Evidence map›Paper›PMID 34801557›Full record

ArticleThe Journal of biological chemistry2021

Malonyl-acyl carrier protein decarboxylase activity promotes fatty acid and cell envelope biosynthesis in Proteobacteria.

Sarah G Whaley, Christopher D Radka, Chitra Subramanian, Matthew W Frank, Charles O Rock

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Functional disparities of malonyl-ACP decarboxylase betweenApplied and environmental microbiology · 2025
    Article
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  7. Article
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  11. Cross-talk between phospholipid synthesis and peptidoglycan expansion by a cell wall hydrolase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. 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 at 1 institution in 1 country.

Sarah G WhaleyDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Christopher D RadkaDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Chitra SubramanianDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Matthew W FrankDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA.
Charles O RockDepartment of Infectious Diseases, St Jude Children's Research Hospital, Memphis, Tennessee, USA. Electronic address: charles.rock@stjude.org.
St. Jude Children's Research Hospital · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
REGULATION OF LIPID METABOLISM IN E COLIR01GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 1985 to 2022
$9.2M
REGULATION OF LIPID METABOLISM IN BACTERIAR37GM034496 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ROCK, CHARLES O · 2001 to 2010
$5.7M
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
$529k
NCI NIH HHS P30 CA021765NIGMS NIH HHS P41 GM103622NIGMS NIH HHS R01 GM034496NIGMS NIH HHS R37 GM034496NIH HHS S10 OD018090
6 · The paper itself

Abstract

Bacterial fatty acid synthesis in Escherichia coli is initiated by the condensation of an acetyl-CoA with a malonyl-acyl carrier protein (ACP) by the β-ketoacyl-ACP synthase III enzyme, FabH. E. coli ΔfabH knockout strains are viable because of the yiiD gene that allows FabH-independent fatty acid synthesis initiation. However, the molecular function of the yiiD gene product is not known. Here, we show the yiiD gene product is a malonyl-ACP decarboxylase (MadA). MadA has two independently folded domains: an amino-terminal N-acetyl transferase (GNAT) domain (MadA

Indexed as

Acyl Carrier ProteinCell WallEscherichia coliEscherichia coli ProteinsFatty AcidsFatty Acid Synthase, Type IIShewanellaacpP protein, E coliAcyl Carrier ProteinEscherichia coli ProteinsFatty AcidsFatty Acid Synthase, Type IIEscherichia coliFabHfatty acid synthesisGlmUmalonyl-ACP decarboxylase

Identifiers

PMID34801557
PMCPMC8666670
OpenAlexW3213933564

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.