Evidence map›Paper›PMID 38373465›Full record

ArticleBioorganic & medicinal chemistry letters2024

α-Amino bisphosphonate triazoles serve as GGDPS inhibitors.

Nathaniel R Gehrke, Dan Feng, Md Ayub Ali, Mona A Maalouf, Sarah A Holstein, David F Wiemer

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Synthesis of Amino-Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Article
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

6 authors at 3 institutions in 2 countries.

Nathaniel R GehrkeDepartment of Chemistry, University of Iowa, Iowa City, IA 52242-1294, US.
Dan FengDepartment of Internal Medicine, University of Nebraska Medical Center, Omaha, NE 68198, US.
Md Ayub AliDepartment of Chemistry, University of Iowa, Iowa City, IA 52242-1294, US; Department of Chemistry, Bangladesh University of Engineering and Technology (BUET), Dhaka-1000, Bangladesh.
Mona A MaaloufDepartment of Chemistry, University of Iowa, Iowa City, IA 52242-1294, US.
Sarah A HolsteinDepartment of Internal Medicine, University of Nebraska Medical Center, Omaha, NE 68198, US; Fred and Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, NE, 68198, US.
David F WiemerDepartment of Chemistry, University of Iowa, Iowa City, IA 52242-1294, US; Department of Pharmacology, University of Iowa, Iowa City, IA 52242-1109, US. Electronic address: david-wiemer@uiowa.edu.
University of Iowa · USUniversity of Nebraska Medical Center · USBangladesh University of Engineering and Technology · BD

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI James Eudy · 1985 to 2026
$55.0M
Geranylgeranyl diphosphate synthase inhibitor therapy for multiple myelomaR01CA258621 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI HOLSTEIN, SARAH A, MOHS, AARON M. · 2021 to 2025
$2.5M
NCI NIH HHS P30 CA036727NCI NIH HHS R01 CA258621
6 · The paper itself

Abstract

Depletion of cellular levels of geranylgeranyl diphosphate by inhibition of the enzyme geranylgeranyl diphosphate synthase (GGDPS) is a potential strategy for disruption of protein transport by limiting the geranylgeranylation of the Rab proteins that regulate intracellular trafficking. As such, there is interest in the development of GGDPS inhibitors for the treatment of malignancies characterized by abnormal protein production, including multiple myeloma. Our previous work has explored the structure-function relationship of a series of isoprenoid triazole bisphosphonate-based GGDPS inhibitors, with modifications having impact on enzymatic, cellular and in vivo activities. We have synthesized a new series of α-amino bisphosphonates to understand the impact of modifying the alpha position with a moiety that is potentially linkable to other agents. Bioassays evaluating the enzymatic and cellular activities of these compounds demonstrate that incorporation of the α-amino group affords compounds with GGDPS inhibitory activity which is modulated by isoprenoid tail chain length and olefin stereochemistry. These studies provide further insight into the complexity of the structure-function relationship and will enable future efforts focused on tumor-specific drug delivery.

Indexed as

DiphosphonatesEnzyme InhibitorsFarnesyltranstransferaseTerpenesTriazolesDiphosphonatesEnzyme InhibitorsFarnesyltranstransferaseTerpenesTriazolesGGDP synthaseinhibitionisoprenoid biosynthesistriazole, amino bisphosphonates

Identifiers

PMID38373465
PMCPMC10981527
OpenAlexW4391900127

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.