Evidence map›Paper›PMID 37069270›Full record

ArticleNature chemistry2023

Spatiotemporal functional assembly of split protein pairs through a light-activated SpyLigation.

Emily R Ruskowitz, Brizzia G Munoz-Robles, Alder C Strange, Carson H Butcher, Sebastian Kurniawan, Jeremy R Filteau, Cole A DeForest

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Stimuli-triggered formation ofCell biomaterials · 2026
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  4. Enzymatic Methods for Assembling and Modifying Hydrogel Biomaterials.Regenerative engineering and translational medicine · 2025
    Article
  5. Photocleavable Systems for Cell Biology: Conceptual Design across Molecular Modalities.Chembiochem : a European journal of chemical biology · 2025
    Review
  6. Article
  7. Article
  8. A hydrophobic photouncaging reaction to profile the lipid droplet interactome in tissues.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Photoactivatable Nanobody Conjugate Dimerizer Temporally Resolves Tiam1-Rac1 Signaling Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  16. De novo design of modular protein hydrogels with programmable intra- and extracellular viscoelasticity.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Article
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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

7 authors at 2 institutions in 1 country.

Emily R Ruskowitz *Department of Chemical Engineering, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0001-8772-4869
Brizzia G Munoz-Robles *Department of Bioengineering, University of Washington, Seattle, WA, USA.
Alder C StrangeDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Carson H ButcherDepartment of Biology, University of Washington, Seattle, WA, USA.
Sebastian KurniawanDepartment of Chemical Engineering, University of Washington, Seattle, WA, USA.ORCID http://orcid.org/0000-0003-4662-3548
Jeremy R FilteauDepartment of Chemical Engineering, University of Washington, Seattle, WA, USA.
Cole A DeForestDepartment of Chemical Engineering, University of Washington, Seattle, WA, USA. profcole@uw.edu.ORCID http://orcid.org/0000-0003-0337-3577
University of Washington · USCalifornia Institute for Regenerative Medicine · US

Funding

Mimicking, Exploiting, and Understanding Biology's Heterogeneity in 4DR35GM138036 · NIGMS · UNIVERSITY OF WASHINGTON · PI Cole A DeForest · 2020 to 2026
$2.3M
NIGMS NIH HHS R35 GM138036
6 · The paper itself

Abstract

Proteins provide essential functional regulation of many bioprocesses across all scales of life; however, new techniques to specifically modulate protein activity within living systems and in engineered biomaterials are needed to better interrogate fundamental cell signalling and guide advanced decisions of biological fate. Here we establish a generalizable strategy to rapidly and irreversibly activate protein function with full spatiotemporal control. Through the development of a genetically encoded and light-activated SpyLigation (LASL), bioactive proteins can be stably reassembled from non-functional split fragment pairs following brief exposure (typically minutes) to cytocompatible light. Employing readily accessible photolithographic processing techniques to specify when, where and how much photoligation occurs, we demonstrate precise protein activation of UnaG, NanoLuc and Cre recombinase using LASL in solution, biomaterials and living mammalian cells, as well as optical control over protein subcellular localization. Looking forward, we expect that these photoclick-based optogenetic approaches will find tremendous utility in probing and directing complex cellular fates in both time and three-dimensional space.

Indexed as

MammalsAnimals

Identifiers

PMID37069270
PMCPMC10164143
OpenAlexW4366163192

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.