Evidence map›Paper›PMID 27306313›Full record

ReviewAnnual review of analytical chemistry (Palo Alto, Calif.)2016

Progress in Top-Down Proteomics and the Analysis of Proteoforms.

Timothy K Toby, Luca Fornelli, Neil L Kelleher

Abstract readReview
In one paragraph

Review in Annual review of analytical chemistry (Palo Alto, Calif.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 299 papers.

0numbers the graph read from it
0cells of the map it votes in
299citing papers in PubMed
–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

299 citing papers in PubMed.

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  13. Probing Proteoform Heterogeneity From Single Human Oocytes.Molecular & cellular proteomics : MCP · 2026
    Article
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239 more citing papers are in PubMed but not listed here.

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

3 authors.

Timothy K TobyDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208; email: n-kelleher@northwestern.edu.
Luca FornelliDepartment of Chemistry, Northwestern University, Evanston, Illinois 60208.
Neil L KelleherDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208; email: n-kelleher@northwestern.edu.

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Eukaryotic Post-Translational ModificationsR01GM067193 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KELLEHER, NEIL L · 2003 to 2015
$4.0M
Chemistry of Life Processes Predoctoral Training ProgramT32GM105538 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2013 to 2022
$2.7M
NCI NIH HHS P30 CA060553NIGMS NIH HHS P41 GM108569NIGMS NIH HHS R01 GM067193NIGMS NIH HHS T32 GM105538
6 · The paper itself

Abstract

From a molecular perspective, enactors of function in biology are intact proteins that can be variably modified at the genetic, transcriptional, or post-translational level. Over the past 30 years, mass spectrometry (MS) has become a powerful method for the analysis of proteomes. Prevailing bottom-up proteomics operates at the level of the peptide, leading to issues with protein inference, connectivity, and incomplete sequence/modification information. Top-down proteomics (TDP), alternatively, applies MS at the proteoform level to analyze intact proteins with diverse sources of intramolecular complexity preserved during analysis. Fortunately, advances in prefractionation workflows, MS instrumentation, and dissociation methods for whole-protein ions have helped TDP emerge as an accessible and potentially disruptive modality with increasingly translational value. In this review, we discuss technical and conceptual advances in TDP, along with the growing power of proteoform-resolved measurements in clinical and translational research.

Indexed as

ProteomicsAnimalsHumansMass SpectrometryProteinsProteinsintact protein analysismass spectrometryproteoformstop-down proteomicstranslational proteomics

Identifiers

PMID27306313
PMCPMC5373801

What OpenQuestion holds

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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.