Evidence map›Paper›PMID 23523554›Full record

ArticleMethods (San Diego, Calif.)2013

Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.

Paul J Bujalowski, Andres F Oberhauser

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  17. Nanoimaging methods for biomedicine.Methods (San Diego, Calif.) · 2013
    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

2 authors.

Paul J BujalowskiDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, TX 77555, USA.
Andres F Oberhauser

Funding

UTMB OAIC Research Education Component (REC)P30AG024832 · NIA · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI JAMES S. GOODWIN, MD, MELISSA M. MORROW · 2005 to 2026
$26.7M
The Nano-mechanics of Polycystin-1R01DK073394 · NIDDK · UNIVERSITY OF TEXAS MED BR GALVESTON · PI OBERHAUSER, ANDRES F. · 2006 to 2010
$1.2M
NIA NIH HHS P30 AG024832NIDDK NIH HHS R01 DK073394NIDDK NIH HHS R01DK073394
6 · The paper itself

Abstract

During the last two decades single-molecule manipulation techniques such as atomic force microscopy (AFM) has risen to prominence through their unique capacity to provide fundamental information on the structure and function of biomolecules. Here we describe the use of single-molecule AFM to track protein unfolding and refolding pathways, enzymatic catalysis and the effects of osmolytes and chaperones on protein stability and folding. We will outline the principles of operation for two different AFM pulling techniques: length clamp and force-clamp and discuss prominent applications. We provide protocols for the construction of polyproteins which are amenable for AFM experiments, the preparation of different coverslips, choice and calibration of AFM cantilevers. We also discuss the selection criteria for AFM recordings, the calibration of AFM cantilevers, protein sample preparations and analysis of the obtained data.

Indexed as

Microscopy, Atomic ForceProtein RefoldingProtein UnfoldingBuffersCalibrationComputer SimulationHumansImmobilized ProteinsMechanical PhenomenaModels, MolecularOsmolar ConcentrationPolyproteinsBuffersImmobilized ProteinsPolyproteins

Identifiers

PMID23523554
PMCPMC3669651

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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.