Citation: 'acrosome' in the IUPAC Compendium of Chemical Terminology, 5th ed.; International Union of Pure and Applied Chemistry; 2025. Online version 5.0.0, 2025. 10.1351/goldbook.10333 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms. Requests for commercial usage
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Wheat germ agglutinin blocks the acrosome reaction in Strongylocentrotus purpuratus sperm by binding a 210,000-mol-wt membrane protein. [PDF]
Sheila Podell, Victor D. Vacquier
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Effect of Dilauroylphosphatidylcholine on the Acrosome Reaction and Subsequent Penetration of Bull Spermatozoa into Zona-Free Hamster Eggs [PDF]
J.K. Graham, R.H. Foote, J.J. Parrish
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El espermatozoide de Cancer setosus está compuesto de un acrosoma esférico y un núcleo en forma de copa que rodea la mitad basal del acrosoma que se ensancha en la zona ecuatorial del acrosoma.
Merari Goldstein, Enrique Dupré
doaj
The Multi‐PDZ domain protein MUPP1 as a lipid raft‐associated scaffolding protein controlling the acrosome reaction in mammalian spermatozoa [PDF]
Frauke Ackermann +5 more
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Animal Experimentation: The Biological Significance of Phospholipase C β1 Gene Mutation in Mouse Sperm in the Acrosome Reaction, Fertilization, and Embryo Development [PDF]
DooSeok Choi +7 more
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The ultrastructure of the spermatozoon of Paradynome tuberculata Sakai, 1963 (Crustacea, Brachyura, Dynomenidae) : synapomorphies with dromiid sperm [PDF]
The dynomenid spermatozoon, exemplified here by #Paradynomene tuberculata$, resembles the spermatozoa of the #Dromiidae$, #Homolidae$ and lyreidine raninoids and differs markedly from those of other crabs (the heterotreme, thoracotremes, raninines and ...
Guinot, D. +2 more
core
Effect of amino acids and dipeptides on the acrosome reaction and accumulation of ammonia in porcine spermatozoa [PDF]
K. M. A. Tareq +6 more
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Sperm acrosome reaction: its site and role in fertilization†
N. Hirohashi, R. Yanagimachi
semanticscholar +1 more source
Elasto-plastic response of reversibly crosslinked biopolymer bundles
We study the response of F-actin bundles to driving forces through a simple analytical model. We consider two filaments connected by reversibly bound crosslinks and driven by an external force. Two failure modes under load can be defined. \textit{Brittle
Heussinger, Claus +2 more
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