Evidence map›Paper›PMID 28375742›Full record

ReviewAnnual review of biochemistry2017

How α-Helical Motifs Form Functionally Diverse Lipid-Binding Compartments.

Lucy Malinina, Dinshaw J Patel, Rhoderick E Brown

Abstract readReview
In one paragraph

Review in Annual review of biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Human Saposin B Ligand Binding and Presentation to α-Galactosidase A.bioRxiv : the preprint server for biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Characterization of CNPY5 and its family members.Protein science : a publication of the Protein Society · 2019
    Article
  10. Article
  11. Upregulation of human glycolipid transfer protein (GLTP) induces necroptosis in colon carcinoma cells.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
    Article
  12. Article
  13. Article
  14. A Comparative Study of Human Saposins.Molecules (Basel, Switzerland) · 2018
    Article
  15. Article
  16. 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.

Lucy MalininaThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912; email: lucy@hi.umn.edu , reb@umn.edu.
Dinshaw J PatelStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065; email: pateld@mskcc.org.
Rhoderick E BrownThe Hormel Institute, University of Minnesota, Austin, Minnesota 55912; email: lucy@hi.umn.edu , reb@umn.edu.

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
GLYCOLIPID TRANSFER--REGULATION BY MEMBRANE INTERFACESR01GM045928 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI BROWN, RHODERICK E · 1992 to 2014
$4.8M
The functional role of the cPLA2alpha/C1P interaction in sepsis resolutionR01HL125353 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI BROWN, RHODERICK E, CHALFANT, CHARLES E. · 2014 to 2018
$4.0M
MOLECULAR BASIS OF GLYCOSPHINGOLIPID BINDING SPECIFICITYR01CA121493 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI PATEL, DINSHAW J · 2006 to 2010
$1.2M
NCI NIH HHS P30 CA008748NCI NIH HHS R01 CA121493NHLBI NIH HHS R01 HL125353NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Lipids are produced site-specifically in cells and then distributed nonrandomly among membranes via vesicular and nonvesicular trafficking mechanisms. The latter involves soluble amphitropic proteins extracting specific lipids from source membranes to function as molecular solubilizers that envelope their insoluble cargo before transporting it to destination sites. Lipid-binding and lipid transfer structural motifs range from multi-β-strand barrels, to β-sheet cups and baskets covered by α-helical lids, to multi-α-helical bundles and layers. Here, we focus on how α-helical proteins use amphipathic helical layering and bundling to form modular lipid-binding compartments and discuss the functional consequences. Preformed compartments generally rely on intramolecular disulfide bridging to maintain conformation (e.g., albumins, nonspecific lipid transfer proteins, saposins, nematode polyprotein allergens/antigens). Insights into nonpreformed hydrophobic compartments that expand and adapt to accommodate a lipid occupant are few and provided mostly by the three-layer, α-helical ligand-binding domain of nuclear receptors. The simple but elegant and nearly ubiquitous two-layer, α-helical glycolipid transfer protein (GLTP)-fold now further advances understanding.

Indexed as

AlbuminsAllergensAnimalsAntigensBinding SitesBiological TransportCarrier ProteinsGene ExpressionHumansLipid MetabolismLipidsModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein DomainsAlbuminsAllergensAntigensCarrier ProteinsLipidslipid transfer proteinsterol carrier proteinsalbuminsfixed versus expandable hydrophobic pocketsGLTP-foldlipid headgroup recognition centersnematode polyprotein allergens/antigensnonspecific lipid transfer proteinsnuclear receptor ligand-binding domainsprotein helical layering/bundlingsaposinssphingolipid transfer proteins

Identifiers

PMID28375742
PMCPMC7935428

What OpenQuestion holds

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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.