Evidence map›Paper›PMID 26244839›Full record

ArticleStructure (London, England : 1993)2015

Catalytic Mechanism of Eukaryotic Neutral Ceramidase.

Lucy Malinina, Rhoderick E Brown

Open access · bronzeAbstract readComment
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Lucy MalininaHormel Institute, University of Minnesota, Austin, MN 55912, USA. Electronic address: lucy@hi.umn.edu.
Rhoderick E BrownHormel Institute, University of Minnesota, Austin, MN 55912, USA. Electronic address: reb@umn.edu.
University of Minnesota · US

Funding

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 R01 CA121493NHLBI NIH HHS R01 HL125353NIGMS NIH HHS R01 GM045928
6 · The paper itself

Abstract

Neutral ceramidases are key enzymes of sphingolipid metabolism that hydrolyze the fatty acyl/sphingosine amide linkage of ceramide at neutral pH. In this issue of Structure, Airola et al. (2015) present the first crystal structure of human nCDase and show how complexation with phosphate supports a new catalytic mechanism for Zn-dependent amidases while providing a structurally based explanation for ceramide specificity.

Indexed as

AnimalsCeramidesHumansLysophospholipidsNeutral CeramidaseSphingosineCeramidesLysophospholipidsNeutral CeramidaseSphingosine

Identifiers

PMID26244839
PMCPMC8318198
OpenAlexW2159796698

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.