Evidence map›Paper›PMID 21910966›Full record

ReviewBiochimica et biophysica acta2012

Transmembrane helix dimerization: beyond the search for sequence motifs.

Edwin Li, William C Wimley, Kalina Hristova

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 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

85 citing papers in PubMed, 164 citations in OpenAlex.

  1. Article
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  7. Review
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  9. Article
  10. Rescue ofeLife · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. ACS chemical biology · 2022
    Article
  15. Uncoupling Proteins and Regulated Proton Leak in Mitochondria.International journal of molecular sciences · 2022
    Review
  16. Article
  17. Review
  18. Article
  19. Interaction between the type 4 pili machinery and a diguanylate cyclase fine-tune c-di-GMP levels during early biofilm formation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

3 authors at 3 institutions in 1 country.

Edwin LiDepartment of Biology, Saint Joseph's University, Philadelphia, PA 19131, USA.
William C Wimley
Kalina Hristova
Johns Hopkins University · USSaint Joseph's University · USTulane University · US

Funding

Seeking the Physical Basis of AchondroplasiaR01GM068619 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2004 to 2022
$5.4M
Folding and Design of Beta Sheets in MembranesR01GM060000 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI WIMLEY, WILLIAM C · 2001 to 2010
$2.6M
QI-FRET: a new tool in Receptor Tyrosine Kinase researchR01GM095930 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI HRISTOVA, KALINA · 2011 to 2014
$1.4M
NIGMS NIH HHS GM060000NIGMS NIH HHS GM068619NIGMS NIH HHS GM095930NIGMS NIH HHS R01 GM060000NIGMS NIH HHS R01 GM068619NIGMS NIH HHS R01 GM095930
6 · The paper itself

Abstract

Studies of the dimerization of transmembrane (TM) helices have been ongoing for many years now, and have provided clues to the fundamental principles behind membrane protein (MP) folding. Our understanding of TM helix dimerization has been dominated by the idea that sequence motifs, simple recognizable amino acid sequences that drive lateral interaction, can be used to explain and predict the lateral interactions between TM helices in membrane proteins. But as more and more unique interacting helices are characterized, it is becoming clear that the sequence motif paradigm is incomplete. Experimental evidence suggests that the search for sequence motifs, as mediators of TM helix dimerization, cannot solve the membrane protein folding problem alone. Here we review the current understanding in the field, as it has evolved from the paradigm of sequence motifs into a view in which the interactions between TM helices are much more complex. This article is part of a Special Issue entitled: Membrane protein structure and function.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCell MembraneDimerizationHumansMembrane ProteinsMolecular Sequence DataProtein FoldingProtein Structure, SecondaryMembrane Proteins

Identifiers

PMID21910966
PMCPMC3253898
OpenAlexW2122510434

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.