Evidence map›Paper›PMID 22579257›Full record

ArticleStructure (London, England : 1993)2012

Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributions.

Chaim A Schramm, Brett T Hannigan, Jason E Donald, Chen Keasar, Jeffrey G Saven, William F Degrado, Ilan Samish

Abstract read
In one paragraph

Article 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 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Spatial arrangement of proteins in planar and curved membranes by PPM 3.0.Protein science : a publication of the Protein Society · 2022
    Article
  11. Multifaceted membrane binding head of the SARS-CoV-2 spike protein.Current research in structural biology · 2022
    Article
  12. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  13. Article
  14. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  15. Article
  16. Article
  17. A paradigm of thermal adaptation in penguins and elephants by tuning cold activation in TRPM8.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Quarterly reviews of biophysics · 2020
    Review
  19. Article
  20. 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

7 authors.

Chaim A SchrammGraduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Brett T Hannigan
Jason E Donald
Chen Keasar
Jeffrey G Saven
William F Degrado
Ilan Samish

Funding

De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
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 HL085303NHLBI NIH HHS R01 HL085303NIGMS NIH HHS GM54616NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

The complex hydrophobic and hydrophilic milieus of membrane-associated proteins pose experimental and theoretical challenges to their understanding. Here, we produce a nonredundant database to compute knowledge-based asymmetric cross-membrane potentials from the per-residue distributions of C(β), C(γ) and functional group atoms. We predict transmembrane and peripherally associated regions from genomic sequence and position peptides and protein structures relative to the bilayer (available at http://www.degradolab.org/ez). The pseudo-energy topological landscapes underscore positional stability and functional mechanisms demonstrated here for antimicrobial peptides, transmembrane proteins, and viral fusion proteins. Moreover, experimental effects of point mutations on the relative ratio changes of dual-topology proteins are quantitatively reproduced. The functional group potential and the membrane-exposed residues display the largest energetic changes enabling to detect native-like structures from decoys. Hence, focusing on the uniqueness of membrane-associated proteins and peptides, we quantitatively parameterize their cross-membrane propensity, thus facilitating structural refinement, characterization, prediction, and design.

Indexed as

AlgorithmsDatabases, FactualHydrophobic and Hydrophilic InteractionsKnowledge BasesMembrane ProteinsModels, MolecularProteinsThermodynamicsMembrane ProteinsProteins

Identifiers

PMID22579257
PMCPMC3366090

What OpenQuestion holds

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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.