Evidence map›Paper›PMID 36107339›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Fluorescent Proteins: Crystallization, Structural Determination, and Nonnatural Amino Acid Incorporation.

Rochelle D Ahmed, Husam Sabah Auhim, Harley L Worthy, D Dafydd Jones

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. 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

4 authors at 3 institutions in 2 countries.

Rochelle D AhmedSchool of Biosciences, Molecular Biosciences Division, Cardiff University, Cardiff, UK.
Husam Sabah AuhimDepartment of Biology, College of Science, University of Baghdad, Baghdad, Iraq.
Harley L WorthyDepartment of Biosciences, University of Exeter, Exeter, UK.
D Dafydd JonesSchool of Biosciences, Molecular Biosciences Division, Cardiff University, Cardiff, UK. JonesDD@cardiff.ac.uk.
Cardiff University · GBUniversity of Baghdad · IQUniversity of Exeter · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H003746/1Biotechnology and Biological Sciences Research Council BB/M000249/1
6 · The paper itself

Abstract

Fluorescent proteins have revolutionized cell biology and cell imaging through their use as genetically encoded tags. Structural biology has been pivotal in understanding how their unique fluorescent properties manifest through the formation of the chromophore and how the spectral properties are tuned through interaction networks. This knowledge has in turn led to the construction of novel variants with new and improved properties. Here we describe the process by which fluorescent protein structures are determined, starting from recombinant protein production to structure determination by molecular replacement. We also describe how to incorporate and determine the structures of proteins containing non-natural amino acids. Recent advances in protein engineering have led to reprogramming of the genetic code to allow incorporation of new chemistry at designed residue positions, with fluorescent proteins being at the forefront of structural studies in this area. The impact of such new chemistry on protein structure is still limited; the accumulation of more protein structures will undoubtedly improve our understanding and ability to engineer proteins with new chemical functionality.

Indexed as

Amino AcidsGenetic CodeColoring AgentsCrystallizationProtein EngineeringRecombinant ProteinsAmino AcidsColoring AgentsRecombinant ProteinsExpanded genetic codeFluorescent proteinMolecular replacementNon-natural amino acidProtein engineeringProtein structureRecombinant protein productionSynchrotron light sourceX-ray crystallography

Identifiers

PMID36107339
OpenAlexW4295901395

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.