Evidence map›Paper›PMID 33401638›Full record

ReviewMolecules (Basel, Switzerland)2021

Ultrafast Fluorescence Spectroscopy via Upconversion and Its Applications in Biophysics.

Simin Cao, Haoyang Li, Zenan Zhao, Sanjun Zhang, Jinquan Chen, Jianhua Xu, Jay R Knutson, Ludwig Brand

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

2 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
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

8 authors at 3 institutions in 2 countries.

Simin CaoState Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China.
Haoyang LiState Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China.
Zenan ZhaoState Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China.
Sanjun ZhangState Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China.
Jinquan ChenState Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China.
Jianhua XuState Key Laboratory of Precision Spectroscopy, East China Normal University, Shanghai 200062, China.
Jay R KnutsonLaboratory for Advanced Microscopy and Biophotonics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Ludwig BrandDepartment of Biology, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
East China Normal University · CNJohns Hopkins University · USNational Heart Lung and Blood Institute · US

Funding

Time Resolved Fluorescence SpectroscopyZIAHL001452 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KNUTSON, JAY R · 2009 to 2025
$5.1M
National Natural Science Foundation of China No. 11674101
6 · The paper itself

Abstract

In this review, the experimental set-up and functional characteristics of single-wavelength and broad-band femtosecond upconversion spectrophotofluorometers developed in our laboratory are described. We discuss applications of this technique to biophysical problems, such as ultrafast fluorescence quenching and solvation dynamics of tryptophan, peptides, proteins, reduced nicotinamide adenine dinucleotide (NADH), and nucleic acids. In the tryptophan dynamics field, especially for proteins, two types of solvation dynamics on different time scales have been well explored: ~1 ps for bulk water, and tens of picoseconds for "biological water", a term that combines effects of water and macromolecule dynamics. In addition, some proteins also show quasi-static self-quenching (QSSQ) phenomena. Interestingly, in our more recent work, we also find that similar mixtures of quenching and solvation dynamics occur for the metabolic cofactor NADH. In this review, we add a brief overview of the emerging development of fluorescent RNA aptamers and their potential application to live cell imaging, while noting how ultrafast measurement may speed their optimization.

Indexed as

FluorescenceBiophysicsNucleic AcidsPeptidesProteinsSpectrometry, FluorescenceTryptophanNucleic AcidsPeptidesProteinsTryptophanfluorescent RNA aptamerNADHquasi-static self-quenchingsolvation dynamicstryptophanupconversion

Identifiers

PMID33401638
PMCPMC7794851
OpenAlexW3119502363

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.