Evidence map›Paper›PMID 10548543›Full record

ArticleThe Biochemical journal1999

Identification and molecular characterization of acyl-CoA synthetase in human erythrocytes and erythroid precursors.

K T Malhotra, K Malhotra, B H Lubin, F A Kuypers

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 40 citations in OpenAlex.

  1. Acyl-CoA synthetases as regulators of brain phospholipid acyl-chain diversity.Prostaglandins, leukotrienes, and essential fatty acids · 2020
    Review
  2. Article
  3. Acyl-CoA synthetase 6 enriches the neuroprotective omega-3 fatty acid DHA in the brain.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Article
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  11. Mammalian long-chain acyl-CoA synthetases.Experimental biology and medicine (Maywood, N.J.) · 2008
    Review
  12. Article
  13. Article
  14. 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

4 authors at 1 institution in 1 country.

K T MalhotraChildren's Hospital, Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, CA 94609, USA.
K Malhotra
B H Lubin
F A Kuypers
Martin Luther King, Jr. Multi-Service Ambulatory Care Center · US

Funding

YEAST MEMBRANE CYTOSKELETONP01DK032094 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI NARLA, MOHANDAS · 1987 to 2021
$26.7M
ZIDOVUDINE &LAMIVUDINE &NEVIRAPINE COMBINATION THERAPY IN HIV 1 INFM01RR001271 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KESSLER, DAVID A · 1985 to 2006
$22.7M
SIGNIFICANCE OF MEMBRANE PHOSPHOLIPID ASYMMETRYR01HL027059 · NHLBI · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI LUBIN, BERTRAM HAROLD · 1985 to 1999
–
NCRR NIH HHS MO1RR01271NHLBI NIH HHS HL27059NIDDK NIH HHS DK 32094
6 · The paper itself

Abstract

Full-length cDNA species encoding two forms of acyl-CoA synthetase from a K-562 human erythroleukaemic cell line were cloned, sequenced and expressed. The first form, named long-chain acyl-CoA synthetase 5 (LACS5), was found to be a novel, unreported, human acyl-CoA synthetase with high similarity to rat brain ACS2 (91% identical). The second form (66% identical with LACS5) was 97% identical with human liver LACS1. The LACS5 gene encodes a highly expressed 2.9 kb mRNA transcript in human haemopoietic stem cells from cord blood, bone marrow, reticulocytes and fetal blood cells derived from fetal liver. An additional 6.3 kb transcript is also found in these erythrocyte precursors; 2.9 and 9.6 kb transcripts of LACS5 are found in human brain, but transcripts are virtually absent from human heart, kidney, liver, lung, pancreas, spleen and skeletal muscle. The 78 kDa expressed LACS5 protein used the long-chain fatty acids palmitic acid, oleic acid and arachidonic acid as substrates. Antibodies directed against LACS5 cross-reacted with erythrocyte membranes. We conclude that early erythrocyte precursors express at least two different forms of acyl-CoA synthetase and that LACS5 is present in mature erythrocyte plasma membranes.

Indexed as

AdultAmino Acid SequenceAnimalsBase SequenceCoenzyme A LigasesDNA, ComplementaryDNA PrimersErythrocyte MembraneErythrocytesFetal BloodHematopoietic Stem CellsHumansInfant, NewbornIn Vitro TechniquesK562 CellsMolecular Sequence DataCoenzyme A LigasesDNA, ComplementaryDNA PrimersRNA, Messenger

Identifiers

PMID10548543
PMCPMC1220623
OpenAlexW2046118162

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.