Evidence map›Paper›PMID 15519306›Full record

ReviewBiochimica et biophysica acta2004

Diversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.

William Dowhan, Eugenia Mileykovskaya, Mikhail Bogdanov

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020
    Review
  9. An essential role for cardiolipin in the stability and function of the mitochondrial calcium uniporter.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. The Influence of Dietary Fat Source on Life Span in Calorie Restricted Mice.The journals of gerontology. Series A, Biological sciences and medical sciences · 2015
    Article
  16. Review
  17. Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Protein science : a publication of the Protein Society · 2015
    Review
  18. Targeting of the hydrophobic metabolome by pathogens.Traffic (Copenhagen, Denmark) · 2015
    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

3 authors at 2 institutions in 1 country.

William DowhanDepartment of Biochemistry and Molecular Biology, University of Texas-Houston, Medical School, Suite 6.200, 6431 Fannin St., Houston, TX, 77030, USA. william.dowhan@uth.tmc.edu
Eugenia Mileykovskaya
Mikhail Bogdanov
The University of Texas Health Science Center at Houston · USTexas Medical Center · US

Funding

Structure and Function in Membrane ProteinsR37GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 2005 to 2015
$5.4M
PHOSPHOLIPIDS AND MITOCHONDRIAL FUNCTIONR01GM056389 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 1998 to 2011
$4.2M
STRUCTURE/FUNCTION OF MEMBRANE PROTEINSR01GM020478 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DOWHAN, WILLIAM · 1985 to 2004
$1.8M
KARYOPHERIN X, A NOVEL TRANSPORT RECEPTORF32GM020478 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI PLAFKER, SCOTT M · 2000 to 2000
$38k
NIGMS NIH HHS F32 GM020478NIGMS NIH HHS GM20478NIGMS NIH HHS GM56389NIGMS NIH HHS R01 GM020478NIGMS NIH HHS R01 GM056389NIGMS NIH HHS R37 GM020478
6 · The paper itself

Abstract

The diversity in structures and physical properties of lipids provides a wide variety of possible interactions with proteins that affect their assembly, organization, and function either at the surface of or within membranes. Because lipids have no catalytic activity, it has been challenging to define many of their precise functions in vivo in molecular terms. Those processes responsive to lipids are attuned to the native lipid environment for optimal function, but evidence that lipids with similar properties or even detergents can sometimes partially replace the natural lipid environment has led to uncertainty as to the requirement for specific lipids. The development of strains of microorganisms in which membrane lipid composition can be genetically manipulated in viable cells has provided a set of reagents to probe lipid functions. These mutants have uncovered previously unrecognized roles for lipids and provided in vivo verification for putative functions described in vitro. In this review, we summarize how these reagent strains have provided new insight into the function of lipids. The role of specific lipids in membrane protein folding and topological organization is reviewed. The evidence is summarized for the involvement of anionic lipid-enriched domains in the organization of amphitropic proteins on the membrane surface into molecular machines involved in DNA replication and cell division.

Indexed as

Bacterial ProteinsFungal ProteinsMacromolecular SubstancesMembrane LipidsMembrane ProteinsProtein BindingBacterial ProteinsFungal ProteinsMacromolecular SubstancesMembrane LipidsMembrane Proteins

Identifiers

PMID15519306
PMCPMC4109649
OpenAlexW2069234108

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.