Evidence map›Paper›PMID 37322011›Full record

ArticleLight, science & applications2023

Mid-infrared chemical imaging of intracellular tau fibrils using fluorescence-guided computational photothermal microscopy.

Jian Zhao, Lulu Jiang, Alex Matlock, Yihong Xu, Jiabei Zhu, Hongbo Zhu, Lei Tian, Benjamin Wolozin, Ji-Xin Cheng

Abstract read
In one paragraph

Article in Light, science & applications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Review
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  4. Label-Free Molecular Characterization of Protein Aggregates in Differentiated Astrocytes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Jian ZhaoDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA. jianzhao@knights.ucf.edu.ORCID http://orcid.org/0000-0002-3947-4049
Lulu JiangDepartment of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118, USA.
Alex MatlockDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA.ORCID http://orcid.org/0000-0002-4337-2715
Yihong XuDepartment of Physics, Boston University, Boston, MA, 02215, USA.
Jiabei ZhuDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA.
Hongbo ZhuState Key Laboratory of Luminescence and Applications, Changchun Institute of Optics, Fine Mechanics and Physics, Chinese Academy of Sciences, 130033, Changchun, China.ORCID http://orcid.org/0000-0002-8820-3907
Lei TianDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA.ORCID http://orcid.org/0000-0002-1316-4456
Benjamin WolozinDepartment of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118, USA.
Ji-Xin ChengDepartment of Electrical and Computer Engineering, Boston University, Boston, MA, 02215, USA. jxcheng@bu.edu.ORCID http://orcid.org/0000-0002-5607-6683

Funding

The Center for Label-free Imagingand Multiscale Biophotonics (CLIMB)P41EB031772 · NIBIB · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Stephen A Boppart · 2022 to 2026
$7.6M
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
NIBIB NIH HHS P41 EB031772NIGMS NIH HHS R35 GM136223
6 · The paper itself

Abstract

Amyloid proteins are associated with a broad spectrum of neurodegenerative diseases. However, it remains a grand challenge to extract molecular structure information from intracellular amyloid proteins in their native cellular environment. To address this challenge, we developed a computational chemical microscope integrating 3D mid-infrared photothermal imaging with fluorescence imaging, termed Fluorescence-guided Bond-Selective Intensity Diffraction Tomography (FBS-IDT). Based on a low-cost and simple optical design, FBS-IDT enables chemical-specific volumetric imaging and 3D site-specific mid-IR fingerprint spectroscopic analysis of tau fibrils, an important type of amyloid protein aggregates, in their intracellular environment. Label-free volumetric chemical imaging of human cells with/without seeded tau fibrils is demonstrated to show the potential correlation between lipid accumulation and tau aggregate formation. Depth-resolved mid-infrared fingerprint spectroscopy is performed to reveal the protein secondary structure of the intracellular tau fibrils. 3D visualization of the β-sheet for tau fibril structure is achieved.

Identifiers

PMID37322011
PMCPMC10272128

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Registered trials

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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.