Evidence map›Paper›PMID 37681210›Full record

ArticleMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents2023

Development of convenient crystallization inhibition assays for structure-activity relationship studies in the discovery of crystallization inhibitors.

Jeffrey Yang, Haifa Albanyan, Yiling Wang, Yanhui Yang, Amrik Sahota, Longqin Hu

Open access · greenAbstract read
In one paragraph

Article in Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

5 citing papers in PubMed, 5 citations in OpenAlex.

  1. Systematic evaluation and comparison of theCurrent research in food science · 2026
    Article
  2. Article
  3. Structure-activity relationships and pharmacokinetic evaluation of L-cystine diamides as L-cystine crystallization inhibitors for cystinuria.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents · 2024
    Article
  4. Article
  5. 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 1 institution in 1 country.

Jeffrey YangDepartment of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States.ORCID 0000-0002-5647-1464
Haifa AlbanyanDepartment of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States.
Yiling WangDepartment of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States.ORCID 0000-0002-0693-3480
Yanhui YangDepartment of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States.
Amrik SahotaDepartment of Genetics, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States.ORCID 0000-0002-3603-673X
Longqin HuDepartment of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854, United States.ORCID 0000-0002-1799-5652
Rutgers, The State University of New Jersey · US

Funding

L-Cystine Diamides as Inhibitors of L-Cystine Stone Formation in CystinuriaR01DK112782 · NIDDK · RUTGERS, THE STATE UNIV OF N.J. · PI HU, LONGQIN, SAHOTA, AMRIK · 2017 to 2021
$2.9M
NIDDK NIH HHS R01 DK112782
6 · The paper itself

Abstract

Kidney stone diseases are increasing globally in prevalence and recurrence rates, indicating an urgent medical need for developing new therapies that can prevent stone formation. One approach we have been working on is to develop small molecule inhibitors that can interfere with the crystallization process of the chemical substances that form the stones. For these drug discovery efforts, it is critical to have available easily accessible assay methods to evaluate the potential inhibitors and rank them for structure-activity relationship studies. Herein, we report a convenient, medium-to-high throughput assay platform using, as an example, the screening and evaluation of inhibitors of

Indexed as

Crystallization inhibition assayCrystallization inhibitorsCystinuriaKidney stone diseaseL-CystineUrolithiasis

Identifiers

PMID37681210
PMCPMC10482073
OpenAlexW4366758004

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.