reported. Protein composition reflects a common range of proteins related to immune response, inflammation, injury, and tissue repair, along with a more diverse set of proteins unique to each stone.

conclusionThe use of a simple chaotropic reducing solution and moderate sonication for extraction and solubilization of kidney stone powders combined with label-free quantitative mass spectrometry has yielded the most comprehensive list to date of the proteins that constitute the human kidney stone proteome.

Indexed as

Calcium oxalateKidney stoneLabel-free quantitative liquid chromatography–tandem mass spectrometryMatrix proteinNephrolithiasisProteomics

Identifiers

PMID26924944
PMCPMC4769560
OpenAlexW2282084501

What OpenQuestion holds

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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.