Reference health
Sperm plasma membrane breakdown during <i>Drosophila</i> fertilization requires Sneaky, an acrosomal membrane protein
40/40 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.
9 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 40 checked references that resolve
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Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
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ConPred II: a consensus prediction method for obtaining transmembrane topology models with high reliability
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Molecular Analysis of Cellulose Biosynthesis in
<i>Arabidopsis</i>
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Membrane Fusion in Relation to Sperm-Egg Association**Part of the work reported here was supported by National Institutes of Health research grants GM-04948 and HD-00007.
resolves10.1016/S0040-8166(02)00099-X
New findings on sperm ultrastructure of Xenos vesparum (Rossi) (Strepsiptera, Insecta)
resolves10.1006/dbio.1995.1115
Mammalian CD2 Is an Effective Heterologous Marker of the Cell Surface in Drosophila
resolves10.1093/humupd/8.4.297
The molecular basis of sperm-oocyte membrane interactions during mammalian fertilization
resolves10.1016/S0304-4157(00)00018-6
Dynamics of the mammalian sperm plasma membrane in the process of fertilization
resolves10.1074/jbc.M009298200
The Structure of the C4C4RING Finger of Human NOT4 Reveals Features Distinct from Those of C3HC4 RING Fingers
resolves10.1002/1521-4141(200012)30:12<3585::AID-IMMU3585>3.0.CO;2-Y
DC-STAMP, a novel multimembrane-spanning molecule preferentially expressed by dendritic cells
resolves10.1093/bioinformatics/14.4.378
SOSUI: classification and secondary structure prediction system for membrane proteins.
resolves10.1002/dvg.1020160208
Regulation of β‐tubulin function and expression in <i>Drosophila</i> spermatogenesis
resolves10.1016/j.jmb.2004.03.016
A Combined Transmembrane Topology and Signal Peptide Prediction Method
resolves10.1074/jbc.M412999200
Solution Structure of the C-terminal Domain of TFIIH P44 Subunit Reveals a Novel Type of C4C4 Ring Domain Involved in Protein-Protein Interactions
resolves10.1534/genetics.167.1.203
The Zuker Collection: A Resource for the Analysis of Autosomal Gene Function in Drosophila melanogaster
resolves10.1016/j.ydbio.2005.07.020
The spe-42 gene is required for sperm–egg interactions during C. elegans fertilization and encodes a sperm-specific transmembrane protein
resolves10.1006/jmbi.2000.4315
Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen
resolves10.1266/ggs.78.253
The Drosophila misfire gene has an essential role in sperm activation during fertilization.
resolves10.1016/S0960-9822(00)00381-X
The progeny of wingless-expressing cells deliver the signal at a distance in Drosophila embryos
resolves10.1016/S0960-9822(02)00867-9
Producing Cells Retain and Recycle Wingless in Drosophila Embryos
resolves10.1093/genetics/144.4.1623
Flanking Duplications and Deletions Associated With <i>P</i>-Induced Male Recombination in Drosophila
resolves10.1186/1472-6807-6-1
DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways
resolves10.1095/biolreprod.102.007856
Cell Adhesion and Fertilization: Steps in Oocyte Transport, Sperm-Zona Pellucida Interactions, and Sperm-Egg Fusion1
resolves10.1016/0092-8674(92)90191-E
brahma: A regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2SWI2
resolves10.1093/nar/22.22.4673
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
resolves10.1534/genetics.167.1.207
Toward a Comprehensive Genetic Analysis of Male Fertility in Drosophila melanogaster
resolves10.1083/jcb.130.4.857
Inositol 1,4,5-trisphosphate receptors selectively localized to the acrosomes of mammalian sperm.
resolves10.1016/j.cub.2005.06.060
PIP2 Hydrolysis and Calcium Release Are Required for Cytokinesis in Drosophila Spermatocytes
resolves10.1084/jem.20050645
DC-STAMP is essential for cell–cell fusion in osteoclasts and foreign body giant cells
The 9 references without a DOI — listed, not checked
no DOI — not checkedBaccetti, B. (1979). The evolution of the acrosomal complex. In The Spermatozoon: Maturation, Motility,Surface Properties, and Comparative Aspects (ed. D. W. Fawcett and J. M. Bedford), pp. 305-329. Baltimore-Munich:Urban and Schwarzenberg.
no DOI — not checkedFitch, K. R. and Wakimoto, B. T. (1998). The paternal effect gene ms(3)sneaky is required for sperm activation and the initiation of embryogenesis in Drosophila melanogaster.Dev. Biol. 197,270-282.
no DOI — not checkedFitch, K. R., Yasuda, G. Y., Owens, K. N. and Wakimoto, B. T. (1998). Paternal effects in Drosophila:Implications for the mechanisms of early development. Curr. Top. Dev. Biol. 38,1-34.
no DOI — not checkedFuller, M. T. (1993). Spermatogenesis. In The Development of Drosophila melanogaster. Vol.I (ed. M. Bate and A. Martinez-Arias), pp.71-148. Cold Spring Harbor: Cold Spring Harbor Laboratory Press.
no DOI — not checkedNeill, A. T. and Vacquier, V. D. (2004). Ligands and receptors mediating signal tranduction in sea urchin. Reproduction127,141-149.
no DOI — not checkedSambrook, J. and Russell, D. W. (2001). Molecular Cloning: a Laboratory Manual. Cold Spring Harbor, CSHL Press.
no DOI — not checkedTakano, H., Yanagimachi, R. and Urch, U. A.(1998). Evidence that acrosin activity is important for the development of fusibility of mammalian spermatozoa with the oolema: inhibitor studies using the golden hamster. Zygote1, 79-91.
no DOI — not checkedThummel, C. and Pirrotta, V. (1992). New pCasPeR P element vectors. Dros. Info. Serv. 71, 150.
no DOI — not checkedYanagimachi, R. (1994). Mammalian fertilization. In The Physiology of Reproduction (ed. J. D. Neill and E. Knobil), pp. 189-317. New York:Raven Press.
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