PreprintCited by 28Advanced Proteomics Techniques and ApplicationsHeat shock proteins researchUbiquitin and proteasome pathways

Temperature sensitive Mutant Proteome Profiling: a novel tool for the characterization of the global impact of missense mutations on the proteome

Open access
Peck Justice, Sarah A., Qi, Guihong, Wijeratne, H. R. Sagara, Victorino, José F., Simpson, Ed R., Wijeratne, Aruna B., Mosley, Amber L.·2019·Journal of Biological Chemistry

Preprint — published as 10.1074/jbc.ra120.014576 · Paper page

Abstract

Temperature sensitive (TS) mutants have been foundational in the characterization of essential genes. However, a high-throughput workflow for characterization of biophysical changes in TS mutants is lacking. Te mperature sensitive M utant P roteome P rofiling (TeMPP) is a novel application of mass spectrometry (MS) based thermal proteome profiling (TPP) to characterize effects of missense mutations on protein stability and PPIs. This study characterizes missense mutations in two different subunits of the 26S proteasome on the thermal stability of the proteome at large, revealing distinct mechanistic details that were not obtained using only steady-state transcriptome and proteome analyses. TeMPP is a precise approach to measure changes in missense mutant containing proteomes without the requirement for large amounts of starting material, specific antibodies against proteins of interest, and/or genetic manipulation of the biological system. Overall, TeMPP provides unique mechanistic insights into missense mutation dysfunction and connection of genotype to phenotype in a rapid, non-biased fashion.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1101/2019.12.30.891267

Cites

154 of 154 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

2 of the 156 references couldn’t be matched to a known paper.

Cited by

Sorted by citations

Authors
Peck Justice, S. A., Qi, G., Wijeratne, H. R. S., Victorino, J. F., Simpson, E. R., Wijeratne, A. B., & Mosley, A. L.
Affiliations
Indiana University Indianapolis (US)
Corresponding author
  • Wijeratne, Aruna B.
  • Mosley, Amber L.
Venue
Journal of Biological Chemistry
Publisher
openRxiv
Published
2019-12-30
Volume
295
Issue
48
Pages
16219-16238
ISSN
0021-9258 (ISSN-L)
OpenAlex
W3082270748
Cited by
28
References
156
Citations by year
2025: 4 · 2024: 6 · 2023: 3 · 2022: 6 · 2021: 7 · 2020: 2
FWCI
1.72
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • IUScholarWorks (Indiana University) (submittedVersion, cc-by)
Funders
  • Eli Lilly and Company
  • Indiana Clinical and Translational Sciences Institute (UL1TR002529)
  • Lilly Endowment
  • Ralph W. and Grace M. Showalter Research Trust Fund
  • Thermo Fisher Scientific
  • National Institutes of Health (UL1TR002529, HL007910)
  • School of Medicine, Indiana University (UL1TR002529)
  • National Heart, Lung, and Blood Institute (HL007910, T32HL007910)
  • National Institute of General Medical Sciences (R01GM099714)
  • National Center for Advancing Translational Sciences
Topics
  • Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
missense mutations, temperature sensitivity, 26S proteasome, proteasome subunits, protein stability, genotype-phenotype correlation
MeSH terms
RNA-Seq, Saccharomyces cerevisiae, Temperature, Mutation, Missense, Proteome, Saccharomyces cerevisiae Proteins, Proteasome Endopeptidase Complex

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review