Advances in the measurement of vitamin D binding protein.

Karen W Phinney, Lisa E Kilpatrick

Abstract readReview

In one paragraph

Review in Analytical and bioanalytical chemistry, 2026. 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.

No citing paper in PubMed yet.

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

2 authors.

Karen W PhinneyBiomolecular Measurement Division, Material Measurement Laboratory, National Institute of Standards and Technology, Gaithersburg, MD, USA. karen.phinney@nist.gov.

Lisa E KilpatrickBiomolecular Measurement Division, Material Measurement Laboratory, National Institute of Standards and Technology, Gaithersburg, MD, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vitamin D binding protein (DBP) is a polymorphic protein known for its function in transporting vitamin D metabolites. DBP also plays several other important roles in the body's response to tissue damage and inflammation. Measurement of DBP is fundamental to understanding its relationship to vitamin D status and to elucidating potential links between DBP concentration and various health outcomes. Early studies on DBP primarily used antibody-based techniques for quantification, and mass spectrometry-based methods have been reported during the past decade. This review will outline the different methodologies used in DBP studies and to assign values to reference materials, describe their advantages and limitations, and highlight some future trends.

Indexed as

Immunoassays/ELISAMass spectrometryMetaboliteProtein quantificationReference materialsVitamin D

Identifiers

PMID42745028

DOI10.3390/ijms21217822

What OpenQuestion holds

Textmetadata

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.