Evidence map›Paper›PMID 34765745›Full record

ArticleBiochemistry and biophysics reports2021

Purification and characterization of recombinant FAD synthetase from

Nirupama Puvvada, Sridhar Gunde, Ch Venkata Ramana Devi, Raghu Gogada

Open access · goldAbstract read
In one paragraph

Article in Biochemistry and biophysics reports, 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
–field-weighted citation impact, top 90% 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, 0 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 2 institutions in 1 country.

Nirupama PuvvadaDepartment of Biochemistry, Osmania University, Hyderabad, India.
Sridhar GundeDepartment of Zoology, University College of Science, Osmania University, Hyderabad, 500 007, India.
Ch Venkata Ramana DeviDepartment of Biochemistry, Osmania University, Hyderabad, India.
Raghu GogadaDepartment of Biochemistry, Osmania University, Hyderabad, India.
Osmania University · INCenturion University of Technology and Management · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FAD Synthetase (FADS) [EC 2.7.7.2], the second enzyme in flavin cofactor biosynthetic pathway converts FMN to FAD, plays an important role in many redox reactions.

Indexed as

Enzyme kineticsFlavo proteinsIntrinsic fluorescence

Identifiers

PMID34765745
PMCPMC8571487
OpenAlexW3208565405

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.