Evidence map›Paper›PMID 22276737›Full record

ArticleACS nano2012

Manipulating protein conformations by single-molecule AFM-FRET nanoscopy.

Yufan He, Maolin Lu, Jin Cao, H Peter Lu

Abstract read
In one paragraph

Article in ACS nano, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 80 citations in OpenAlex.

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  7. Quantifying molecular- to cellular-level forces in living cells.Journal of physics D: Applied physics · 2021
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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

4 authors at 1 institution in 1 country.

Yufan HeCenter for Photochemical Sciences, Department of Chemistry, Bowling Green State University, Bowling Green, Ohio 43403, United States.
Maolin Lu
Jin Cao
H Peter Lu
Bowling Green State University · US

Funding

Manipulating Single-Molecule Enzyme Conformations and ActivitiesR01GM084402 · NIGMS · BOWLING GREEN STATE UNIVERSITY · PI LU, H PETER · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM084402
6 · The paper itself

Abstract

Combining atomic force microscopy and fluorescence resonance energy transfer spectroscopy (AFM-FRET), we have developed a single-molecule AFM-FRET nanoscopy approach capable of effectively pinpointing and mechanically manipulating a targeted dye-labeled single protein in a large sampling area and simultaneously monitoring the conformational changes of the targeted protein by recording single-molecule FRET time trajectories. We have further demonstrated an application of using this nanoscopy on manipulation of single-molecule protein conformation and simultaneous single-molecule FRET measurement of a Cy3-Cy5-labeled kinase enzyme, HPPK (6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase). By analyzing time-resolved FRET trajectories and correlated AFM force pulling curves of the targeted single-molecule enzyme, we are able to observe the protein conformational changes of a specific coordination by AFM mechanic force pulling.

Indexed as

DiphosphotransferasesFluorescence Resonance Energy TransferGlassMechanical PhenomenaMicroscopyMicroscopy, Atomic ForceModels, MolecularNanotechnologyProtein Conformation2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinaseDiphosphotransferases

Identifiers

PMID22276737
PMCPMC3662055
OpenAlexW1992930044

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.