Evidence map›Paper›PMID 36948708›Full record

ArticleMethods in enzymology2023

Multiplex substrate profiling by mass spectrometry for proteases.

Peter J Rohweder, Zhenze Jiang, Brianna M Hurysz, Anthony J O'Donoghue, Charles S Craik

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
14.0field-weighted citation impact, top 1% of its field
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

17 citing papers in PubMed, 24 citations in OpenAlex.

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  9. Enhancing schistosomiasis drug discovery approaches with optimized proteasome substrates.Protein science : a publication of the Protein Society · 2025
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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

5 authors at 3 institutions in 1 country.

Peter J RohwederDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, United States.
Zhenze JiangSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San Diego, CA, United States.
Brianna M HuryszSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San Diego, CA, United States.
Anthony J O'DonoghueSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, San Diego, CA, United States. Electronic address: ajodonoghue@health.ucsd.edu.
Charles S CraikDepartment of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA, United States. Electronic address: charles.craik@ucsf.edu.
University of California, San Francisco · USUniversity of Montana · USUniversity of California, San Diego · US

Funding

Targeting Viroporins and Coronavirus M ProteinU19AI171110 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI James Solomon Fraser · 2022 to 2026
$103.4M
GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Molecular control of cardiac regenerative potentialR01HL138456 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Guo Huang · 2018 to 2026
$5.1M
Proteasome inhibitors against mucosal protozoan pathogensR01AI158612 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ECKMANN, LARS, O'DONOGHUE, ANTHONY JOHN · 2021 to 2025
$3.2M
Research Training in Chemistry and Chemical BiologyT32GM145460 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Jason E Gestwicki · 2022 to 2026
$3.1M
Tumor-specific drug activation by pericellular proteasesR21CA256460 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI O'DONOGHUE, ANTHONY JOHN, OWEN, SHAWN C · 2022 to 2023
$409k
NCI NIH HHS R21 CA256460NIAID NIH HHS R01 AI158612NIAID NIH HHS U19 AI171110NIGMS NIH HHS T32 GM007752NIGMS NIH HHS T32 GM145460
6 · The paper itself

Abstract

Proteolysis is a central regulator of many biological pathways and the study of proteases has had a significant impact on our understanding of both native biology and disease. Proteases are key regulators of infectious disease and misregulated proteolysis in humans contributes to a variety of maladies, including cardiovascular disease, neurodegeneration, inflammatory diseases, and cancer. Central to understanding a protease's biological role, is characterizing its substrate specificity. This chapter will facilitate the characterization of individual proteases and complex, heterogeneous proteolytic mixtures and provide examples of the breadth of applications that leverage the characterization of misregulated proteolysis. Here we present the protocol of Multiplex Substrate Profiling by Mass Spectrometry (MSP-MS), a functional assay that quantitatively characterizes proteolysis using a synthetic library of physiochemically diverse, model peptide substrates, and mass spectrometry. We present a detailed protocol as well as examples of the use of MSP-MS for the study of disease states, for the development of diagnostic and prognostic tests, for the generation of tool compounds, and for the development of protease-targeted drugs.

Indexed as

Peptide HydrolasesProteomicsEndopeptidasesHumansMass SpectrometryProteolysisSubstrate SpecificityEndopeptidasesPeptide HydrolasesCancerDiagnosticsEnzymologyInfectious diseaseMass spectrometryPost-translational modifying enzymesPrognosticsProteasesSubstrate profiling

Identifiers

PMID36948708
PMCPMC10201391
OpenAlexW4312313284

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.