Evidence map›Paper›PMID 12543672›Full record

ArticleAntimicrobial agents and chemotherapy2003

MUC7 20-Mer: investigation of antimicrobial activity, secondary structure, and possible mechanism of antifungal action.

Libuse A Bobek, Hongsa Situ

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

33 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The Contribution of Human Antimicrobial Peptides to Fungi.International journal of molecular sciences · 2025
    Review
  6. Review
  7. Review
  8. Article
  9. ThePolymers · 2024
    Review
  10. Article
  11. Article
  12. Therapeutic Effect of an Antibody-Derived Peptide in aInternational journal of molecular sciences · 2021
    Article
  13. Article
  14. Review
  15. New Genes and Functional Innovation in Mammals.Genome biology and evolution · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Libuse A BobekDepartment of Oral Biology, University at Buffalo, The State University of New York, Buffalo, New York 14214, USA. lbobek@acsu.buffalo.edu
Hongsa Situ
University at Buffalo, State University of New York · US

Funding

SALIVARY PROTEINS--MOLECULAR STUDY OF STRUCTURE/FUNCTIONR01DE009820 · NIDCR · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI BOBEK, LIBUSE ANNA · 1992 to 2007
$1.7M
NIDCR NIH HHS DE09820NIDCR NIH HHS R01 DE009820
6 · The paper itself

Abstract

This study was aimed at examining the spectrum of antimicrobial activity of MUC7 20-mer (N-LAHQKPFIRKSYKCLHKRCR-C; residues 32 to 51 of MUC7, the low-molecular-weight human salivary mucin, comprised of 357 residues) and comparing its antifungal properties to those of salivary histatin 5 (Hsn-5). We also examined the secondary structure of the 20-mer and the possible mechanism of its antifungal action. Our results showed that MUC7 20-mer displays potent killing activity against a variety of fungi and both gram-positive and gram-negative bacteria at micromolar concentrations. Time-dependent killing of Candida albicans and Cryptococcus neoformans by MUC7 20-mer and Hsn-5 indicated differences in killing rates between MUC7 20-mer and Hsn-5. The secondary structure prediction showed that MUC7 20-mer adopts an amphiphilic helix with distinguishable hydrophilic and hydrophobic faces (a characteristic that is associated with antimicrobial activity). In comparison to that of Hsn-5, the fungicidal activity of MUC7 20-mer against C. albicans seems to be independent of fungal cellular metabolic activity, as evidenced by its killing potency at a low temperature (4 degrees C) and in the presence of inhibitors of oxidative phosphorylation in the mitochondrial system. Fluorescence microscopy showed the ability of MUC7 20-mer to cross the fungal cell membrane and to accumulate inside the cells. The internalization of MUC7 20-mer was inhibited by divalent cations. Confocal microscopy of cells doubly labeled with MUC7 20-mer and a mitochondrion-specific dye indicated that mitochondria are not the target of MUC7 20-mer for either C. albicans or C. neoformans.

Indexed as

Amino Acid SequenceAntifungal AgentsCandida albicansCell SurvivalCryptococcus neoformansFluorescein-5-isothiocyanateHistatinsHumansMicrobial Sensitivity TestsMucinsSalivary Proteins and PeptidesStructure-Activity RelationshipAntifungal AgentsFluorescein-5-isothiocyanateHistatinsHTN3 protein, humanMUC7 protein, humanMucinsSalivary Proteins and Peptides

Identifiers

PMID12543672
PMCPMC151741
OpenAlexW2124901551

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.