Evidence map›Paper›PMID 23602357›Full record

ReviewCurrent opinion in structural biology2013

Library methods for structural biology of challenging proteins and their complexes.

Darren J Hart, Geoffrey S Waldo

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Crystallization studies of the keratin-like domain from Arabidopsis thaliana SEPALLATA 3.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    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.

Darren J HartEMBL Grenoble Outstation and Unit of Virus Host-Cell Interactions, UMI3265 UJF-EMBL-CNRS, Grenoble, France. hart@embl.fr
Geoffrey S Waldo

Funding

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
NIGMS NIH HHS GM98177-01A1NIGMS NIH HHS P01 GM098177
6 · The paper itself

Abstract

Genetic engineering of constructs to improve solubility or stability is a common approach, but it is often unclear how to obtain improvements. When the domain composition of a target is poorly understood, or if there are insufficient structure data to guide sited directed mutagenesis, long iterative phases of subcloning or mutation and expression often prove unsuccessful despite much effort. Random library approaches can offer a solution to this problem and involve construction of large libraries of construct variants that are analysed via screens or selections for the desired phenotype. Huge improvements in construct behaviour can be achieved rapidly with no requirement for prior knowledge of the target. Here we review the development of these experimental strategies and recent successes.

Indexed as

Peptide LibraryDirected Molecular EvolutionMultiprotein ComplexesProtein ConformationProtein EngineeringSolubilityMultiprotein ComplexesPeptide Library

Identifiers

PMID23602357
PMCPMC4172339

What OpenQuestion holds

Textmetadata
LicenceTDM
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.