Evidence map›Paper›PMID 22393405›Full record

ArticlePloS one2012

Raman spectroscopy provides a powerful diagnostic tool for accurate determination of albumin glycation.

Narahara Chari Dingari, Gary L Horowitz, Jeon Woong Kang, Ramachandra R Dasari, Ishan Barman

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

42 citing papers in PubMed, 164 citations in OpenAlex.

  1. Review
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  4. Protein-functionalized and intrinsically radiolabeled [European journal of nuclear medicine and molecular imaging · 2025
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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

5 authors at 2 institutions in 1 country.

Narahara Chari DingariLaser Biomedical Research Center, G. R. Harrison Spectroscopy Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts, United States of America.
Gary L Horowitz
Jeon Woong Kang
Ramachandra R Dasari
Ishan Barman
Massachusetts Institute of Technology · USHarvard University · US

Funding

WIDE-FIELD REFLECTION PHASE MICROSCOPYP41RR002594 · NCRR · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI KONG, CHULHO · 1985 to 2011
$12.3M
NCRR NIH HHS P41 RR002594NCRR NIH HHS P41-RR02594
6 · The paper itself

Abstract

We present the first demonstration of glycated albumin detection and quantification using Raman spectroscopy without the addition of reagents. Glycated albumin is an important marker for monitoring the long-term glycemic history of diabetics, especially as its concentrations, in contrast to glycated hemoglobin levels, are unaffected by changes in erythrocyte life times. Clinically, glycated albumin concentrations show a strong correlation with the development of serious diabetes complications including nephropathy and retinopathy. In this article, we propose and evaluate the efficacy of Raman spectroscopy for determination of this important analyte. By utilizing the pre-concentration obtained through drop-coating deposition, we show that glycation of albumin leads to subtle, but consistent, changes in vibrational features, which with the help of multivariate classification techniques can be used to discriminate glycated albumin from the unglycated variant with 100% accuracy. Moreover, we demonstrate that the calibration model developed on the glycated albumin spectral dataset shows high predictive power, even at substantially lower concentrations than those typically encountered in clinical practice. In fact, the limit of detection for glycated albumin measurements is calculated to be approximately four times lower than its minimum physiological concentration. Importantly, in relation to the existing detection methods for glycated albumin, the proposed method is also completely reagent-free, requires barely any sample preparation and has the potential for simultaneous determination of glycated hemoglobin levels as well. Given these key advantages, we believe that the proposed approach can provide a uniquely powerful tool for quantification of glycation status of proteins in biopharmaceutical development as well as for glycemic marker determination in routine clinical diagnostics in the future.

Indexed as

AlbuminsBlood GlucoseDiabetes ComplicationsDiabetes MellitusGlycated HemoglobinGlycated Serum AlbuminGlycation End Products, AdvancedGlycosylationHemoglobinsHumansModels, StatisticalMultivariate AnalysisPrincipal Component AnalysisRegression AnalysisReproducibility of ResultsSerum AlbuminAlbuminsBlood GlucoseGlycated HemoglobinGlycated Serum AlbuminGlycation End Products, AdvancedHemoglobinsSerum Albumin

Identifiers

PMID22393405
PMCPMC3290592
OpenAlexW2024895662

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.