Evidence map›Paper›PMID 22244752›Full record

ReviewStructure (London, England : 1993)2012

Computational design of membrane proteins.

Jose Manuel Perez-Aguilar, Jeffery G Saven

Abstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2012. 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. Review
  2. Review
  3. Article
  4. Membrane Protein Engineering with Rosetta.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  5. Designing minimalist membrane proteins.Biochemical Society transactions · 2019
    Review
  6. Review
  7. Review
  8. Article
  9. Computational design of membrane proteins using RosettaMembrane.Protein science : a publication of the Protein Society · 2018
    Article
  10. Outer membrane protein design.Current opinion in structural biology · 2017
    Review
  11. Membrane proteins: always an insoluble problem?Biochemical Society transactions · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Naturally evolved G protein-coupled receptors adopt metastable conformations.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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.

Jose Manuel Perez-AguilarDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
Jeffery G Saven

Funding

X-ray and Neutron Interferometry Studies of Anesthetic Interactions with VoltageP01GM055876 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LOLL, PATRICK J · 1997 to 2017
$22.4M
Force Microscopy of Endothelial Cells on Novel Peptide MaterialsR01HL085303 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI HAMMER, DANIEL A · 2007 to 2011
$2.1M
NHLBI NIH HHS R01 HL085303NIGMS NIH HHS P01 GM055876NIGMS NIH HHS P01 GM55876
6 · The paper itself

Abstract

Membrane proteins are involved in a wide variety of cellular processes, and are typically part of the first interaction a cell has with extracellular molecules. As a result, these proteins comprise a majority of known drug targets. Membrane proteins are among the most difficult proteins to obtain and characterize, and a structure-based understanding of their properties can be difficult to elucidate. Notwithstanding, the design of membrane proteins can provide stringent tests of our understanding of these crucial biological systems, as well as introduce novel or targeted functionalities. Computational design methods have been particularly helpful in addressing these issues, and this review discusses recent studies that tailor membrane proteins to display specific structures or functions and examines how redesigned membrane proteins are being used to facilitate structural and functional studies.

Indexed as

Models, MolecularProtein ConformationComputational BiologyMembrane ProteinsProtein BindingProtein EngineeringMembrane Proteins

Identifiers

PMID22244752
PMCPMC4108999

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.