Evidence map›Paper›PMID 20383133›Full record

ArticleNature methods2010

A streptavidin variant with slower biotin dissociation and increased mechanostability.

Claire E Chivers, Estelle Crozat, Calvin Chu, Vincent T Moy, David J Sherratt, Mark Howarth

Abstract read
In one paragraph

Article in Nature methods, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing 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

90 citing papers in PubMed.

  1. Review
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30 more citing papers are in PubMed but not listed here.

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

6 authors.

Claire E ChiversDepartment of Biochemistry, Oxford University, UK.
Estelle Crozat
Calvin Chu
Vincent T Moy
David J Sherratt
Mark Howarth

Funding

AFM studies of SNARE-mediated membrane fusionR01GM086808 · NIGMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MOY, VINCENT T · 2009 to 2012
$1.2M
Biotechnology and Biological Sciences Research CouncilNIGMS NIH HHS R01 GM086808Wellcome Trust
6 · The paper itself

Abstract

Streptavidin binds biotin conjugates with exceptional stability but dissociation does occur, limiting its use in imaging, DNA amplification and nanotechnology. We identified a mutant streptavidin, traptavidin, with more than tenfold slower biotin dissociation, increased mechanical strength and improved thermostability; this resilience should enable diverse applications. FtsK, a motor protein important in chromosome segregation, rapidly displaced streptavidin from biotinylated DNA, whereas traptavidin resisted displacement, indicating the force generated by Ftsk translocation.

Indexed as

Biomechanical PhenomenaBiotinBiotinylationEscherichia coli ProteinsMembrane ProteinsMicroscopy, Atomic ForceMolecular Sequence DataProtein BindingProtein EngineeringStreptavidinBiotinEscherichia coli ProteinsFtsK protein, E coliMembrane ProteinsStreptavidintraptavidin

Identifiers

PMID20383133
PMCPMC2862113

What OpenQuestion holds

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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.