Evidence map›Paper›PMID 30222357›Full record

ReviewJournal of proteome research2018

Proteome-Wide Structural Biology: An Emerging Field for the Structural Analysis of Proteins on the Proteomic Scale.

Upneet Kaur, He Meng, Fang Lui, Renze Ma, Ryenne N Ogburn, Julia H R Johnson, Michael C Fitzgerald, Lisa M Jones

Abstract readReview
In one paragraph

Review in Journal of proteome research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing 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

43 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Target Engagement Assays in Early Drug Discovery.Journal of medicinal chemistry · 2025
    Review
  8. Analysis of Limited Proteolysis-Coupled Mass Spectrometry Data.Molecular & cellular proteomics : MCP · 2025
    Article
  9. Article
  10. Review
  11. G-Computational and structural biotechnology journal · 2024
    Article
  12. Factors affecting protein recovery during Hsp40 affinity profiling.Analytical and bioanalytical chemistry · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. CJournal of proteome research · 2023
    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

8 authors.

Upneet KaurDepartment of Pharmaceutical Sciences , University of Maryland , Baltimore , Maryland 21201 , United States.
He MengDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0346 , United States.
Fang Lui
Renze MaDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0346 , United States.
Ryenne N OgburnDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0346 , United States.
Julia H R JohnsonDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0346 , United States.
Michael C FitzgeraldDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0346 , United States.ORCID 0000-0002-6719-4722
Lisa M JonesDepartment of Pharmaceutical Sciences , University of Maryland , Baltimore , Maryland 21201 , United States.ORCID 0000-0001-8825-060X

Funding

Analysis of Protein-Ligand Binding on the Proteomic ScaleR01GM084174 · NIGMS · DUKE UNIVERSITY · PI FITZGERALD, MICHAEL C · 2009 to 2017
$2.6M
NIGMS NIH HHS R01 GM084174
6 · The paper itself

Abstract

Over the past decade, a suite of new mass-spectrometry-based proteomics methods has been developed that now enables the conformational properties of proteins and protein-ligand complexes to be studied in complex biological mixtures, from cell lysates to intact cells. Highlighted here are seven of the techniques in this new toolbox. These techniques include chemical cross-linking (XL-MS), hydroxyl radical footprinting (HRF), Drug Affinity Responsive Target Stability (DARTS), Limited Proteolysis (LiP), Pulse Proteolysis (PP), Stability of Proteins from Rates of Oxidation (SPROX), and Thermal Proteome Profiling (TPP). The above techniques all rely on conventional bottom-up proteomics strategies for peptide sequencing and protein identification. However, they have required the development of unconventional proteomic data analysis strategies. Discussed here are the current technical challenges associated with these different data analysis strategies as well as the relative analytical capabilities of the different techniques. The new biophysical capabilities that the above techniques bring to bear on proteomic research are also highlighted in the context of several different application areas in which these techniques have been used, including the study of protein ligand binding interactions (e.g., protein target discovery studies and protein interaction network analyses) and the characterization of biological states.

Indexed as

Protein Processing, Post-TranslationalAnimalsCross-Linking ReagentsDatabases, ProteinDeuterium Exchange MeasurementHumansIsotope LabelingLigandsMass SpectrometryProtein BindingProtein FoldingProteinsProtein StabilityProteolysisProteomeProteomicsCross-Linking ReagentsLigandsProteinsProteomemass spectrometryprotein foldingproteomicsthermodynamics

Identifiers

PMID30222357
PMCPMC6524533

What OpenQuestion holds

Textmetadata
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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.