Evidence map›Paper›PMID 23095057›Full record

ArticleJournal of the American Chemical Society2012

Effect of surfactant hydrophobicity on the pathway for unfolding of ubiquitin.

Bryan F Shaw, Grégory F Schneider, George M Whitesides

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 20 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Bryan F ShawDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States. bryan_shaw@baylor.edu
Grégory F Schneider
George M Whitesides
Harvard University · USHarvard University Press · US

Funding

Capillary Electrophoresis and Protein BiophysicsR01GM051559 · NIGMS · HARVARD UNIVERSITY · PI WHITESIDES, GEORGE M · 1994 to 2010
$2.6M
Net charge in protein structure and aggregation: a charge ladder approachF32GM081055 · NIGMS · HARVARD UNIVERSITY · PI SHAW, BRYAN F. · 2007 to 2008
$96k
NIGMS NIH HHS F32 GM081055NIGMS NIH HHS GM 051559NIGMS NIH HHS GM081055NIGMS NIH HHS R01 GM051559
6 · The paper itself

Abstract

This paper describes the interaction between ubiquitin (UBI) and three sodium n-alkyl sulfates (SC(n)S) that have the same charge (Z = -1) but different hydrophobicity (n = 10, 12, or 14). Increasing the hydrophobicity of the n-alkyl sulfate resulted in (i) an increase in the number of distinct intermediates (that is, complexes of UBI and surfactant) that form along the pathway of unfolding, (ii) a decrease in the minimum concentrations of surfactant at which intermediates begin to form (i.e., a more negative ΔG(binding) of surfactant for UBI), and (iii) an increase in the number of surfactant molecules bound to UBI in each intermediate or complex. These results demonstrate that small changes in the hydrophobicity of a surfactant can significantly alter the binding interactions with a folded or unfolded cytosolic protein.

Indexed as

Hydrophobic and Hydrophilic InteractionsModels, MolecularProtein UnfoldingSulfuric Acid EstersSurface-Active AgentsUbiquitinSulfuric Acid EstersSurface-Active AgentsUbiquitin

Identifiers

PMID23095057
PMCPMC3518387
OpenAlexW2142895923

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.