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Identification of biotransformation enzymes in the antennae of codling moth Cydia pomonella

https://doi.org/10.1016/j.gene.2016.01.008
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31/31 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.

5 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 31 checked references that resolve
resolves10.1016/j.jinsphys.2005.05.003
Responses to sex pheromone and plant odours by olfactory receptor neurons housed in sensilla auricillica of the codling moth, Cydia pomonella (Lepidoptera: Tortricidae)
resolves10.1021/jf0100548
Plant Odor Analysis of Apple:  Antennal Response of Codling Moth Females to Apple Volatiles during Phenological Development
resolves10.1371/journal.pone.0031620
Putative Chemosensory Receptors of the Codling Moth, Cydia pomonella, Identified by Antennal Transcriptome Analysis
resolves10.1111/imb.12100
Antennal uridine diphosphate ( <scp>UDP)</scp> ‐glycosyltransferases in a pest insect: diversity and putative function in odorant and xenobiotics clearance
resolves10.1186/1741-7007-10-56
A carboxylesterase, Esterase-6, modulates sensory physiological and behavioral response dynamics to pheromone in Drosophila
resolves10.1371/journal.pone.0067794
Identification and Characterization of an Antennae-Specific Aldehyde Oxidase from the Navel Orangeworm
resolves10.1371/journal.pone.0015026
Characterization of an Antennal Carboxylesterase from the Pest Moth Spodoptera littoralis Degrading a Host Plant Odorant
resolves10.1111/j.1365-2583.2009.00939.x
A diversity of putative carboxylesterases are expressed in the antennae of the noctuid moth <i>Spodoptera littoralis</i>
resolves10.1371/journal.pone.0029147
Degradation of Pheromone and Plant Volatile Components by a Same Odorant-Degrading Enzyme in the Cotton Leafworm, Spodoptera littoralis
resolves10.1042/bj20030121
Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology
resolves10.1139/gen-2014-0041
Two esterases from the genus <i>Spodoptera</i> degrade sex pheromones and plant volatiles
resolves10.1002/arch.21164
FUNCTIONAL CHARACTERIZATION OF AN ANTENNAL ESTERASE FROM THE NOCTUID MOTH, <i>Spodoptera exigua</i>
resolves10.1111/imb.12095
An antennae‐enriched carboxylesterase from <i> <scp>S</scp> podoptera exigua </i> displays degradation activity in both plant volatiles and female sex pheromones
resolves10.1007/s00114-003-0484-6
A female-specific attractant for the codling moth, Cydia pomonella , from apple fruit volatiles
resolves10.1073/pnas.0505340102
Rapid inactivation of a moth pheromone
resolves10.1073/pnas.0802610105
Chiral discrimination of the Japanese beetle sex pheromone and a behavioral antagonist by a pheromone-degrading enzyme
resolves10.1016/j.ibmb.2013.10.001
CYP345E2, an antenna-specific cytochrome P450 from the mountain pine beetle, Dendroctonus ponderosae Hopkins, catalyses the oxidation of pine host monoterpene volatiles
resolves10.1146/annurev-ento-120811-153635
Odorant Reception in Insects: Roles of Receptors, Binding Proteins, and Degrading Enzymes
resolves10.1007/BF01256549
Host-plant green-leaf volatiles synergize the synthetic sex pheromones of the corn earworm and codling moth (Lepidoptera)
resolves10.1007/s001140100243
A pear-derived kairomone with pheromonal potency that attracts male and female codling moth, Cydia pomonella (L.)
resolves10.1002/arch.21078
FUNCTIONAL ANALYSIS OF A MOSQUITO SHORT‐CHAIN DEHYDROGENASE CLUSTER
resolves10.1016/j.bbrc.2005.04.084
A new aldehyde oxidase selectively expressed in chemosensory organs of insects
resolves10.1242/dev.045641
<i>Non-molting glossy</i>/<i>shroud</i> encodes a short-chain dehydrogenase/reductase that functions in the ‘Black Box’ of the ecdysteroid biosynthesis pathway
resolves10.1016/j.gene.2007.08.022
Identification of candidate aldehyde oxidases from the silkworm Bombyx mori potentially involved in antennal pheromone degradation
resolves10.1603/EC09249
Susceptibility to Organophosphate Insecticides and Activity of Detoxifying Enzymes in Spanish Populations of &lt;I&gt;Cydia pomonella&lt;/I&gt; (Lepidoptera: Tortricidae)
resolves10.1111/j.1570-7458.2010.01088.x
Resistance of Spanish codling moth (Cydia pomonella) populations to insecticides and activity of detoxifying enzymatic systems
resolves10.1126/science.174.4006.297
Sex Attractant of the Codling Moth: Characterization with Electroantennogram Technique
resolves10.1242/jeb.202.12.1625
An olfactory-specific glutathione-<i>S</i>-transferase in the sphinx moth <i>Manduca sexta</i>
resolves10.1584/jpestics.R10-07
Carboxylesterases: dual roles in lipid and pesticide metabolism
resolves10.1007/s10886-014-0433-1
Putative Pathway of Sex Pheromone Biosynthesis and Degradation by Expression Patterns of Genes Identified from Female Pheromone Gland and Adult Antenna of Sesamia inferens (Walker)
resolves10.1016/S0965-1748(99)00018-1
Differential mRNA expression levels and gene sequences of a putative carboxylesterase-like enzyme from two strains of the parasitoid Anisopteromalus calandrae (Hymenoptera: Pteromalidae)
The 5 references without a DOI — listed, not checked
no DOI — not checkedMass rearing codling moths: improvements and modifications
no DOI — not checkedUse of ethyl (E, Z)-2, 4-decadienoate in codling moth management: kairomone species specificity
no DOI — not checkedBiochemical genetics and genomics of insect esterases
no DOI — not checkedMolecular basis of pheromone detection in insects
no DOI — not checkedPreferential expression of biotransformation enzymes in the olfactory organs of Drosophila melanogaster, theantennae
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.

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