Evidence map›Paper›PMID 27468111›Full record

ReviewCurrent opinion in structural biology2016

Structure-guided wavelength tuning in far-red fluorescent proteins.

Ho-Leung Ng, Michael Z Lin

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Recent Advances in Gene Therapy for Cancer Theranostics.Current opinion in biomedical engineering · 2021
    Article
  5. 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

2 authors.

Ho-Leung NgDepartment of Chemistry, University of Hawaii at Manoa, Honolulu, HI, USA; University of Hawaii Cancer Center, Honolulu, HI, USA. Electronic address: hng@hawaii.edu.
Michael Z LinDepartment of Neurobiology, Stanford University, Stanford, CA, USA; Department of Bioengineering, Stanford University, Stanford, CA, USA; Department of Pediatrics, Stanford University, Stanford, CA, USA. Electronic address: mzlin@stanford.edu.

Funding

TRAINING & OUTREACH COREP50GM107615 · NIGMS · STANFORD UNIVERSITY · PI FERRELL, JAMES E. · 2013 to 2017
$10.9M
Optogenetics for all: A general method for optical control of protein activityDP1GM111003 · NIGMS · STANFORD UNIVERSITY · PI LIN, MICHAEL Z. · 2013 to 2017
$4.0M
Protein voltage sensors: kilohertz imaging of neural dynamics in behaving animalsU01NS090600 · NINDS · STANFORD UNIVERSITY · PI LIN, MICHAEL Z., SCHNITZER, MARK J · 2014 to 2016
$2.8M
NIGMS NIH HHS DP1 GM111003NIGMS NIH HHS P50 GM107615NINDS NIH HHS U01 NS090600
6 · The paper itself

Abstract

In recent years, protein engineers have succeeded in tuning the excitation spectra of natural fluorescent proteins from green wavelengths into orange and red wavelengths, resulting in the creation of a series of fluorescent proteins with emission in the far-red portions of the optical spectrum. These results have arisen from the synergistic combination of structural knowledge of fluorescent proteins, chemical intuition, and high-throughput screening methods. Here we review structural features found in autocatalytic far-red fluorescent proteins, and discuss how they add to our understanding of the biophysical mechanisms of wavelength tuning in biological chromophores.

Indexed as

AnimalsBiocatalysisEvolution, MolecularLuminescent ProteinsRed Fluorescent ProteinLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID27468111
PMCPMC5548387

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Registered trials

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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.