Evidence map›Paper›PMID 22650985›Full record

ReviewBiochemistry2012

Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.

Hao Dong, Mukesh Sharma, Huan-Xiang Zhou, Timothy A Cross

Abstract readReview
In one paragraph

Review in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

56 citing papers in PubMed, 91 citations in OpenAlex.

  1. System reconstruction ofSynthetic and systems biotechnology · 2027
    Article
  2. Review
  3. Article
  4. Novel homozygousTherapeutic advances in neurological disorders · 2026
    Article
  5. Article
  6. Article
  7. Rescue of Epilepsy-Associated Mutations of the Highly Conserved Glycine Residue 443 in the Human GABA Transporter 1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  8. Structural insights into glucose-6-phosphate recognition and hydrolysis by human G6PC1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
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  17. The role of TMS 12 in the staphylococcal multidrug efflux protein QacA.The Journal of antimicrobial chemotherapy · 2023
    Article
  18. Article
  19. Genetics, Functions, and Clinical Impact of Presenilin-1 (PSEN1) Gene.International journal of molecular sciences · 2022
    Review
  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

4 authors at 2 institutions in 1 country.

Hao DongInstitute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.
Mukesh Sharma
Huan-Xiang Zhou
Timothy A Cross
Florida State University · USNational High Magnetic Field Laboratory · US

Funding

Target IdentificationP01AI074805 · NIAID · FLORIDA STATE UNIVERSITY · PI CROSS, TIMOTHY A · 2009 to 2013
$8.7M
Modeling Crowding and Confinement of Cellular EnvironmentsR01GM088187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 2010 to 2015
$1.6M
NIAID NIH HHS AI-074805NIAID NIH HHS P01 AI074805NIGMS NIH HHS GM-088187NIGMS NIH HHS R01 GM088187
6 · The paper itself

Abstract

Among the growing number of membrane protein structures in the Protein Data Bank, there are many transmembrane domains that appear to be native-like; at the same time, there are others that appear to have less than complete native-like character. Hence, there is an increasing need for validation tools that distinguish native-like from non-native-like structures. Membrane mimetics used in protein structural characterizations differ in numerous physicochemical properties from native membranes and provide many opportunities for introducing non-native-like features into membrane protein structures. One possible approach for validating membrane protein structures is based on the use of glycine residues in transmembrane domains. Here, we have reviewed the membrane protein structure database and identified a set of benchmark proteins that appear to be native-like. In these structures, conserved glycine residues rarely face the lipid interstices, and many of them participate in close helix-helix packing. Glycine-based validation allowed the identification of non-native-like features in several membrane proteins and also shows the potential for verifying the native-like character for numerous other membrane protein structures.

Indexed as

Cell MembraneConserved SequenceGlycineHumansMembrane ProteinsProtein Structure, SecondaryProtein Structure, TertiaryGlycineMembrane Proteins

Identifiers

PMID22650985
PMCPMC3426646
OpenAlexW1967586709

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.