Evidence map›Paper›PMID 19825625›Full record

ArticleMolecular plant2009

The interaction of spinach nitrite reductase with ferredoxin: a site-directed mutation study.

Masakazu Hirasawa, Jatindra N Tripathy, Ramasamy Somasundaram, Michael K Johnson, Megha Bhalla, James P Allen, David B Knaff

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant, 2009. 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
1.4field-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

10 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Remembering David B. Knaff (1941-2016).Photosynthesis research · 2016
    Article
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  9. Article
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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

7 authors at 3 institutions in 1 country.

Masakazu HirasawaDepartment of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA.
Jatindra N Tripathy
Ramasamy Somasundaram
Michael K Johnson
Megha Bhalla
James P Allen
David B Knaff
Texas Tech University · USUniversity of Georgia · USArizona State University · US

Funding

Assembly of Biological Iron-Sulfur ClustersR01GM062524 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI JOHNSON, MICHAEL K. · 2001 to 2012
$2.7M
NIGMS NIH HHS GM62524NIGMS NIH HHS R01 GM062524
6 · The paper itself

Abstract

A series of site-directed mutants of the ferredoxin-dependent spinach nitrite reductase has been characterized and several amino acids have been identified that appear to be involved in the interaction of the enzyme with ferredoxin. In a complementary study, binding constants to nitrite reductase and steady-state kinetic parameters of site-directed mutants of ferredoxin were determined in an attempt to identify ferredoxin amino acids involved in the interaction with nitrite reductase. The results have been interpreted in terms of an in-silico docking model for the 1:1 complex of ferredoxin with nitrite reductase.

Indexed as

Mutagenesis, Site-DirectedBinding SitesConserved SequenceFerredoxin-Nitrite ReductaseFerredoxinsMutationNitrite ReductasesSequence AlignmentSequence Homology, Amino AcidSpinacia oleraceaFerredoxin-Nitrite ReductaseFerredoxinsNitrite Reductases

Identifiers

PMID19825625
PMCPMC2902899
OpenAlexW2071632610

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.