Evidence map›Paper›PMID 31384043›Full record

ArticleNature methods2019

High throughput discovery of functional protein modifications by Hotspot Thermal Profiling.

Jun X Huang, Gihoon Lee, Kate E Cavanaugh, Jae W Chang, Margaret L Gardel, Raymond E Moellering

Abstract read
In one paragraph

Article in Nature methods, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

65 citing papers in PubMed.

  1. Article
  2. AnFrontiers in chemistry · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Jun X HuangDepartment of Chemistry, The University of Chicago, Chicago, IL, USA.ORCID http://orcid.org/0000-0002-1318-8562
Gihoon LeeDepartment of Chemistry, The University of Chicago, Chicago, IL, USA.
Kate E CavanaughDepartment of Physics, The University of Chicago, Chicago, IL, USA.
Jae W ChangDepartment of Chemistry, The University of Chicago, Chicago, IL, USA.
Margaret L GardelDepartment of Physics, The University of Chicago, Chicago, IL, USA.
Raymond E MoelleringDepartment of Chemistry, The University of Chicago, Chicago, IL, USA. rmoellering@uchicago.edu.ORCID http://orcid.org/0000-0002-2043-7838

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Mechanical Regulation of Cell Adhesion by Dynamic Cytoskeletal Assemblies - Resubmission 01R01GM104032 · NIGMS · UNIVERSITY OF CHICAGO · PI GARDEL, MARGARET LISE · 2015 to 2023
$2.5M
Targeting Transcription with Synthetic BiologicsDP2GM128199 · NIGMS · UNIVERSITY OF CHICAGO · PI MOELLERING, RAYMOND E · 2017 to 2017
$2.3M
Mapping Protein Social Network Dynamics with Photoproximity Profiling PlatformsR01GM145852 · NIGMS · UNIVERSITY OF CHICAGO · PI MOELLERING, RAYMOND E · 2022 to 2025
$1.5M
Distribution, regulation and function of a novel lysine PTM in metabolic diseaseR00CA175399 · NCI · UNIVERSITY OF CHICAGO · PI MOELLERING, RAYMOND E · 2015 to 2017
$712k
NCI NIH HHS R00 CA175399NIGMS NIH HHS DP2 GM128199NIGMS NIH HHS R01 GM104032NIGMS NIH HHS R01 GM145852NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Mass spectrometry enables global analysis of posttranslationally modified proteoforms from biological samples, yet we still lack methods to systematically predict, or even prioritize, which modification sites may perturb protein function. Here we describe a proteomic method, Hotspot Thermal Profiling, to detect the effects of site-specific protein phosphorylation on the thermal stability of thousands of native proteins in live cells. This massively parallel biophysical assay unveiled shifts in overall protein stability in response to site-specific phosphorylation sites, as well as trends related to protein function and structure. This method can detect intrinsic changes to protein structure as well as extrinsic changes to protein-protein and protein-metabolite interactions resulting from phosphorylation. Finally, we show that functional 'hotspot' protein modification sites can be discovered and prioritized for study in a high-throughput and unbiased fashion. This approach is applicable to diverse organisms, cell types and posttranslational modifications.

Indexed as

Protein Processing, Post-TranslationalTemperatureHeLa CellsHigh-Throughput Screening AssaysHumansPhosphoproteinsPhosphorylationProtein Interaction Domains and MotifsProtein StabilityProteomePhosphoproteinsProteome

Identifiers

PMID31384043
PMCPMC7238970

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.