Evidence map›Paper›PMID 38293009›Full record

ArticlebioRxiv : the preprint server for biology2024

Drugs Form Ternary Complexes with Human Liver Fatty Acid Binding Protein (FABP1) and FABP1 Binding Alters Drug Metabolism.

King Clyde B Yabut, Alice Martynova, Abhinav Nath, Benjamin P Zercher, Matthew F Bush, Nina Isoherranen

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
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

6 authors at 1 institution in 1 country.

King Clyde B YabutDepartment of Pharmaceutics, School of Pharmacy, University of Washington, Seattle, WA, United States.
Alice MartynovaDepartment of Chemistry, University of Washington, Seattle, WA, United States.
Abhinav NathDepartment of Medicinal Chemistry, University of Washington, Seattle, WA.
Benjamin P ZercherDepartment of Chemistry, University of Washington, Seattle, WA, United States.
Matthew F BushDepartment of Chemistry, University of Washington, Seattle, WA, United States.
Nina IsoherranenDepartment of Pharmaceutics, School of Pharmacy, University of Washington, Seattle, WA, United States.ORCID 0000-0002-9548-3126
University of Washington · US

Funding

Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Understanding Fetal Exposure to Cannabinoids Through In Vitro and In Vivo StudiesP01DA032507 · NIDA · UNIVERSITY OF WASHINGTON · PI UNADKAT, JASHVANT D · 2013 to 2023
$12.4M
Mechanisms of Brain Dysmorphology in MN1 C-Terminal Truncation Syndrome, a Novel Intellectual Developmental Disability Disorder P50HD103524 · NICHD · UNIVERSITY OF WASHINGTON · PI DANIEL DOHERTY · 2020 to 2026
$9.9M
NICHD NIH HHS P50 HD103524NIDA NIH HHS P01 DA032507NIGMS NIH HHS T32 GM007750
6 · The paper itself

Abstract

Liver fatty acid binding protein (FABP1) binds diverse endogenous lipids and is highly expressed in the human liver. Binding to FABP1 alters the metabolism and homeostasis of endogenous lipids in the liver. Drugs have also been shown to bind to rat FABP1, but limited data is available for human FABP1 (hFABP1). FABP1 has a large binding pocket and multiple fatty acids can bind to FABP1 simultaneously. We hypothesized that drug binding to hFABP1 results in formation of ternary complexes and that FABP1 binding alters drug metabolism. To test these hypotheses native protein mass spectrometry (MS) and fluorescent 11-(dansylamino)undecanoic acid (DAUDA) displacement assays were used to characterize drug binding to hFABP1 and diclofenac oxidation by cytochrome P450 2C9 (CYP2C9) was studied in the presence and absence of hFABP1. DAUDA binding to hFABP1 involved high (K

Indexed as

fatty acid binding proteinsfluorescence displacementligand bindingprotein-membrane interactionsprotein-protein interactions

Identifiers

PMID38293009
PMCPMC10827205
OpenAlexW4391045699

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.