Evidence map›Paper›PMID 9303296›Full record

ArticleThe EMBO journal1997

Mutagenesis of phospholipase D defines a superfamily including a trans-Golgi viral protein required for poxvirus pathogenicity.

T C Sung, R L Roper, Y Zhang, S A Rudge, R Temel, S M Hammond, A J Morris, B Moss, J Engebrecht, M A Frohman

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

116 citing papers in PubMed, 356 citations in OpenAlex.

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  16. Crystal Structure of a Phospholipase D from the Plant-Associated BacteriaInternational journal of molecular sciences · 2021
    Article
  17. Article
  18. Review
  19. Review
  20. Studies on the mechanism of general anesthesia.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

56 more citing papers are in PubMed but not listed here.

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

10 authors at 1 institution in 1 country.

T C SungDepartment of Pharmacological Sciences, SUNY at Stony Brook, NY 11794-8651, USA.
R L Roper
Y Zhang
S A Rudge
R Temel
S M Hammond
A J Morris
B Moss
J Engebrecht
M A Frohman
Stony Brook University · US

Funding

Role of Lipid Phosphatases in Cholesterol and Triglyceride SynthesisR01GM050388 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI MORRIS, ANDREW J · 1994 to 2011
$2.7M
EXPRESSION AND FUNCTION OF MAMMALIAN GASTRULATION GENESR01HD029758 · NICHD · STATE UNIVERSITY NEW YORK STONY BROOK · PI FROHMAN, MICHAEL A · 1993 to 1997
–
GENETIC ANALYSIS OF MEIOTIC CHROMOSOME SEGREGATIONR29GM048639 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI ENGEBRECHT, JOANNE · 1993 to 1998
–
NICHD NIH HHS HD29758NIGMS NIH HHS GM4863903NIGMS NIH HHS GM50388
6 · The paper itself

Abstract

Phospholipase D (PLD) genes are members of a superfamily that is defined by several highly conserved motifs. PLD in mammals has been proposed to play a role in membrane vesicular trafficking and signal transduction. Using site-directed mutagenesis, 25 point mutants have been made in human PLD1 (hPLD1) and characterized. We find that a motif (HxKxxxxD) and a serine/threonine conserved in all members of the PLD superfamily are critical for PLD biochemical activity, suggesting a possible catalytic mechanism. Functional analysis of catalytically inactive point mutants for yeast PLD demonstrates that the meiotic phenotype ensuing from PLD deficiency in yeast derives from a loss of enzymatic activity. Finally, mutation of an HxKxxxxD motif found in a vaccinia viral protein expressed in the Golgi complex results in loss of efficient vaccinia virus cell-to-cell spreading, implicating the viral protein as a member of the superfamily and suggesting that it encodes a lipid modifying or binding activity. The results suggest that vaccinia virus and hPLD1 may act through analogous mechanisms to effect viral cellular egress and vesicular trafficking, respectively.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCatalysisConserved SequenceCOS CellsEvolution, MolecularHumansLysineModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedPhospholipase DPoint MutationSaccharomyces cerevisiaeSequence Homology, Amino AcidLysinePhospholipase DViral Proteins

Identifiers

PMID9303296
PMCPMC1170078
OpenAlexW2104302589

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.