Evidence map›Paper›PMID 26278175›Full record

ArticleStructure (London, England : 1993)2015

A Suite of Engineered GFP Molecules for Oligomeric Scaffolding.

David J Leibly, Mark A Arbing, Inna Pashkov, Natasha DeVore, Geoffrey S Waldo, Thomas C Terwilliger, Todd O Yeates

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020
    Review
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Crystal structure of the cyan fluorescent protein Cerulean-S175G.Acta crystallographica. Section F, Structural biology communications · 2016
    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

7 authors.

David J LeiblyDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA; UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA.
Mark A ArbingUCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA.
Inna PashkovUCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA.
Natasha DeVoreBioscience Division, Los Alamos National Laboratory, MS M888, Los Alamos, NM 87545, USA.
Geoffrey S WaldoBioscience Division, Los Alamos National Laboratory, MS M888, Los Alamos, NM 87545, USA.
Thomas C TerwilligerBioscience Division, Los Alamos National Laboratory, MS M888, Los Alamos, NM 87545, USA.
Todd O YeatesDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA; UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, CA 90095, USA. Electronic address: yeates@mbi.ucla.edu.

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Proj 3: Enhancing crystallization by supplying natural binding partnersP01GM098177 · NIGMS · LOS ALAMOS NAT SECTY-LOS ALAMOS NAT LAB · PI BRADBURY, ANDREW, EISENBERG, DAVID · 2012 to 2015
$4.7M
NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NIGMS NIH HHS P01 GM098177NIGMS NIH HHS T32 GM007185NIGMS NIH HHS T32GM007185
6 · The paper itself

Abstract

Applications ranging from synthetic biology to protein crystallization could be advanced by facile systems for connecting multiple proteins together in predefined spatial relationships. One approach to this goal is to engineer many distinct assembly forms of a single carrier protein or scaffold, to which other proteins of interest can then be readily attached. In this work we chose GFP as a scaffold and engineered many alternative oligomeric forms, driven by either specific disulfide bond formation or metal ion addition. We generated a wide range of spatial arrangements of GFP subunits from 11 different oligomeric variants, and determined their X-ray structures in a total of 33 distinct crystal forms. Some of the oligomeric GFP variants show geometric polymorphism depending on conditions, while others show considerable geometric rigidity. Potential future applications of this system are discussed.

Indexed as

Crystallography, X-RayGreen Fluorescent ProteinsModels, MolecularMutagenesis, Site-DirectedProtein FoldingProtein MultimerizationGreen Fluorescent Proteins

Identifiers

PMID26278175
PMCPMC4568552

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.