Reference health

Cecropins contribute to <i>Drosophila</i> host defense against a subset of fungal and Gram-negative bacterial infection

https://doi.org/10.1093/genetics/iyab188
CiteStamped reference-health badge
62/62 checkable references clean · checked 2026-07-22

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

2 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

The 62 checked references that resolve
resolves10.1007/s430-001-8025-x
Cecropins, antibacterial peptides from insects and mammals, are potently fungicidal against Candida albicans
resolves10.1242/dmm.037721
Anti-tumour effects of antimicrobial peptides, components of the innate immune system, against haematopoietic tumours in <i>Drosophila mxc</i> mutants
resolves10.1371/journal.pgen.1007440
Antimicrobial peptides modulate long-term memory
resolves10.1073/pnas.97.7.3376
The phytopathogenic bacteria <i>Erwinia carotovora</i> infects <i>Drosophila</i> and activates an immune response
resolves10.1104/pp.108.4.1353
Plant Defensins: Novel Antimicrobial Peptides as Components of the Host Defense System
resolves10.1016/S0145-305X(99)00015-4
Antimicrobial peptides in insects; structure and function
resolves10.15252/embj.2020104486
Temporal specificity and heterogeneity of Drosophila immune cells
resolves10.1007/s10126-002-0021-1
Effect of Cecropin B and a Synthetic Analogue on Propagation of Fish Viruses In Vitro
resolves10.1371/journal.ppat.1004876
An Effector Peptide Family Required for Drosophila Toll-Mediated Immunity
resolves10.1023/B:PLAN.0000028791.34706.80
Transgenic Rice Plants Expressing the Antifungal AFP Protein from Aspergillus Giganteus Show Enhanced Resistance to the Rice Blast Fungus Magnaporthe Grisea
resolves10.3389/fimmu.2020.00009
The Daisho Peptides Mediate Drosophila Defense Against a Subset of Filamentous Fungi
resolves10.1093/emboj/21.11.2568
The Toll and Imd pathways are the major regulators of the immune response in Drosophila
resolves10.1128/AAC.41.2.481
Fungicidal activity of cecropin A
resolves10.18632/oncotarget.16743
Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications
resolves10.1016/j.celrep.2019.03.101
More Than Black or White: Melanization and Toll Share Regulatory Serine Proteases in Drosophila
resolves10.1016/S0965-1748(99)00071-5
Drosophila cecropin as an antifungal agent
resolves10.1371/journal.ppat.1004507
The Toll-Dorsal Pathway Is Required for Resistance to Viral Oral Infection in Drosophila
resolves10.1016/j.micinf.2011.02.005
Comparative pathology of bacteria in the genus Providencia to a natural host, Drosophila melanogaster
resolves10.1172/JCI112120
Defensins. Natural peptide antibiotics of human neutrophils.
resolves10.1073/pnas.221458698
Genome-wide analysis of the <i>Drosophila</i> immune response by using oligonucleotide microarrays
resolves10.1126/science.1165265
Antimicrobial Defense and Persistent Infection in Insects
resolves10.7554/eLife.44341
Synergy and remarkable specificity of antimicrobial peptides in vivo using a systematic knockout approach
resolves10.7554/eLife.48778
Correction: Synergy and remarkable specificity of antimicrobial peptides in vivo using a systematic knockout approach
resolves10.1016/j.coi.2019.11.008
New insights on Drosophila antimicrobial peptide function in host defense and beyond
resolves10.1371/journal.ppat.1009846
The Drosophila Baramicin polypeptide gene protects against fungal infection
resolves10.1074/jbc.M313856200
Differential Activation of the NF-κB-like Factors Relish and Dif in Drosophila melanogaster by Fungi and Gram-positive Bacteria
resolves10.1111/j.1432-1033.1980.tb05991.x
Insect Immunity. Purification and Properties of Three Inducible Bactericidal Proteins from Hemolymph of Immunized Pupae of <i>Hyalophora cecropia</i>
resolves10.1159/000086648
Antimicrobial Peptides in Drosophila: Structures,Activities and Gene Regulation
resolves10.1038/s41522-020-0116-3
The insect antimicrobial peptide cecropin A disrupts uropathogenic Escherichia coli biofilms
resolves10.1073/pnas.1003056107
Blocking of <i>Plasmodium</i> transmission by cooperative action of Cecropin A and Defensin A in transgenic <i>Aedes aegypti</i> mosquitoes
resolves10.7554/eLife.64919
Tissue-autonomous immune response regulates stress signaling during hypertrophy
resolves10.7554/eLife.50414
Drosophila macrophages switch to aerobic glycolysis to mount effective antibacterial defense
resolves10.1002/j.1460-2075.1990.tb08098.x
The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection.
resolves10.1016/j.mib.2008.05.001
Natural selection on the Drosophila antimicrobial immune system
resolves10.1073/pnas.94.26.14614
<i>Drosophila</i> host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
resolves10.1038/nri1390
The road to Toll
resolves10.1038/ni922
The Drosophila immune system detects bacteria through specific peptidoglycan recognition
resolves10.1074/mcp.M300114-MCP200
Proteomic Analysis of the Systemic Immune Response of Drosophila
resolves10.1371/journal.ppat.1008480
Effector specificity and function in Drosophila innate immunity: Getting AMPed and dropping Boms
resolves10.1159/000489831
Short-Form Bomanins Mediate Humoral Immunity in &lt;b&gt;&lt;i&gt;Drosophila&lt;/i&gt;&lt;/b&gt;
resolves10.1128/mBio.00824-21
<i>Drosophila</i> Antimicrobial Peptides and Lysozymes Regulate Gut Microbiota Composition and Abundance
resolves10.1038/s41573-019-0058-8
Antimicrobial host defence peptides: functions and clinical potential
resolves10.1371/journal.pone.0142451
Cecropins from Plutella xylostella and Their Interaction with Metarhizium anisopliae
resolves10.7554/eLife.45061
The antimicrobial peptide defensin cooperates with tumour necrosis factor to drive tumour cell death in Drosophila
resolves10.1016/j.peptides.2016.01.016
The functional interaction between abaecin and pore-forming peptides indicates a general mechanism of antibacterial potentiation
resolves10.1126/science.1149357
Innate Immune Homeostasis by the Homeobox Gene <i>Caudal</i> and Commensal-Gut Mutualism in <i>Drosophila</i>
resolves10.1038/ng.2007.60
Dynamic evolution of the innate immune system in Drosophila
resolves10.1002/j.1460-2075.1990.tb07489.x
The immune response in Drosophila: pattern of cecropin expression and biological activity.
resolves10.1002/j.1460-2075.1991.tb07932.x
The andropin gene and its product, a male‐specific antibacterial peptide in Drosophila melanogaster.
resolves10.1186/s12864-021-07593-3
Dense time-course gene expression profiling of the Drosophila melanogaster innate immune response
resolves10.3390/molecules171012276
Antimicrobial Peptides for Therapeutic Applications: A Review
resolves10.1038/292246a0
Sequence and specificity of two antibacterial proteins involved in insect immunity
resolves10.1016/0005-2736(88)90069-7
Binding and action of cecropin and cecropin analogues: Antibacterial peptides from insects
resolves10.1186/1471-2490-8-5
Antimicrobial peptides of the Cecropin-family show potent antitumor activity against bladder cancer cells
resolves10.7554/eLife.54818
A single-cell survey of Drosophila blood
resolves10.1371/journal.ppat.1006847
Comparative transcriptomics reveals CrebA as a novel regulator of infection tolerance in D. melanogaster
resolves10.1073/pnas.042411999
Constitutive expression of a single antimicrobial peptide can restore wild-type resistance to infection in immunodeficient <i>Drosophila</i> mutants
resolves10.1016/j.cub.2015.11.063
Convergent Balancing Selection on an Antimicrobial Peptide in Drosophila
resolves10.1073/pnas.95.19.11342
Differential display of peptides induced during the immune response of <i>Drosophila</i> : A matrix-assisted laser desorption ionization time-of-flight mass spectrometry study
resolves10.1128/AAC.45.5.1558-1560.2001
Synergistic Interactions between Mammalian Antimicrobial Defense Peptides
resolves10.1016/j.bbamem.2012.06.008
Synergistic action of Galleria mellonella anionic peptide 2 and lysozyme against Gram-negative bacteria
resolves10.1128/AEM.01913-08
Mitogen-Activated Protein Kinase hog1 in the Entomopathogenic Fungus<i>Beauveria bassiana</i>Regulates Environmental Stress Responses and Virulence to Insects
The 2 references without a DOI — listed, not checked
no DOI — not checked2022010607423203700_iyab188-B27
no DOI — not checked2022010607423203700_iyab188-B8138803
What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-07-22 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

Embed this badge

Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.

<a href="https://citestamp.com/citestamped/10.1093/genetics/iyab188"><img src="https://citestamp.com/citestamped/10.1093/genetics/iyab188/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1093/genetics/iyab188/badge.svg)](https://citestamp.com/citestamped/10.1093/genetics/iyab188)