Evidence map›Paper›PMID 26062601›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2015

New aminopeptidase from "microbial dark matter" archaeon.

Karolina Michalska, Andrew D Steen, Gekleng Chhor, Michael Endres, Austen T Webber, Jordan Bird, Karen G Lloyd, Andrzej Joachimiak

Open access · bronzeAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

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  10. Growth of sedimentaryProceedings of the National Academy of Sciences of the United States of America · 2018
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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

8 authors at 3 institutions in 1 country.

Karolina Michalska*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Andrew D Steen*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Gekleng Chhor*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Michael Endres*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Austen T Webber*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Jordan Bird*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Karen G Lloyd*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA.
Andrzej Joachimiak*Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois, USA; Department of Microbiology and Department of Earth and Planetary Sciences, University of Tennessee, Knoxville, Tennessee, USA; and Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA andrzejj@anl.gov.
University of Tennessee at Knoxville · USArgonne National Laboratory · USJoint Center for Structural Genomics · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS GM094585NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

Marine sediments host a large population of diverse, heterotrophic, uncultured microorganisms with unknown physiologies that control carbon flow through organic matter decomposition. Recently, single-cell genomics uncovered new key players in these processes, such as the miscellaneous crenarchaeotal group. These widespread archaea encode putative intra- and extracellular proteases for the degradation of detrital proteins present in sediments. Here, we show that one of these enzymes is a self-compartmentalizing tetrameric aminopeptidase with a preference for cysteine and hydrophobic residues at the N terminus of the hydrolyzed peptide. The ability to perform detailed characterizations of enzymes from native subsurface microorganisms, without requiring that those organisms first be grown in pure culture, holds great promise for understanding key carbon transformations in the environment as well as identifying new enzymes for biomedical and biotechnological applications.

Indexed as

AminopeptidasesAquatic OrganismsArchaeaArchaeal ProteinsAminopeptidasesArchaeal Proteinscarbon cycledetrital proteinsmarine sedimentssingle-cell genomics

Identifiers

PMID26062601
PMCPMC4550370
OpenAlexW2102281041

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.