Evidence map›Paper›PMID 27538185›Full record

ArticleProtein science : a publication of the Protein Society2016

Patterning protein complexes on DNA nanostructures using a GFP nanobody.

R F Sommese, R F Hariadi, K Kim, M Liu, M J Tyska, S Sivaramakrishnan

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. DNA Transformations for Diagnosis and Therapy.Advanced functional materials · 2021
    Review
  11. 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

6 authors.

R F SommeseDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, 55455.
R F HariadiDepartment of Physics, Arizona State University, Tempe, Arizona, 85287.
K KimDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, 55455.
M LiuBiodesign Center for Molecular Design and Biomimetics, Arizona State University, Tempe, Arizona, 85287.
M J TyskaDepartment of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, Tennessee, 37232.
S SivaramakrishnanDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, 55455. sivaraj@umn.edu.

Funding

Molecular basis of brush border assemblyR01DK095811 · NIDDK · VANDERBILT UNIVERSITY · PI MATTHEW J TYSKA · 2013 to 2026
$4.9M
Regulation of Brush Border Structure by Myosin-1aR01DK075555 · NIDDK · VANDERBILT UNIVERSITY · PI TYSKA, MATTHEW J · 2007 to 2016
$2.7M
The kinase toolbox: Mapping the spatial and temporal regulation of cell signalingDP2CA186752 · NCI · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2013 to 2013
$2.3M
Probing molecular mechanisms of GPCR functional selectivity in live cellsR01GM105646 · NIGMS · UNIVERSITY OF MINNESOTA · PI SIVARAMAKRISHNAN, SIVARAJ · 2014 to 2017
$1.1M
NCI NIH HHS DP2 CA186752NIDDK NIH HHS R01 DK075555NIDDK NIH HHS R01 DK095811NIGMS NIH HHS R01 GM105646
6 · The paper itself

Abstract

DNA nanostructures have become an important and powerful tool for studying protein function over the last 5 years. One of the challenges, though, has been the development of universal methods for patterning protein complexes on DNA nanostructures. Herein, we present a new approach for labeling DNA nanostructures by functionalizing them with a GFP nanobody. We demonstrate the ability to precisely control protein attachment via our nanobody linker using two enzymatic model systems, namely adenylyl cyclase activity and myosin motility. Finally, we test the power of this attachment method by patterning unpurified, endogenously expressed Arp2/3 protein complex from cell lysate. By bridging DNA nanostructures with a fluorescent protein ubiquitous throughout cell and developmental biology and protein biochemistry, this approach significantly streamlines the application of DNA nanostructures as a programmable scaffold in biological studies.

Indexed as

Actin-Related Protein 2-3 ComplexAnimalsDNAGreen Fluorescent ProteinsNanostructuresRecombinant Fusion ProteinsSingle-Domain AntibodiesSwineActin-Related Protein 2-3 ComplexDNAGreen Fluorescent ProteinsRecombinant Fusion ProteinsSingle-Domain Antibodiesadenylyl cyclaseArp2/3DNA nanostructuresGFPmyosin VInanobody

Identifiers

PMID27538185
PMCPMC5079250

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.