Mass spectrometry searches using MASST
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MASST revealed that a metabolite differentially expressed in two cohorts of mice is also differentially expressed in healthy and non-alcoholic fatty liver disease in humans, even without knowing the molecule's chemical structure.
“The authors demonstrated an example of a metabolite differentially expressed within two cohorts of mice and utilized MASST to reveal that this metabolite is also differentially expressed in healthy and non-alcoholic fatty liver disease in humans – even without knowing the molecule's chemical structure.”
From Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products (2024) · cites this paper as [155]
The main text says MASST can search public MS/MS data for unknown or unannotated molecules and suggests translating findings from model organisms to humans (page unavailable). It does not describe the claimed example of a metabolite differentially expressed in two mouse cohorts and in healthy versus non-alcoholic fatty liver disease human groups. (LLM, conf=0.78)
Experimental — accuracy not yet measuredThe Mass Spectrometry Search Tool (MASST) can be utilized to add context to molecules detected in a bioactivity experiment.
“The Mass Spectrometry Search Tool (MASST)155 can be utilized to add context to molecules detected in a bioactivity experiment.”
From Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products (2024) · cites this paper as [155]
MASST finds all occurrences of a query MS/MS spectrum across all public metabolomics experiments.
“The MASST tool finds all occurrences of a query MS/MS spectrum across all public metabolomics experiments.”
From Connecting metabolome and phenotype: recent advances in functional metabolomics tools for the identification of bioactive natural products (2024) · cites this paper as [155]
The bacterial enzymes responsible for producing amino acid bile acid amidates are unknown.
“The enzymes responsible for these conjugation reactions are unknown.”
From Bile Acids Are Substrates for Amine N-Acyl Transferase Activity by Bile Salt Hydrolase (2022) · cites this paper as [17]
The paper’s main text describes MASST as a tool for searching mass-spectrometry data; it does not address which enzymes produce amino acid bile acid amidates. Searches for the conjugation reactions, bile acids, and their bacterial enzymes found no relevant passage in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredRecent studies demonstrated that bacteria have bile acid amine N-acyltransferase activity, with dozens of bacterially conjugated amino acid amidates identified.
“Recent studies demonstrated that bacteria, in addition to the host, have bile acid amine N-acyltransferase activity, with dozens of bacterially conjugated amino acid amidates identified1–4,6,17.”
From Bile Acids Are Substrates for Amine N-Acyl Transferase Activity by Bile Salt Hydrolase (2022) · cites this paper as [17]
The main text describes MASST searches of public mass-spectrometry data, not bacterial bile-acid conjugation. Searches for bile acids, amine N-acyltransferase activity, and amino-acid amidates found no passage addressing the claimed activity or the identification of dozens of amidates. (LLM, conf=0.75)
Experimental — accuracy not yet measured
Characterization data for all MCBAs are consistent with reported data.
“All MCBAs were purified according to literature precedent and characterization data are consistent with reported data31,33,42,77,78.”
From Bile salt hydrolases shape the bile acid landscape and restrict Clostridioides difficile growth in the murine gut (2023) · cites this paper as [42]
The paper’s main text (page not provided) describes MASST searches and spectral matching, not the purification or characterization of MCBAs. Searches for “MCBAs,” “purified according to literature precedent,” and characterization data found no passage addressing the claim. (LLM, conf=0.77)
Experimental — accuracy not yet measured
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Nematode-Trapping Fungi Produce Diverse Metabolites during Predator–Prey Interaction
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- Authors
- Wang, M., Jarmusch, A. K., Vargas, F., Aksenov, A. A., Gauglitz, J. M., Weldon, K., Petras, D., da Silva, R., Quinn, R., Melnik, A. V., van der Hooft, J. J. J., Caraballo-Rodríguez, A. M., Nothias, L. F., Aceves, C. M., Panitchpakdi, M., Brown, E., Di Ottavio, F., Sikora, N., Elijah, E. O., Labarta-Bajo, L., Gentry, E. C., Shalapour, S., Kyle, K. E., Puckett, S. P., Watrous, J. D., Carpenter, C. S., Bouslimani, A., Ernst, M., Swafford, A. D., Zúñiga, E. I., Balunas, M. J., Klassen, J. L., Loomba, R., Knight, R., Bandeira, N., & Dorrestein, P. C.
- Affiliations
- University of California San Diego (US)
- University of Connecticut (US)
- Corresponding author
- Dorrestein, Pieter C.
- ORCID
- Wang, Mingxun
- Jarmusch, Alan K.
- Vargas, Fernando
- Aksenov, Alexander A.
- Gauglitz, Julia M.
- Weldon, Kelly
- Petras, Daniel
- Quinn, Robert
- Melnik, Alexey V.
- van der Hooft, Justin J. J.
- Caraballo-Rodríguez, Andrés Mauricio
- Aceves, Christine M.
- Panitchpakdi, Morgan
- Brown, Elizabeth
- Sikora, Nicole
- Labarta-Bajo, Lara
- Gentry, Emily C.
- Shalapour, Shabnam
- Kyle, Kathleen E.
- Puckett, Sara P.
- Watrous, Jeramie D.
- Carpenter, Carolina S.
- Bouslimani, Amina
- Ernst, Madeleine
- Swafford, Austin D.
- Zúñiga, Elina I.
- Balunas, Marcy J.
- Klassen, Jonathan L.
- Loomba, Rohit
- Knight, Rob
- Bandeira, Nuno
- Dorrestein, Pieter C.
- Venue
- Nature Biotechnology
- Published
- 2020-01
- Volume
- 38
- Issue
- 1
- Pages
- 23-26
- ISSN
- 0733-222X (ISSN-L)
- 1087-0156
- 1546-1696
- PMC
- PMC7236533
- OpenAlex
- W2997345427
- Cited by
- 281
- References
- 26
- Citations by year
- 2026: 40 · 2025: 45 · 2024: 57 · 2023: 43 · 2022: 27 · 2021: 39 · 2020: 29 · 2019: 1
- FWCI
- 11.19
- Type
- journal article
- Language
- en
- Open access
- green
- research.wur.nl
- Licence
- public-domain
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
- Locations
- Nature Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Socio-Environmental Systems Modeling (acceptedVersion, public-domain)
- PubMed Central (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- Netherlands eScience Center ASDI eScience grant
- Gordon and Betty Moore Foundation (GBMF7622)
- Alfred P. Sloan Foundation (N/A)
- U.S. Department of Health & Human Services | National Institutes of Health (CA211211, P41 GM103484)
- United States Department of Defense | United States Navy | Office of Naval Research (N00014-15-1-2809)
- United States Department of Justice | National Institute of Justice (2015-DN-BX-K047)
- National Science Foundation (IOS-1656475)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolomics and Mass Spectrometry Studies
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- spectral library search, metabolite annotation, unknown metabolites, cold pressor test, multi-omics, metabolic networks, medicinal plants, traditional East Asian medicine
- MeSH terms
- Algorithms, Mass Spectrometry, Reproducibility of Results, Knowledge Bases, Search Engine
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