Evidence map›Paper›PMID 34292546›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Expression, Isolation, and Characterization of Vanadium Nitrogenase from Azotobacter vinelandii.

Katharina Parison, Jakob Gies-Elterlein, Christian Trncik, Oliver Einsle

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
1.9field-weighted citation impact, top 19% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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.

Katharina ParisonInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Jakob Gies-ElterleinInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Christian TrncikInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany.
Oliver EinsleInstitut für Biochemie, Albert-Ludwigs-Universität Freiburg, Freiburg, Germany. einsle@bio.chemie.uni-freiburg.de.
University of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nitrogenases are the sole enzymes known to mediate biological nitrogen fixation, an essential process for sustaining life on earth. Among the three known variants, molybdenum nitrogenase is the best-studied to date. Recent work on the alternative vanadium nitrogenase provided important insights into the mechanism of nitrogen fixation since this enzyme differs from its molybdenum counterpart in some important aspects. Here, we present a protocol to obtain unmodified vanadium nitrogenase in high yield and purity from the paradigmatic diazotroph Azotobacter vinelandii, including procedures for cell cultivation, purification, and protein characterization.

Indexed as

Azotobacter vinelandiiMolybdenumNitrogenaseNitrogen FixationMolybdenumNitrogenaseAlternative nitrogenaseAnoxic protein biochemistryAzotobacter vinelandiiBiological nitrogen fixationFe proteinNitrogen fixationProtein expressionProtein isolationProtein purificationVanadiumVanadium nitrogenaseVFe protein

Identifiers

PMID34292546
OpenAlexW3185063666

What OpenQuestion holds

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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.