Evidence map›Paper›PMID 21854852›Full record

ReviewMethods (San Diego, Calif.)2011

Crystallization chaperone strategies for membrane proteins.

Raquel L Lieberman, Jeffrey A Culver, Kevin C Entzminger, Jennifer C Pai, Jennifer A Maynard

Open access · greenAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Preparing for successful protein crystallization experiments.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  3. General Strategies for RNA X-ray Crystallography.Molecules (Basel, Switzerland) · 2023
    Review
  4. Article
  5. Article
  6. Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016
    Review
  13. Increased Fab thermoresistance via VH-targeted directed evolution.Protein engineering, design & selection : PEDS · 2015
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors at 2 institutions in 1 country.

Raquel L LiebermanSchool of Chemistry and Biochemistry, Institute for Bioscience and Bioengineering, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, GA 30332, USA. raquel.lieberman@chemistry.gatech.edu
Jeffrey A Culver
Kevin C Entzminger
Jennifer C Pai
Jennifer A Maynard
The University of Texas at Austin · USGeorgia Institute of Technology · US

Funding

Returning to the workforce supplement request for R01 GM095638R01GM095638 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MAYNARD, JENNIFER A · 2010 to 2014
$1.3M
Crystal structure of signal peptide peptidase with engineered antibody fragmentR21DK091357 · NIDDK · GEORGIA INSTITUTE OF TECHNOLOGY · PI LIEBERMAN, RAQUEL L, MAYNARD, JENNIFER A · 2010 to 2011
$404k
NIDDK NIH HHS R21 DK091357NIDDK NIH HHS R21DK91357NIGMS NIH HHS R01 GM095638NIGMS NIH HHS R01GM095638
6 · The paper itself

Abstract

From G protein-coupled receptors to ion channels, membrane proteins represent over half of known drug targets. Yet, structure-based drug discovery is hampered by the dearth of available three-dimensional models for this large category of proteins. Other than efforts to improve membrane protein expression and stability, current strategies to improve the ability of membrane proteins to crystallize involve examining many orthologs and DNA constructs, testing the effects of different detergents for purification and crystallization, creating a lipidic environment during crystallization, and cocrystallizing with covalent or non-covalent soluble protein chaperones with an intrinsic high propensity to crystallize. In this review, we focus on this last category, highlighting successes of crystallization chaperones in membrane protein structure determination and recent developments in crystal chaperone engineering, including molecular display to enhance chaperone crystallizability, and end with a novel generic approach in development to target any membrane protein of interest.

Indexed as

AnimalsAntibodies, MonoclonalCrystallizationCrystallography, X-RayDetergentsHumansHybridomasMembrane ProteinsMultiprotein ComplexesProtein BindingProtein ConformationProtein EngineeringRecombinant Fusion ProteinsAntibodies, MonoclonalDetergentsMembrane ProteinsMultiprotein ComplexesRecombinant Fusion Proteins

Identifiers

PMID21854852
PMCPMC6186007
OpenAlexW2008142453

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.