Evidence map›Paper›PMID 27229621›Full record

ArticleNature communications2016

A method to rapidly create protein aggregates in living cells.

Yusuke Miyazaki, Kota Mizumoto, Gautam Dey, Takamasa Kudo, John Perrino, Ling-Chun Chen, Tobias Meyer, Thomas J Wandless

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Unfolding or aggregation, that is the question.The Journal of biological chemistry · 2019
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

8 authors.

Yusuke MiyazakiDepartment of Chemical &Systems Biology Stanford University, Stanford, California 94305, USA.
Kota MizumotoDepartment of Biology Stanford University, Stanford, California 94305, USA.
Gautam DeyDepartment of Chemical &Systems Biology Stanford University, Stanford, California 94305, USA.ORCID 0000-0003-1416-6223
Takamasa KudoDepartment of Chemical &Systems Biology Stanford University, Stanford, California 94305, USA.
John PerrinoCell Sciences Imaging Facility Stanford University, Stanford, California 94305, USA.
Ling-Chun ChenDepartment of Chemical &Systems Biology Stanford University, Stanford, California 94305, USA.
Tobias MeyerDepartment of Chemical &Systems Biology Stanford University, Stanford, California 94305, USA.
Thomas J WandlessDepartment of Chemical &Systems Biology Stanford University, Stanford, California 94305, USA.

Funding

TRAINING & OUTREACH COREP50GM107615 · NIGMS · STANFORD UNIVERSITY · PI FERRELL, JAMES E. · 2013 to 2017
$10.9M
Chemotactic Signal TransductionR01GM063702 · NIGMS · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 2002 to 2017
$5.3M
REGULATION OF CA++/CALMODULIN KINASE BY NEUROTRANSMITTERR01GM030179 · NIGMS · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 1985 to 2018
$4.9M
Novel Molecules as In Vivo Biological ProbesR01GM073046 · NIGMS · STANFORD UNIVERSITY · PI WANDLESS, THOMAS JAMES · 2006 to 2017
$3.6M
CV7000S10OD018073 · OD · STANFORD UNIVERSITY · PI MEYER, TOBIAS · 2014 to 2014
$599k
NIGMS NIH HHS P50 GM107615NIGMS NIH HHS R01 GM030179NIGMS NIH HHS R01 GM063702NIGMS NIH HHS R01 GM073046NIH HHS S10 OD018073
6 · The paper itself

Abstract

The accumulation of protein aggregates is a common pathological hallmark of many neurodegenerative diseases. However, we do not fully understand how aggregates are formed or the complex network of chaperones, proteasomes and other regulatory factors involved in their clearance. Here, we report a chemically controllable fluorescent protein that enables us to rapidly produce small aggregates inside living cells on the order of seconds, as well as monitor the movement and coalescence of individual aggregates into larger structures. This method can be applied to diverse experimental systems, including live animals, and may prove valuable for understanding cellular responses and diseases associated with protein aggregates.

Indexed as

Protein AggregatesProtein Aggregation, PathologicalAnimalsBinding SitesCaenorhabditis elegansCell Line, TumorGreen Fluorescent ProteinsHEK293 CellsHumansMiceMicroscopy, ConfocalMicroscopy, FluorescenceNIH 3T3 CellsTacrolimus Binding Protein 1ATime-Lapse ImagingGreen Fluorescent ProteinsProtein AggregatesTacrolimus Binding Protein 1A

Identifiers

PMID27229621
PMCPMC4894968

What OpenQuestion holds

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LicenceCC BY
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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.