ArticleJournal of pharmaceutical and biomedical analysis2021
High-Performance affinity chromatographic studies of repaglinide and nateglinide interactions with normal and glyoxal- or methylglyoxal-modified human albumin serum.
Article in Journal of pharmaceutical and biomedical analysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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.
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.
Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Gaining Insights Into the Formation of the Cathepsin B Inhibitor II-Human Serum Albumin Complex: A Multidisciplinary Approach.Luminescence : the journal of biological and chemical luminescence · 2026Article
- Microscale Affinity Chromatography for Biointeraction Analysis: Strategies, Principles and Applications.Journal of separation science · 2026Review
- Characterization of binding by sulfonylureas with normal or modified human serum albumin using affinity microcolumns prepared by entrapment.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2023Article
- Characterization of binding by repaglinide and nateglinide with glycated human serum albumin using high-performance affinity microcolumns.Journal of separation science · 2022Article
- Analysis of the binding of warfarin to glyoxal- and methylglyoxal-modified human serum albumin by ultrafast affinity extraction.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2022Article
- Structural Analysis of Human Serum Albumin in Complex with the Fibrate Drug Gemfibrozil.International journal of molecular sciences · 2022Article
- [Advances in chromatography in the study of drug-plasma protein interactions].Se pu = Chinese journal of chromatography · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
During diabetes human serum albumin (HSA), an important drug transport protein, can be modified by agents such as glyoxal (Go) and methylglyoxal (MGo) to form advanced glycation end-products. High-performance affinity microcolumns and zonal elution competition studies were used to compare interactions by the anti-diabetic drugs repaglinide and nateglinide with normal and Go- or MGo-modified HSA at Sudlow sites I and II of this protein. Both drugs had their strongest binding at Sudlow site II for the normal and modified forms of HSA. The association equilibrium constants at this site for repaglinide and nateglinide with normal HSA were 6.1 (± 0.2) × 10
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.