Evidence map›Paper›PMID 28696524›Full record

ArticleSmall (Weinheim an der Bergstrasse, Germany)2017

Molecular Hyperthermia: Spatiotemporal Protein Unfolding and Inactivation by Nanosecond Plasmonic Heating.

Peiyuan Kang, Zhuo Chen, Steven O Nielsen, Kenneth Hoyt, Sheena D'Arcy, Jeremiah J Gassensmith, Zhenpeng Qin

Open access · greenAbstract read
In one paragraph

Article in Small (Weinheim an der Bergstrasse, Germany), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 43 citations in OpenAlex.

  1. The Nature of Non-Arrhenius Kinetics in the Heat Denaturation of Proteins.International journal of molecular sciences · 2026
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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

7 authors at 1 institution in 1 country.

Peiyuan KangDepartment of Mechanical Engineering, The University of Texas at Dallas 800 West Campbell Rd., Richardson, TX, 75080, USA.
Zhuo ChenDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 West Campbell Rd., Richardson, TX, 75080, USA.
Steven O NielsenDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 West Campbell Rd., Richardson, TX, 75080, USA.
Kenneth HoytDepartment of Bioengineering, The University of Texas at Dallas, 800 West Campbell Rd., Richardson, TX, 75080, USA.
Sheena D'ArcyDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 West Campbell Rd., Richardson, TX, 75080, USA.
Jeremiah J GassensmithDepartment of Chemistry and Biochemistry, The University of Texas at Dallas, 800 West Campbell Rd., Richardson, TX, 75080, USA.
Zhenpeng QinDepartment of Mechanical Engineering, The University of Texas at Dallas 800 West Campbell Rd., Richardson, TX, 75080, USA.ORCID 0000-0003-3406-3045
The University of Texas at Dallas · US

Funding

Molecular Ultrasound Imaging of Cancer Response to Antiangiogenic TherapyK25EB017222 · NIBIB · UNIVERSITY OF TEXAS DALLAS · PI HOYT, KENNETH · 2014 to 2018
$804k
Noninvasive Pressure Estimation in Breast Cancer using UltrasoundR21CA212851 · NCI · UNIVERSITY OF TEXAS DALLAS · PI HOYT, KENNETH · 2017 to 2018
$366k
NCI NIH HHS R21 CA212851NIBIB NIH HHS K25 EB017222
6 · The paper itself

Abstract

Spatiotemporal control of protein structure and activity in biological systems has important and broad implications in biomedical sciences as evidenced by recent advances in optogenetic approaches. Here, this study demonstrates that nanosecond pulsed laser heating of gold nanoparticles (GNP) leads to an ultrahigh and ultrashort temperature increase, coined as "molecular hyperthermia", which causes selective unfolding and inactivation of proteins adjacent to the GNP. Protein inactivation is highly dependent on both laser pulse energy and GNP size, and has a well-defined impact zone in the nanometer scale. It is anticipated that the fine control over protein structure and function enabled by this discovery will be highly enabling within a number of arenas, from probing the biophysics of protein folding/unfolding to the nanoscopic manipulation of biological systems via an optical trigger, to developing novel therapeutics for disease treatment without genetic modification.

Indexed as

Hot TemperatureProtein UnfoldingGoldMetal NanoparticlesProteinsTime FactorsGoldProteinsgold nanoparticleslaser heatingprotein inactivationprotein unfoldingthermoplasmonics

Identifiers

PMID28696524
PMCPMC5686774
OpenAlexW2734883636

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.