Evidence map›Paper›PMID 42115735›Full record

ArticleCommunications chemistry2026

Resolving protein condensates and aggregates in vivo by boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL Microscopy (FILM).

Bethany Weinberg, Zhongyue Guo, Rong Tang, Jianpeng Ao, Jiaze Yin, Guangrui Ding, Todd A Blute, Marzia Savini, Giulio Chiesa, Wentao Wang and 3 more

Abstract read
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In one paragraph

Article in Communications 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

13 authors.

Bethany Weinberg *Department of Molecular Biology, Cell Biology, & Biochemistry, Boston University, Boston, MA, USA.
Zhongyue Guo *Department of Biomedical Engineering, Boston University, Boston, MA, USA.
Rong TangDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, USA.
Jianpeng AoDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, USA.ORCID http://orcid.org/0000-0002-9625-4245
Jiaze YinDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, USA.ORCID http://orcid.org/0000-0001-6080-3073
Guangrui DingPhotonics Center, Boston University, Boston, MA, USA.
Todd A BluteDepartment of Molecular Biology, Cell Biology, & Biochemistry, Boston University, Boston, MA, USA.
Marzia SaviniHHMI Janelia Research Campus, Ashburn, VA, USA.ORCID http://orcid.org/0000-0001-8945-7629
Giulio ChiesaDepartment of Biomedical Engineering, University of Toronto, Toronto, ON, Canada.
Wentao WangCell and Developmental Biology, School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Matt GoodCell and Developmental Biology, School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0002-6367-1034
Meng C WangHHMI Janelia Research Campus, Ashburn, VA, USA. mengwang@janelia.hhmi.org.
Ji-Xin ChengDepartment of Biomedical Engineering, Boston University, Boston, MA, USA. jxcheng@bu.edu.ORCID http://orcid.org/0000-0002-5607-6683

Funding

Vibrational Spectroscopic Imaging to Unveil Hidden Signatures in Living SystemsR35GM136223 · NIGMS · BOSTON UNIVERSITY (CHARLES RIVER CAMPUS) · PI CHENG, JI-XIN · 2020 to 2025
$5.7M
NIGMS NIH HHS R35 GM136223U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM136223
6 · The paper itself

Abstract

Protein assemblies, including aggregates and condensates, are closely linked to health and diseases. We demonstrate boxcar-enhanced Fluorescence-detected mid-Infrared photothermaL Microscopy (FILM), using two model species, Caenorhabditis elegans and Saccharomyces cerevisiae, to quantitatively resolve these protein states in vivo by imaging β-sheet and α-helix secondary structures and analyzing their ratios. This method directly distinguishes polyglutamine (PolyQ) protein aggregates, α-synuclein protein condensates, and P-granule condensates implicated in neurodegenerative diseases and embryonic development in live organisms. It further enables the unraveling of protein assembly dynamics and their physio-pathological roles, such as age-related progression of PolyQ from condensates to aggregates.

Identifiers

PMID42115735
PMCPMC13522537

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