Evidence map›Paper›PMID 36067026›Full record

ArticleAnalytical chemistry2022

Enhanced Spatial Mapping of Histone Proteoforms in Human Kidney Through MALDI-MSI by High-Field UHMR-Orbitrap Detection.

Kevin J Zemaitis, Dušan Veličković, William Kew, Kyle L Fort, Maria Reinhardt-Szyba, Annapurna Pamreddy, Yanli Ding, Dharam Kaushik, Kumar Sharma, Alexander A Makarov and 2 more

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.

  1. Pooled it
  2. Emerging technologies in the spatial proteomics landscape.Analytical and bioanalytical chemistry · 2026
    Review
  3. Review
  4. MALDI spatial proteomics: a mini review of approaches and techniques.Analytical methods : advancing methods and applications · 2026
    Review
  5. Review
  6. Review
  7. Mass Spectrometry Imaging.Analytical chemistry · 2025
    Review
  8. Review
  9. Article
  10. Article
  11. Spatial Proteomics towards cellular Resolution.Expert review of proteomics · 2024
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Journal of the American Society for Mass Spectrometry · 2023
    Article
  18. Article
  19. Article
  20. 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

12 authors at 4 institutions in 3 countries.

Kevin J ZemaitisEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.ORCID 0000-0002-3524-9776
Dušan VeličkovićEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.ORCID 0000-0001-7945-9620
William KewEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.ORCID 0000-0002-4281-4630
Kyle L FortThermo Fisher Scientific (Bremen) GmbH, 28199 Bremen, Germany.
Maria Reinhardt-SzybaThermo Fisher Scientific (Bremen) GmbH, 28199 Bremen, Germany.
Annapurna PamreddyCenter for Renal Precision Medicine, Department of Medicine, University of Texas Health, San Antonio, Texas 78284, United States.
Yanli DingDepartment of Pathology and Laboratory Medicine, University of Texas Health, San Antonio, Texas 78284, United States.
Dharam KaushikDepartment of Urology, University of Texas Health, San Antonio, Texas 78284, United States.
Kumar SharmaCenter for Renal Precision Medicine, Department of Medicine, University of Texas Health, San Antonio, Texas 78284, United States.
Alexander A MakarovThermo Fisher Scientific (Bremen) GmbH, 28199 Bremen, Germany.ORCID 0000-0002-7046-6709
Mowei ZhouEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.ORCID 0000-0003-3575-3224
Ljiljana Paša-TolićEnvironmental Molecular Sciences Laboratory, Pacific Northwest National Laboratory, Richland, Washington 99352, United States.
Pacific Northwest National Laboratory · USThe University of Texas Health Science Center at San Antonio · USThermo Fisher Scientific (Germany) · DEUtrecht University · NL

Funding

Spatially resolved characterization of proteoforms for functional proteomicsUH3CA256959 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI PASA-TOLIC, LJILJANA · 2022 to 2023
$1.0M
Spatially resolved characterization of proteoforms for functional proteomicsUG3CA256959 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI PASA-TOLIC, LJILJANA · 2020 to 2021
$600k
NCI NIH HHS UG3 CA256959NCI NIH HHS UH3 CA256959
6 · The paper itself

Abstract

Core histones including H2A, H2B, H3, and H4 are key modulators of cellular repair, transcription, and replication within eukaryotic cells, playing vital roles in the pathogenesis of disease and cellular responses to environmental stimuli. Traditional mass spectrometry (MS)-based bottom-up and top-down proteomics allows for the comprehensive identification of proteins and of post-translational modification (PTM) harboring proteoforms. However, these methodologies have difficulties preserving near-cellular spatial distributions because they typically require laser capture microdissection (LCM) and advanced sample preparation techniques. Herein, we coupled a matrix-assisted laser desorption/ionization (MALDI) source with a Thermo Scientific Q Exactive HF Orbitrap MS upgraded with ultrahigh mass range (UHMR) boards for the first demonstration of complementary high-resolution accurate mass (HR/AM) measurements of proteoforms up to 16.5 kDa directly from tissues using this benchtop mass spectrometer. The platform achieved isotopic resolution throughout the detected mass range, providing confident assignments of proteoforms with low ppm mass error and a considerable increase in duty cycle over other Fourier transform mass analyzers. Proteoform mapping of core histones was demonstrated on sections of human kidney at near-cellular spatial resolution, with several key distributions of histone and other proteoforms noted within both healthy biopsy and a section from a renal cell carcinoma (RCC) containing nephrectomy. The use of MALDI-MS imaging (MSI) for proteoform mapping demonstrates several steps toward high-throughput accurate identification of proteoforms and provides a new tool for mapping biomolecule distributions throughout tissue sections in extended mass ranges.

Indexed as

HistonesProteomicsFourier AnalysisHumansKidneySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationHistones

Identifiers

PMID36067026
PMCPMC10064997
OpenAlexW4294805279

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.