Evidence map›Paper›PMID 15378387›Full record

ReviewJournal of industrial microbiology & biotechnology2004

Acinetobacter lipases: molecular biology, biochemical properties and biotechnological potential.

Erick A Snellman, Rita R Colwell

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Journal of industrial microbiology & biotechnology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

17 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. UnveilingMicroorganisms · 2025
    Article
  3. Distinct codon usage signatures reflecting evolutionary and pathogenic adaptation in the Acinetobacter baumannii complex.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Article
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  14. Review
  15. Article
  16. Process optimization for production and purification of a thermostable, organic solvent tolerant lipase from Acinetobacter sp. AU07.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
    Article
  17. Draft genome sequence of phenol degrading Acinetobacter sp. Strain V2, isolated from oil contaminated soil.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]
    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

2 authors at 1 institution in 1 country.

Erick A SnellmanCenter of Marine Biotechnology, University of Maryland Biotechnology Institute, Baltimore, MD 21202, USA.
Rita R Colwell
University of Maryland, Baltimore · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipases (EC 3.1.1.3) have received increased attention recently, evidenced by the increasing amount of information about lipases in the current literature. The renewed interest in this enzyme class is due primarily to investigations of their role in pathogenesis and their increasing use in biotechnological applications. Also, many microbial lipases are available as commercial products, the majority of which are used in detergents, cosmetic production, food flavoring, and organic synthesis. Lipases are valued biocatalysts because they act under mild conditions, are highly stable in organic solvents, show broad substrate specificity, and usually show high regio- and/or stereo-selectivity in catalysis. A number of lipolytic strains of Acinetobacter have been isolated from a variety of sources and their lipases possess many biochemical properties similar to those that have been developed for biotechnological applications. This review discusses the biology of lipase expression in Acinetobacter, with emphasis on those aspects relevant to potential biotechnology applications.

Indexed as

AcinetobacterAmino Acid SequenceFermentationGene Expression Regulation, BacterialIndustrial MicrobiologyLipaseMolecular Sequence DataPhylogenySequence AlignmentSequence Homology, Amino AcidLipase

Identifiers

PMID15378387
OpenAlexW1978480841

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.