Evidence map›Paper›PMID 35525545›Full record

ArticleMethods in enzymology2022

Dynamics of protein kinases and pseudokinases by HDX-MS.

Joshua B Sheetz, Mark A Lemmon, Yuko Tsutsui

Abstract read
In one paragraph

Article in Methods in enzymology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Modulating pseudokinase conformation from the ATP-binding site.Structure (London, England : 1993) · 2026
    Article
  2. Tyrosine kinases sample unique activation ensembles.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Isoform-specific C-terminal phosphorylation drives autoinhibition of Casein kinase 1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Exploring the conformational landscape of protein kinases.Current opinion in structural biology · 2024
    Review
  8. Article
  9. Fundamentals of HDX-MS.Essays in biochemistry · 2023
    Review
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.

Joshua B SheetzDepartment of Pharmacology and Yale Cancer Biology Institute, Yale University School of Medicine, West Haven, CT, United States.
Mark A LemmonDepartment of Pharmacology and Yale Cancer Biology Institute, Yale University School of Medicine, West Haven, CT, United States. Electronic address: mark.lemmon@yale.edu.
Yuko TsutsuiDepartment of Pharmacology and Yale Cancer Biology Institute, Yale University School of Medicine, West Haven, CT, United States. Electronic address: yuko.tsutsui@yale.edu.

Funding

Understanding Signaling by Non-Canonical Receptor Tyrosine KinasesR35GM122485 · NIGMS · YALE UNIVERSITY · PI Mark A Lemmon · 2017 to 2026
$7.9M
Targeting differential kinase domain dimerization of EGFR mutantsR03CA259881 · NCI · YALE UNIVERSITY · PI TSUTSUI, YUKO · 2021 to 2021
$168k
NCI NIH HHS R03 CA259881NIGMS NIH HHS R35 GM122485
6 · The paper itself

Abstract

Dynamics of the protein kinase fold are deeply intertwined with its structure. The past three decades of kinase biophysical studies revealed key dynamic features of the kinase domain and, more recently, how these features may endow catalytically impaired kinases-or pseudokinases-with signaling properties. Hydrogen-deuterium exchange coupled with mass spectrometry (HDX-MS) is proving to be a valuable approach for studies of kinase and pseudokinase domain dynamics. Here, we briefly discuss the methods that have provided insights into protein kinase dynamics, describe how HDX-MS is being used to answer questions in the kinase/pseudokinase field, and provide a detailed protocol for collecting an HDX-MS dataset to study the impacts of small molecule binding to a pseudokinase domain. As more small molecules are discovered that can disrupt pseudokinase conformations, HDX-MS is likely to be a powerful approach for exploring drug-induced changes in pseudokinase dynamics and structure.

Indexed as

Deuterium Exchange MeasurementHydrogen Deuterium Exchange-Mass SpectrometryMass SpectrometryProtein ConformationProtein KinasesProtein KinasesAllosteryConformationDrug discoveryHydrogen-deuterium exchangeStructural mass spectrometry

Identifiers

PMID35525545
PMCPMC9148214

What Socratic 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 Socratic graph.