Evidence map›Paper›PMID 24336839›Full record

ReviewChemical Society reviews2014

Shedding light on protein folding landscapes by single-molecule fluorescence.

Priya R Banerjee, Ashok A Deniz

Abstract readReview
In one paragraph

Review in Chemical Society reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

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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

2 authors.

Priya R BanerjeeDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA. deniz@scripps.edu.
Ashok A Deniz

Funding

Single Molecule Studies of Protein Folding MechanismsR01GM066833 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2003 to 2017
$5.2M
NIGMS NIH HHS GM R01 066833NIGMS NIH HHS R01 GM066833
6 · The paper itself

Abstract

Single-molecule (SM) fluorescence methods have been increasingly instrumental in our current understanding of a number of key aspects of protein folding and aggregation landscapes over the past decade. With the advantage of a model free approach and the power of probing multiple subpopulations and stochastic dynamics directly in a heterogeneous structural ensemble, SM methods have emerged as a principle technique for studying complex systems such as intrinsically disordered proteins (IDPs), globular proteins in the unfolded basin and during folding, and early steps of protein aggregation in amyloidogenesis. This review highlights the application of these methods in investigating the free energy landscapes, folding properties and dynamics of individual protein molecules and their complexes, with an emphasis on inherently flexible systems such as IDPs.

Indexed as

Protein FoldingAnimalsFluorescenceHumansMolecular Dynamics SimulationProtein ConformationProteinsSpectrometry, FluorescenceProteins

Identifiers

PMID24336839
PMCPMC3958939

What OpenQuestion holds

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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.