Evidence map›Paper›PMID 23357359›Full record

ReviewBiochimica et biophysica acta2013

FTIR spectroscopic imaging of protein aggregation in living cells.

Lisa M Miller, Megan W Bourassa, Randy J Smith

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
21.5field-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

97 citing papers in PubMed, 366 citations in OpenAlex.

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  18. ACS applied polymer materials · 2025
    Article
  19. Regulatory Guidelines for the Analysis of Therapeutic Peptides and Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Review
  20. Protein Analysis by FT-IR/ATR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2025
    Article

37 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Lisa M MillerPhoton Sciences Directorate, Brookhaven National Laboratory, Upton, NY 11973, USA. lmiller@bnl.gov
Megan W Bourassa
Randy J Smith
Brookhaven National Laboratory · USStony Brook University · US

Funding

Synchrotron-Based Infrared Microscope for Chemical Imaging of DiseaseS10RR023782 · NCRR · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, LISA M · 2007 to 2007
$296k
NCRR NIH HHS RR23782NCRR NIH HHS S10 RR023782
6 · The paper itself

Abstract

Protein misfolding and aggregation are the hallmark of a number of diseases including Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, and the prion diseases. In all cases, a naturally-occurring protein misfolds and forms aggregates that are thought to disrupt cell function through a wide range of mechanisms that are yet to be fully unraveled. Fourier transform infrared (FTIR) spectroscopy is a technique that is sensitive to the secondary structure of proteins and has been widely used to investigate the process of misfolding and aggregate formation. This review focuses on how FTIR spectroscopy and spectroscopic microscopy are being used to evaluate the structural changes in disease-related proteins both in vitro and directly within cells and tissues. Finally, ongoing technological advances will be presented that are enabling time-resolved FTIR imaging of protein aggregation directly within living cells, which can provide insight into the structural intermediates, time scale, and mechanisms of cell toxicity associated with aggregate formation. This article is part of a Special Issue entitled: FTIR in membrane proteins and peptide studies.

Indexed as

HumansNeurodegenerative DiseasesProtein ConformationProteinsSpectroscopy, Fourier Transform InfraredProteinsAmyloidFourier transform infrared (FTIR) spectroscopyMicrospectroscopyProtein aggregationProtein secondary structure

Identifiers

PMID23357359
PMCPMC3722250
OpenAlexW2104214361

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.