Evidence map›Paper›PMID 23963991›Full record

ArticleMolecular and cellular biochemistry2013

Structure-activity relationships of αs-casein peptides with multifunctional biological activities.

Srinivas Sistla

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular and cellular biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 26 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Srinivas SistlaDepartment of Protein Chemistry and Technology, Central Food Technological Research Institute (CSIR), Mysore, 570020, Karnataka, India, sistlasrinivas@gmail.com.
Central Food Technological Research Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multifunctional bioactive peptides have a wider role in modulating physiological functions and possess multiple biological activities. Peptides from bovine milk with sequences QKALNEINQF [p10] and TKKTKLTEEEKNRL [p14] from α-S2 casein f (79-88) and α-S2 casein f (148-161) were identified to be having multifunctional biological activities and were synthesized. These synthesized peptides show various biological activities like angiotensin-converting enzyme inhibition, prolyl endopeptidase inhibition, antioxidant, and antimicrobial activities. The mode of antimicrobial mechanism was studied and p10 shows depolarization of cell membrane, whereas p14 was found to display DNA-binding activity. Structural studies envisaged backbone flexibility, for differences in their mode of action. Peptide structure function studies were correlated to understand their multifunctional biological activity.

Indexed as

Angiotensin-Converting Enzyme InhibitorsAnimalsAntimicrobial Cationic PeptidesAntioxidantsBacillus cereusCaseinsDNA-Binding ProteinsHelicobacter pyloriListeria monocytogenesMicrobial Sensitivity TestsMilkProlyl OligopeptidasesProtein Structure, SecondarySerine EndopeptidasesStaphylococcus aureusStructure-Activity RelationshipAngiotensin-Converting Enzyme InhibitorsAntimicrobial Cationic PeptidesAntioxidantsCaseinsDNA-Binding ProteinsProlyl OligopeptidasesSerine Endopeptidases

Identifiers

PMID23963991
OpenAlexW2461121283

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.