Evidence map›Paper›PMID 22943415›Full record

ReviewGenome medicine2012

Mass spectrometry for translational proteomics: progress and clinical implications.

Erin Shammel Baker, Tao Liu, Vladislav A Petyuk, Kristin E Burnum-Johnson, Yehia M Ibrahim, Gordon A Anderson, Richard D Smith

Abstract readReview
In one paragraph

Review in Genome medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

35 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  14. Utilizing Ion Mobility to Identify Isobaric Post-Translational Modifications: Resolving Acrolein and Propionyl Lysine Adducts by TIMS Mass Spectrometry.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2018
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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

7 authors.

Erin Shammel BakerBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Tao LiuBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Vladislav A PetyukBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Kristin E Burnum-JohnsonBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Yehia M IbrahimBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Gordon A AndersonBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Richard D SmithBiological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA.

Funding

WORKSHOP AND TRAINING ACTIVITIESP41RR018522 · NCRR · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI BELOV, MIKHAIL · 2003 to 2011
$25.1M
Equipment Supplement Request for a Research Resource for Ultra-sensitive High Throughput ProteomicsP41GM103493 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2012 to 2022
$22.6M
PNNL Clinical Proteome Characterization CenterU24CA160019 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI RODLAND, KARIN D, SMITH, RICHARD D · 2011 to 2016
$15.7M
A Proteomics Platform for Quantitative, Ultra-High Throughput, and Ultra-SensitivR33CA126191 · NCI · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI SMITH, RICHARD D · 2008 to 2010
$2.4M
NCI NIH HHS R33 CA126191NCI NIH HHS U24 CA160019NCRR NIH HHS P41 RR018522NIGMS NIH HHS P41 GM103493
6 · The paper itself

Abstract

The utility of mass spectrometry (MS)-based proteomic analyses and their clinical applications have been increasingly recognized over the past decade due to their high sensitivity, specificity and throughput. MS-based proteomic measurements have been used in a wide range of biological and biomedical investigations, including analysis of cellular responses and disease-specific post-translational modifications. These studies greatly enhance our understanding of the complex and dynamic nature of the proteome in biology and disease. Some MS techniques, such as those for targeted analysis, are being successfully applied for biomarker verification, whereas others, including global quantitative analysis (for example, for biomarker discovery), are more challenging and require further development. However, recent technological improvements in sample processing, instrumental platforms, data acquisition approaches and informatics capabilities continue to advance MS-based applications. Improving the detection of significant changes in proteins through these advances shows great promise for the discovery of improved biomarker candidates that can be verified pre-clinically using targeted measurements, and ultimately used in clinical studies - for example, for early disease diagnosis or as targets for drug development and therapeutic intervention. Here, we review the current state of MS-based proteomics with regard to its advantages and current limitations, and we highlight its translational applications in studies of protein biomarkers.

Indexed as

biomarkerclinical proteomicsion mobility separationsmass spectrometrymultiple reaction monitoringselected reaction monitoringshotgun proteomicstargeted proteomicstranslational proteomics

Identifiers

PMID22943415
PMCPMC3580401

What OpenQuestion holds

Textmetadata
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.