Evidence map›Paper›PMID 29332127›Full record

ArticleInvestigative ophthalmology & visual science2018

Proteome Profiling of Developing Murine Lens Through Mass Spectrometry.

Shahid Y Khan, Muhammad Ali, Firoz Kabir, Santosh Renuse, Chan Hyun Na, C Conover Talbot, Sean F Hackett, S Amer Riazuddin

Open access · goldAbstract read
In one paragraph

Article in Investigative ophthalmology & visual science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  3. An unbiased proteomic analysis of PAD4 in human monocytes: novel substrates, binding partners and subcellular localizations.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
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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

8 authors at 2 institutions in 1 country.

Shahid Y KhanThe Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
Muhammad AliThe Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
Firoz KabirThe Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
Santosh RenuseDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
Chan Hyun NaDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
C Conover TalbotInstitute for Basic Biomedical Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
Sean F HackettThe Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
S Amer RiazuddinThe Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland, United States.
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

Identification of Lens Function Through Analysis of Human CataractsR01EY022714 · NEI · JOHNS HOPKINS UNIVERSITY · PI RIAZUDDIN, AMER · 2014 to 2018
$2.0M
NEI NIH HHS R01 EY022714
6 · The paper itself

Abstract

Purpose: We previously completed a comprehensive profile of the mouse lens transcriptome. Here, we investigate the proteome of the mouse lens through mass spectrometry-based protein sequencing at the same embryonic and postnatal time points. Methods: We extracted mouse lenses at embryonic day 15 (E15) and 18 (E18) and postnatal day 0 (P0), 3 (P3), 6 (P6), and 9 (P9). The lenses from each time point were preserved in three distinct pools to serve as biological replicates for each developmental stage. The total cellular protein was extracted from the lens, digested with trypsin, and labeled with isobaric tandem mass tags (TMT) for three independent TMT experiments. Results: A total of 5404 proteins were identified in the mouse ocular lens in at least one TMT set, 4244 in two, and 3155 were present in all three TMT sets. The majority of the proteins exhibited steady expression at all six developmental time points; nevertheless, we identified 39 proteins that exhibited an 8-fold differential (higher or lower) expression during the developmental time course compared to their respective levels at E15. The lens proteome is composed of diverse proteins that have distinct biological properties and functional characteristics, including proteins associated with cataractogenesis and autophagy. Conclusions: We have established a comprehensive profile of the developing murine lens proteome. This repository will be helpful in identifying critical components of lens development and processes essential for the maintenance of its transparency.

Indexed as

AnimalsAnimals, NewbornEye ProteinsGene Expression ProfilingLens, CrystallineMass SpectrometryMiceModels, AnimalProteomeRNA, MessengerEye ProteinsProteomeRNA, Messenger

Identifiers

PMID29332127
PMCPMC5769801
OpenAlexW2783014736

What OpenQuestion holds

Textmetadata
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.