Evidence map›Paper›PMID 35560044›Full record

ArticlePloS one2022

Genome-wide exploration of sugar transporter (sweet) family proteins in Fabaceae for Sustainable protein and carbon source.

Nisha Singh, Megha Ujinwal, Sapna Langyan, R Z Sayyed, Hesham Ali El Enshasy, Ahmed A Kenawy

RetractedOpen access · goldAbstract readRetracted Publication
In one paragraph

Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 3 countries.

Nisha SinghICAR-National Institute for Plant Biotechnology, New Delhi, India.ORCID 0000-0002-1950-815X
Megha UjinwalICAR-National Institute for Plant Biotechnology, New Delhi, India.
Sapna LangyanICAR-National Bureau of Plant Genetic Resources (NBPGR), New Delhi, India.
R Z SayyedDepartment of Microbiology, PSGVP Mandal's S I Patil Arts, G B Patel Science and STKVS Commerce College, Shahada, India.
Hesham Ali El EnshasyInstitute of Bioproduct Development (IBD), Universiti Teknologi Malaysia (UTM), Johor, Malayisa.
Ahmed A KenawyCity of Scientific Research and Technology Applications (SRTA), New Burg Al Arab, Alexandria, Egypt.
City of Scientific Research and Technological Applications · EGNational Research Centre on Plant Biotechnology · ING.S. Science, Arts And Commerce College · INNational Bureau of Plant Genetic Resources · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sugar transporter proteins (STPs) are membrane proteins required for sugar transport throughout cellular membranes. They plays an imperative role in sugar transmission across the plant and determinants of crop yield. However, the analysis of these important STPs Sugars Will Eventually be Exported Transporters (SWEET) family in legumes is still not well-documented and remains unclear. Therefore, the in-silico analysis of STPs has been performed to unravel their cellular, molecular, and structural composition in legume species. This study conducted a systematic search for STPs in Cajanus cajan using the Blastp algorithm to understand its molecular basis. Here, we performed a comprehensive analysis of 155 identified SWEET proteins across 12 legumes species, namely (Cajanus cajan, Glycine max, Vigna radiate, Vigna angularis, Medicago truncatula, Lupinus angustifolius, Glycine soja, Spatholobus suberectus, Cicer arietinum, Arachis ipaensis, Arachis hypogaea, Arachis duranensis). The amino acid composition and motif analysis revealed that SWEET proteins are rich in essential amino acids such as leucine, valine, isoleucine, phenylalanine, and serine while less profuse in glutamine, tryptophan, cysteine, and histidine. A total of four main conserved motifs of SWEET proteins are also highly abundant in these amino acids. The present study deciphered the details on primary physicochemical properties, secondary, tertiary structure, and phylogenetic analysis of SWEETs protein. Majorities of SWEET proteins (72.26%) are in stable form with an average instability index of 36.5%, and it comprises a higher fraction of positively charged amino acid Arg + Lys residues. Secondary structure analysis shown that these proteins are richer in alpha-helix (40%) than extended strand (30%) and random coil (25%), respectively. Furthermore, to infer their mechanism at a structural and functional level which play an essential roles in growth, development, and stress responses. This study will be useful to examine photosynthetic productivity, embryo sugar content, seed quality, and yield enhancement in Fabaceae for a sustainable source of essential amino acids and carbon source.

Indexed as

CajanusFabaceaeMedicago truncatulaAmino AcidsAmino Acids, EssentialArachisCarbonGene Expression Regulation, PlantPhylogenyPlant ProteinsSugarsAmino AcidsAmino Acids, EssentialCarbonPlant ProteinsSugars

Identifiers

PMID35560044
PMCPMC9106169
OpenAlexW4280582624

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.