Evidence map›Paper›PMID 38617281›Full record

ArticlebioRxiv : the preprint server for biology2024

Chemoproteomic profiling of substrate specificity in gut microbiota-associated bile salt hydrolases.

Lin Han, Augustus Pendleton, Adarsh Singh, Raymond Xu, Samantha A Scott, Jaymee A Palma, Peter Diebold, Kien P Malarney, Ilana L Brito, Pamela V Chang

Open access · greenAbstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Lin HanDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.
Augustus PendletonDepartment of Microbiology, Cornell University, Ithaca, NY 14853.
Adarsh SinghMeinig School of Biomedical Engineering, Cornell University, Ithaca, NY 14853.
Raymond XuDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853.
Samantha A ScottDepartment of Microbiology and Immunology, Cornell University, Ithaca, NY 14853.
Jaymee A PalmaSmith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY 14853.
Peter DieboldDepartment of Microbiology, Cornell University, Ithaca, NY 14853.
Kien P MalarneyDepartment of Microbiology, Cornell University, Ithaca, NY 14853.
Ilana L BritoMeinig School of Biomedical Engineering, Cornell University, Ithaca, NY 14853.
Pamela V ChangDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853.ORCID 0000-0003-3819-9994
Cornell University · US

Funding

Activity-based protein profiling of gut microbiota-associated bile acid metabolismR35GM133501 · NIGMS · CORNELL UNIVERSITY · PI Pamela Vivian Chang · 2019 to 2026
$2.8M
Acquisition of a Hybrid Quadrupole Time of Flight LC-MS/MS System for the CornellS10OD017992 · OD · CORNELL UNIVERSITY · PI ZHANG, SHENG · 2014 to 2014
$600k
NIGMS NIH HHS R35 GM133501NIH HHS S10 OD017992
6 · The paper itself

Abstract

The gut microbiome possesses numerous biochemical enzymes that biosynthesize metabolites that impact human health. Bile acids comprise a diverse collection of metabolites that have important roles in metabolism and immunity. The gut microbiota-associated enzyme that is responsible for the gateway reaction in bile acid metabolism is bile salt hydrolase (BSH), which controls the host's overall bile acid pool. Despite the critical role of these enzymes, the ability to profile their activities and substrate preferences remains challenging due to the complexity of the gut microbiota, whose metaproteome includes an immense diversity of protein classes. Using a systems biochemistry approach employing activity-based probes, we have identified gut microbiota-associated BSHs that exhibit distinct substrate preferences, revealing that different microbes contribute to the diversity of the host bile acid pool. We envision that this chemoproteomic approach will reveal how secondary bile acid metabolism controlled by BSHs contributes to the etiology of various inflammatory diseases.

Indexed as

bile acidsbile salt hydrolasechemoproteomicsclick chemistryGut microbiome

Identifiers

PMID38617281
PMCPMC11014516
OpenAlexW4393452399

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.