Evidence map›Paper›PMID 22051023›Full record

ReviewBiochimica et biophysica acta2012

Computational studies of membrane proteins: models and predictions for biological understanding.

Jie Liang, Hammad Naveed, David Jimenez-Morales, Larisa Adamian, Meishan Lin

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 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
2.4field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 48 citations in OpenAlex.

  1. Challenges of Protein-Protein Docking of the Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  2. Pharmaceutical science advances · 2023
    Article
  3. Article
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  5. GeTFEP: A general transfer free energy profile of transmembrane proteins.Protein science : a publication of the Protein Society · 2020
    Article
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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 1 institution in 1 country.

Jie LiangDepartment of Bioengineering, Chicago, IL 60607, USA. Jliang@uic.edu
Hammad Naveed
David Jimenez-Morales
Larisa Adamian
Meishan Lin
Bioengineering Center · RU

Funding

Chicago Tri-Institutional Center for Chemical Methods and Library DevelopmentP50GM086145 · NIGMS · UNIVERSITY OF CHICAGO · PI KOZMIN, SERGEY A · 2008 to 2012
$9.9M
Computational assembly of beta-barrel membrane proteinsR01GM079804 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LIANG, JIE · 2007 to 2016
$2.8M
NIGMS NIH HHS GM079804NIGMS NIH HHS GM086145NIGMS NIH HHS P50 GM086145NIGMS NIH HHS R01 GM079804
6 · The paper itself

Abstract

We discuss recent progresses in computational studies of membrane proteins based on physical models with parameters derived from bioinformatics analysis. We describe computational identification of membrane proteins and prediction of their topology from sequence, discovery of sequence and spatial motifs, and implications of these discoveries. The detection of evolutionary signal for understanding the substitution pattern of residues in the TM segments and for sequence alignment is also discussed. We further discuss empirical potential functions for energetics of inserting residues in the TM domain, for interactions between TM helices or strands, and their applications in predicting lipid-facing surfaces of the TM domain. Recent progresses in structure predictions of membrane proteins are also reviewed, with further discussions on calculation of ensemble properties such as melting temperature based on simplified state space model. Additional topics include prediction of oligomerization state of membrane proteins, identification of the interfaces for protein-protein interactions, and design of membrane proteins. This article is part of a Special Issue entitled: Protein Folding in Membranes.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsComputational BiologyEvolution, MolecularHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsMolecular Sequence DataProtein BindingMembrane Proteins

Identifiers

PMID22051023
PMCPMC3737997
OpenAlexW2118504593

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.