Evidence map›Paper›PMID 23084777›Full record

ArticleGenomics, proteomics & bioinformatics2012

Homepeptide repeats: implications for protein structure, function and evolution.

Muthukumarasamy Uthayakumar, Bowdadu Benazir, Sanjeev Patra, Marthandan Kirti Vaishnavi, Manickam Gurusaran, Kanagarajan Sureka, Jeyaraman Jeyakanthan, Kanagaraj Sekar

Abstract read
In one paragraph

Article in Genomics, proteomics & bioinformatics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
  2. Identification and Analysis of Long Repeats of Proteins at the Domain Level.Frontiers in bioengineering and biotechnology · 2019
    Article
  3. Article
  4. Article
  5. Article
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.

Muthukumarasamy UthayakumarSupercomputer Education and Research Centre, Indian Institute of Science, Bangalore, India.
Bowdadu Benazir
Sanjeev Patra
Marthandan Kirti Vaishnavi
Manickam Gurusaran
Kanagarajan Sureka
Jeyaraman Jeyakanthan
Kanagaraj Sekar

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Analysis of protein sequences from Mycobacterium tuberculosis H37Rv (Mtb H37Rv) was performed to identify homopeptide repeat-containing proteins (HRCPs). Functional annotation of the HRCPs showed that they are preferentially involved in cellular metabolism. Furthermore, these homopeptide repeats might play some specific roles in protein-protein interaction. Repeat length differences among Bacteria, Archaea and Eukaryotes were calculated in order to identify the conservation of the repeats in these divergent kingdoms. From the results, it was evident that these repeats have a higher degree of conservation in Bacteria and Archaea than in Eukaryotes. In addition, there seems to be a direct correlation between the repeat length difference and the degree of divergence between the species. Our study supports the hypothesis that the presence of homopeptide repeats influences the rate of evolution of the protein sequences in which they are embedded. Thus, homopeptide repeat may have structural, functional and evolutionary implications on proteins.

Indexed as

Amino AcidsAmino Acid SequenceArchaeal ProteinsBacterial ProteinsBiological EvolutionEscherichia coliEvolution, MolecularHumansModels, MolecularMycobacterium tuberculosisPeptidesProtein ConformationProteinsProtein Structure, TertiaryRepetitive Sequences, Amino AcidSequence Analysis, ProteinAmino AcidsArchaeal ProteinsBacterial ProteinsPeptidesProteins

Identifiers

PMID23084777
PMCPMC5054710

What OpenQuestion holds

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LicenceCC BY-NC-SA
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Registered trials

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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.