Evidence map›Paper›PMID 12391320›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

An approach to membrane protein structure without crystals.

Paul L Sorgen, Yonglin Hu, Lan Guan, H Ronald Kaback, Mark E Girvin

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Gate-controlled proton diffusion and protonation-induced ratchet motion in the stator of the bacterial flagellar motor.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  2. Proton-coupled dynamics in lactose permease.Structure (London, England : 1993) · 2012
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Comparison of human solute carriers.Protein science : a publication of the Protein Society · 2010
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Site-directed alkylation and the alternating access model for LacY.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  16. Article
  17. Amide vibrations are delocalized across the hydrophobic interface of a transmembrane helix dimer.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  18. Article
  19. Lessons from lactose permease.Annual review of biophysics and biomolecular structure · 2006
    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

5 authors.

Paul L SorgenBiochemistry Department, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Yonglin Hu
Lan Guan
H Ronald Kaback
Mark E Girvin

Funding

NEW APPROACHES TO MEMBRANE PROTEIN STRUCTURESR01DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 1996 to 2014
$5.2M
STRUCTURE AND FOLDING OF SUBUNIT C OF THE FLFO ATPASER01GM055371 · NIGMS · YESHIVA UNIVERSITY · PI GIRVIN, MARK E. · 1997 to 2004
$1.5M
Dynamics of the Lactose Permease of Escherichia ColiR56DK051131 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI KABACK, HOWARD RONALD · 2015 to 2015
$154k
BUILDING TOWARDS A MEMBRANE PROTEIN COMPLEXF32GM020504 · NIGMS · YESHIVA UNIVERSITY · PI SORGEN, PAUL L · 2000 to 2002
$119k
NIDDK NIH HHS DK51131:06NIDDK NIH HHS R01 DK051131NIDDK NIH HHS R56 DK051131NIGMS NIH HHS F32 GM020504NIGMS NIH HHS F32 GM20504NIGMS NIH HHS GM55371NIGMS NIH HHS R01 GM055371
6 · The paper itself

Abstract

The lactose permease of Escherichia coli catalyzes coupled translocation of galactosides and H(+) across the cell membrane. It is the best-characterized member of the Major Facilitator Superfamily, a related group of membrane proteins with 12 transmembrane domains that mediate transport of various substrates across cell membranes. Despite decades of effort and their functional importance in all kingdoms of life, no high-resolution structures have been solved for any member of this family. However, extensive biochemical, genetic, and biophysical studies on lactose permease have established its transmembrane topology, secondary structure, and numerous interhelical contacts. Here we demonstrate that this information is sufficient to calculate a structural model at the level of helix packing or better.

Indexed as

Escherichia coli ProteinsMonosaccharide Transport ProteinsSymportersBinding SitesCrystallizationEscherichia coliMembrane Transport ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryEscherichia coli Proteinslactose permeaseLacY protein, E coliMembrane Transport ProteinsMonosaccharide Transport ProteinsSymporters

Identifiers

PMID12391320
PMCPMC137832

What OpenQuestion holds

Textmetadata
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.