Evidence map›Paper›PMID 29510250›Full record

ArticleMethods (San Diego, Calif.)2018

Characterization of solution-phase drug-protein interactions by ultrafast affinity extraction.

Sandya R Beeram, Xiwei Zheng, Kyungah Suh, David S Hage

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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 · 2022
    Article
  5. Evaluation of microcolumn stability in ultrafast affinity extraction for binding and rate studies.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Affinity chromatography: A review of trends and developments over the past 50 years.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020
    Review
  10. Review
  11. Kinetic Analysis by Affinity Chromatography.Frontiers in chemistry · 2019
    Review
  12. 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

4 authors at 1 institution in 1 country.

Sandya R BeeramDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
Xiwei ZhengDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
Kyungah SuhDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.
David S HageDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA. Electronic address: dhage1@unl.edu.
University of Nebraska–Lincoln · US

Funding

CHROMATOGRAPHIC AUTOMATION OF IMMUNOASSAYSR01GM044931 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 1998 to 2014
$2.7M
CHROMATOGRAPHIC STUDIES OF FUNCTIONAL PROTEOMICSR01DK069629 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI HAGE, DAVID S · 2006 to 2017
$1.8M
NIDDK NIH HHS R01 DK069629NIGMS NIH HHS R01 GM044931
6 · The paper itself

Abstract

A number of tools based on high-performance affinity separations have been developed for studying drug-protein interactions. An example of one recent approach is ultrafast affinity extraction. This method has been employed to examine the free (or non-bound) fractions of drugs and other solutes in simple or complex samples that contain soluble binding agents. These free fractions have also been used to determine the binding constants and rate constants for the interactions of drugs with these soluble agents. This report describes the general principles of ultrafast affinity extraction and the experimental conditions under which it can be used to characterize such interactions. This method will be illustrated by utilizing data that have been obtained when using this approach to measure the binding and dissociation of various drugs with the serum transport proteins human serum albumin and alpha

Indexed as

Blood ProteinsChromatography, AffinityHumansKineticsPharmaceutical PreparationsProtein BindingSerum AlbuminBlood ProteinsPharmaceutical PreparationsSerum AlbuminAffinity microcolumnAlpha(1)-acid glycoproteinDrug-protein interactionsHigh performance affinity chromatographyHuman serum albuminUltrafast affinity extraction

Identifiers

PMID29510250
PMCPMC6098730
OpenAlexW2789796737

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.