{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T02:24:20Z","timestamp":1790303060579,"version":"4.1.0"},"reference-count":61,"publisher":"The Company of Biologists","issue":"10","license":[{"start":{"date-parts":[[1995,10,1]],"date-time":"1995-10-01T00:00:00Z","timestamp":812505600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.biologists.com\/user-licence-1-1\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1995,10,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:p>The guinea pig sperm protein, PH-30 (also known as fertilin), is postulated to participate in the interaction between the sperm and egg plasma membranes. The \u03b2 subunit of guinea pig PH-30 (gpPH-30\u03b2) contains a domain with homology to disintegrins, snake venom proteins that bind to integrins via an integrin-binding domain containing the tripeptide RGD. This raises the question of whether an egg integrin serves as a receptor for PH-30. Although mouse eggs express integrin subunits, their role in mouse fertilization is unresolved. Therefore, we examined fertilization for two different hallmarks of integrin function, namely, dependence of ligand binding on divalent cations and the ability to inhibit ligand binding with RGD peptides. We demonstrate that sperm binding to zona pellucida-free eggs is supported by Ca2+, Mg2+, or Mn2+. Ca2+ was necessary and sufficient for sperm-egg fusion, with 2.5 mM Ca2+ being the most effective concentration. In addition, fertilization could be partially inhibited with various RGD peptides, which caused a decrease in sperm-egg fusion by 30-58%. This partial inhibition of fusion with RGD peptides prompted the cloning of the mouse homologue of gpPH-30\u03b2 (hereafter referred to as mPH-30\u03b2) to determine if it possessed the tripeptide RGD or a different amino acid sequence in its disintegrin domain. mPH-30\u03b2, which is expressed during meiotic and post-meiotic phases of spermatogenesis, shares significant similarities to gpPH-30\u03b2 throughout the length of the molecule, from the signal sequence to the cytoplasmic tail. The full-length deduced amino acid sequence of mPH-30\u03b2 is 55% identical and 72% homologous to gpPH-30\u03b2. The disintegrin domain of mPH-30\u03b2 has the tripeptide QDE (instead of RGD) in its cell recognition region. Peptides containing this QDE sequence decrease the binding and fusion of sperm with zona pellucida-free eggs by approximately 70%, suggesting that the disintegrin domain of mPH-30\u03b2 participates in the interaction between sperm and egg membranes.<\/jats:p>","DOI":"10.1242\/jcs.108.10.3267","type":"journal-article","created":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T16:02:42Z","timestamp":1619366562000},"page":"3267-3278","source":"Crossref","is-referenced-by-count":124,"title":["Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) \u03b2"],"prefix":"10.1242","volume":"108","author":[{"given":"Janice P.","family":"Evans","sequence":"first","affiliation":[{"name":"1 Division of Reproductive Biology, Department of Obstetrics and Gynecology, Room 313 John Morgan Building, School of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard M.","family":"Schultz","sequence":"additional","affiliation":[{"name":"University of Pennsylvania, Philadelphia 2 Department of Biology , , PA 19104, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory S.","family":"Kopf","sequence":"additional","affiliation":[{"name":"1 Division of Reproductive Biology, Department of Obstetrics and Gynecology, Room 313 John Morgan Building, School of Medicine"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[1995,10,1]]},"reference":[{"key":"2023122622160427300_JOCES_108_10_3267C1","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1016\/0076-6879(92)19013-V","article-title":"Nuclear protein import using digitonin-permeabilized cells","volume":"219","author":"Adam","year":"1992","journal-title":"Meth. Enzymol"},{"key":"2023122622160427300_JOCES_108_10_3267C2","doi-asserted-by":"publisher","first-page":"10051","DOI":"10.1073\/pnas.90.21.10051","article-title":"The role of complement component C3b and its receptors in sperm-oocyte interaction","volume":"90","author":"Anderson","year":"1993","journal-title":"Proc. Nat. Acad. Aci. USA"},{"key":"2023122622160427300_JOCES_108_10_3267C3","doi-asserted-by":"publisher","first-page":"429","DOI":"10.1016\/0167-4781(94)90198-8","article-title":"Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family","volume":"1218","author":"Barker","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"key":"2023122622160427300_JOCES_108_10_3267C4","doi-asserted-by":"publisher","first-page":"68","DOI":"10.1083\/jcb.74.1.68","article-title":"Spermatogenic cells of the prepubertal mouse: Isolation and morphological characterization","volume":"74","author":"Bellv\u00e9","year":"1977","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C5","doi-asserted-by":"publisher","first-page":"5563","DOI":"10.1073\/pnas.87.14.5563","article-title":"Identification of a ZP3-binding protein on acrosome-intact mouse sperm by photoaffinity crosslinking","volume":"87","author":"Bleil","year":"1990","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"2023122622160427300_JOCES_108_10_3267C6","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1083\/jcb.111.1.69","article-title":"Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence","volume":"111","author":"Blobel","year":"1990","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C7","doi-asserted-by":"publisher","first-page":"248","DOI":"10.1038\/356248a0","article-title":"A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion","volume":"356","author":"Blobel","year":"1992","journal-title":"Nature"},{"key":"2023122622160427300_JOCES_108_10_3267C8","doi-asserted-by":"publisher","first-page":"1019","DOI":"10.1095\/biolreprod43.6.1019","article-title":"Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization","volume":"43","author":"Bronson","year":"1990","journal-title":"Biol. Reprod"},{"key":"2023122622160427300_JOCES_108_10_3267C9","doi-asserted-by":"publisher","first-page":"272","DOI":"10.1006\/dbio.1994.1252","article-title":"The major fibrous sheath polypeptide of mouse sperm: Structural and functional similarities to the A-kinase anchoring proteins","volume":"165","author":"Carrera","year":"1994","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C10","doi-asserted-by":"publisher","first-page":"659","DOI":"10.1016\/0092-8674(94)90551-7","article-title":"Ligand and cation binding are dual function of a discrete segment of the integrin \u03b23 subunit: cation displacement is involved in ligand binding","volume":"79","author":"D\u2019Souza","year":"1994","journal-title":"Cell"},{"key":"2023122622160427300_JOCES_108_10_3267C11","doi-asserted-by":"publisher","first-page":"211","DOI":"10.1002\/mrd.1080400210","article-title":"Identification and localization of integrin subunits in oocytes and eggs of the mouse","volume":"40","author":"Evans","year":"1995","journal-title":"Mol. Reprod. Dev"},{"key":"2023122622160427300_JOCES_108_10_3267C12","doi-asserted-by":"publisher","first-page":"243","DOI":"10.1016\/0012-1606(84)90079-4","article-title":"Enzymatic dissection of the functions of the mouse egg\u2019s receptor for sperm","volume":"106","author":"Florman","year":"1984","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C13","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1530\/jrf.0.0810077","article-title":"Minimum and maximum extracellular Ca2+ requirements during mouse sperm capacitation and fertilization in vitro","volume":"81","author":"Fraser","year":"1987","journal-title":"J. Reprod. Fert"},{"key":"2023122622160427300_JOCES_108_10_3267C14","doi-asserted-by":"publisher","first-page":"54","DOI":"10.1002\/mrd.1080380110","article-title":"Calcium concentration and fertilization by subzonal insemination of a single spermatozoon in mouse oocytes","volume":"38","author":"Fujimoto","year":"1994","journal-title":"Mol. Reprod. Dev"},{"key":"2023122622160427300_JOCES_108_10_3267C15","doi-asserted-by":"publisher","first-page":"212","DOI":"10.1002\/mrd.1080360212","article-title":"Mammalian oocytes exhibit specific recognition of the RGD (Arg-Gly-Asp) tripeptide and express oolemmal integrins","volume":"36","author":"Fusi","year":"1993","journal-title":"Mol. Reprod. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C16","doi-asserted-by":"publisher","first-page":"3361","DOI":"10.4049\/jimmunol.144.9.3361","article-title":"Human B lymphocytes define an alternative mechanism of adhesion to fibronectin: the interaction of \u03b14\u03b21 integrin with the LHGPEILDVPST sequence of the type III connecting segment is sufficient to promote attachment","volume":"144","author":"Garcia-Pardo","year":"1990","journal-title":"J. Immunol"},{"key":"2023122622160427300_JOCES_108_10_3267C17","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1083\/jcb.117.2.449","article-title":"A synthetic peptide derived from the carboxy terminus of the laminin A chain represent a binding site for the \u03b13\u03b21 integrin","volume":"117","author":"Gehlsen","year":"1992","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C18","doi-asserted-by":"publisher","first-page":"168","DOI":"10.3181\/00379727-195-43129B","article-title":"Disintegrins: A family of integrin inhibitory proteins from viper venoms","volume":"195","author":"Gould","year":"1990","journal-title":"Proc. Soc. Exp. Biol. Med"},{"key":"2023122622160427300_JOCES_108_10_3267C19","doi-asserted-by":"publisher","first-page":"656","DOI":"10.1016\/0955-0674(94)90091-4","article-title":"Integrin-ligand interactions: a year in review","volume":"6","author":"Haas","year":"1994","journal-title":"Curr. Opin. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C20","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1111\/j.1440-169X.1994.00049.x","article-title":"Male germ cell-expressed mouse gene TAZ83 encodes a putative cysteine-rich transmembrane protein (cyritestin) sharing homologies with snake toxins and sperm-egg fusion proteins","volume":"36","author":"Heinlein","year":"1994","journal-title":"Dev. Growth Differ"},{"key":"2023122622160427300_JOCES_108_10_3267C21","doi-asserted-by":"publisher","first-page":"33","DOI":"10.3109\/15419069309095680","article-title":"Variants of the \u03b16\u03b21 receptor in early murine development: Distribution, molecular cloning and chromosomal localization of the mouse integrin \u03b16 subunit","volume":"1","author":"Hierck","year":"1993","journal-title":"Cell Adhes. Commun"},{"key":"2023122622160427300_JOCES_108_10_3267C22","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1016\/0012-1606(86)90082-5","article-title":"Rapid visual detection of sperm-egg fusion using the DNA-specific fluorochrome Hoechst 33342","volume":"118","author":"Hinkley","year":"1986","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C23","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/0092-8674(92)90115-S","article-title":"Integrins: Versatility, modulation and signalling in cell adhesion","volume":"69","author":"Hynes","year":"1992","journal-title":"Cell"},{"key":"2023122622160427300_JOCES_108_10_3267C24","doi-asserted-by":"publisher","first-page":"577","DOI":"10.1083\/jcb.120.3.577","article-title":"Signal transduction from the extracellular matrix","volume":"120","author":"Juliano","year":"1993","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C25","doi-asserted-by":"publisher","first-page":"4471","DOI":"10.1016\/S0021-9258(20)64346-0","article-title":"Calcium as a potential physiological regulator of integrin-mediated cell adhesion","volume":"266","author":"Kirchhofer","year":"1991","journal-title":"J. Biol. Chem"},{"key":"2023122622160427300_JOCES_108_10_3267C26","doi-asserted-by":"publisher","first-page":"20205","DOI":"10.1016\/S0021-9258(20)80715-7","article-title":"Selection of peptides binding to the \u03b15\u03b21 integrin from phage display library","volume":"268","author":"Koivunen","year":"1993","journal-title":"J. Biol. Chem"},{"key":"2023122622160427300_JOCES_108_10_3267C27","first-page":"265","article-title":"Phage libraries displaying cyclic peptides with different ring sizes: ligand specificites of the RGD-directed integrins","volume":"13","author":"Koivunen","year":"1995","journal-title":"Bio\/Technology"},{"key":"2023122622160427300_JOCES_108_10_3267C28","doi-asserted-by":"publisher","first-page":"1069","DOI":"10.1242\/dev.113.4.1069","article-title":"Avian neural crest cell attachment to laminin: involvement of divalent cation dependent and independent integrins","volume":"113","author":"Lallier","year":"1991","journal-title":"Development"},{"key":"2023122622160427300_JOCES_108_10_3267C29","doi-asserted-by":"publisher","first-page":"964","DOI":"10.1126\/science.1439808","article-title":"Selectin: Interpreters of cell-specific carbohydrate information during inflammation","volume":"258","author":"Lasky","year":"1992","journal-title":"Science"},{"key":"2023122622160427300_JOCES_108_10_3267C30","doi-asserted-by":"publisher","first-page":"1123","DOI":"10.1016\/0092-8674(89)90049-4","article-title":"95 kD sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding","volume":"57","author":"Leyton","year":"1989","journal-title":"Cell"},{"key":"2023122622160427300_JOCES_108_10_3267C31","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1038\/357589a0","article-title":"Complementarity between sperm surface \u03b2-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding","volume":"357","author":"Miller","year":"1992","journal-title":"Nature"},{"key":"2023122622160427300_JOCES_108_10_3267C32","doi-asserted-by":"publisher","first-page":"523","DOI":"10.1530\/jrf.0.0450523","article-title":"The role of calcium ions in fertilization of mouse and rat eggs in vitro","volume":"45","author":"Miyamoto","year":"1975","journal-title":"J. Reprod. Fert"},{"key":"2023122622160427300_JOCES_108_10_3267C33","doi-asserted-by":"publisher","first-page":"3160","DOI":"10.1093\/nar\/22.15.3160","article-title":"An alternative pathway of histone mRNA 3\u2032 end formation in mouse round spermatids","volume":"22","author":"Moss","year":"1994","journal-title":"Nucl. Acid Res"},{"key":"2023122622160427300_JOCES_108_10_3267C34","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1006\/dbio.1993.1166","article-title":"Molecular mechanisms of sperm-egg membrane binding and fusion in mammals","volume":"158","author":"Myles","year":"1993","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C35","doi-asserted-by":"publisher","first-page":"4195","DOI":"10.1073\/pnas.91.10.4195","article-title":"Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion","volume":"91","author":"Myles","year":"1994","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"2023122622160427300_JOCES_108_10_3267C36","doi-asserted-by":"publisher","first-page":"1295","DOI":"10.1083\/jcb.114.6.1295","article-title":"Monoclonal antibody characterization of two distant sites required for function of the central cell-binding domain of fibronectin in cell adhesion, cell migration, and matrix assembly","volume":"114","author":"Nagai","year":"1991","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C37","doi-asserted-by":"publisher","first-page":"509","DOI":"10.1002\/prot.340140411","article-title":"Identification of novel peptide antagonists for GPIIb\/IIIa from a conformationally constrained phage display peptide library","volume":"14","author":"O\u2019Neill","year":"1992","journal-title":"Proteins"},{"key":"2023122622160427300_JOCES_108_10_3267C38","doi-asserted-by":"publisher","first-page":"671","DOI":"10.1042\/bj2860671","article-title":"A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides","volume":"286","author":"Perry","year":"1992","journal-title":"Biochem. J"},{"key":"2023122622160427300_JOCES_108_10_3267C39","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1016\/0167-4838(94)90062-0","article-title":"Genetic evidence for an additional member of the metalloprotease-like, disintegrin-like, cysteine-rich (MDC) family of mammalian proteins and its abundant expression in the testis","volume":"1207","author":"Perry","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"key":"2023122622160427300_JOCES_108_10_3267C40","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1083\/jcb.104.1.141","article-title":"Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion","volume":"104","author":"Primakoff","year":"1987","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C41","doi-asserted-by":"publisher","first-page":"475","DOI":"10.1016\/0076-6879(87)44196-7","article-title":"Arginine-Glycine-Aspartic acid adhesion receptors","volume":"144","author":"Pytela","year":"1987","journal-title":"Meth. Enzymol"},{"key":"2023122622160427300_JOCES_108_10_3267C42","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1016\/0012-1606(92)90093-V","article-title":"Mammalian sperm-egg fusion: The rat egg has complementary sites for a sperm protein that mediates gamete fusion","volume":"153","author":"Rochwerger","year":"1992","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C43","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1016\/0955-0674(94)90092-2","article-title":"The selectins and their ligands","volume":"6","author":"Rosen","year":"1994","journal-title":"Curr. Opin. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C44","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1095\/biolreprod33.2.515","article-title":"Mouse sperm antigens that participate in fertilization. I. Inhibition of sperm fusion with the egg plasma membrane using monoclonal antibodies","volume":"33","author":"Saling","year":"1985","journal-title":"Biol. Reprod"},{"key":"2023122622160427300_JOCES_108_10_3267C45","volume-title":"Molecular Cloning: A Laboratory Manual. Second edition","author":"Sambrook","year":"1989"},{"key":"2023122622160427300_JOCES_108_10_3267C46","doi-asserted-by":"publisher","first-page":"12267","DOI":"10.1016\/S0021-9258(19)38340-1","article-title":"Interaction of integrins \u03b1v\u03b23 and glycoprotein IIb-IIIa with fibrinogen","volume":"265","author":"Smith","year":"1990","journal-title":"J. Biol. Chem"},{"key":"2023122622160427300_JOCES_108_10_3267C47","doi-asserted-by":"publisher","first-page":"1175","DOI":"10.1242\/dev.119.4.1175","article-title":"Developmental regulation of integrin expression at the time of implantation in the mouse embryo","volume":"119","author":"Sutherland","year":"1993","journal-title":"Development"},{"key":"2023122622160427300_JOCES_108_10_3267C48","doi-asserted-by":"publisher","first-page":"1369","DOI":"10.1242\/dev.117.4.1369","article-title":"Expression of \u03b21 integrin complexes on the surface of unfertilized mouse oocytes","volume":"117","author":"Tarone","year":"1993","journal-title":"Development"},{"key":"2023122622160427300_JOCES_108_10_3267C49","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1002\/mrd.1080370202","article-title":"Expression patterns of novel genes during mouse preimplantation development","volume":"37","author":"Temeles","year":"1994","journal-title":"Mol. Reprod. Dev"},{"key":"2023122622160427300_JOCES_108_10_3267C50","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1083\/jcb.121.2.461","article-title":"A novel integrin specificity exemplified by binding of \u03b1v\u03b25 to the basic domain of HIV-Tat protein and vitronectin","volume":"121","author":"Vogel","year":"1993","journal-title":"J. Cell Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C51","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/0012-1606(84)90084-8","article-title":"Determination of the time course of capacitation in mouse spermatozoa using a chlortetracycline fluorescence assay","volume":"104","author":"Ward","year":"1984","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C52","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1242\/dev.108.1.1","article-title":"Profile of a mammalian sperm receptor","volume":"108","author":"Wassarman","year":"1990","journal-title":"Development"},{"key":"2023122622160427300_JOCES_108_10_3267C53","doi-asserted-by":"publisher","first-page":"917","DOI":"10.1126\/science.1439803","article-title":"Membrane fusion","volume":"258","author":"White","year":"1992","journal-title":"Science"},{"key":"2023122622160427300_JOCES_108_10_3267C54","first-page":"129","article-title":"Nutrient requirements for the culture of preimplantation embryos in vitro","volume":"6","author":"Whitten","year":"1971","journal-title":"Advan. Biol. Sci"},{"key":"2023122622160427300_JOCES_108_10_3267C55","doi-asserted-by":"publisher","first-page":"10783","DOI":"10.1073\/pnas.90.22.10783","article-title":"The precursor region of a protein active in sperm-egg fusion contains metalloprotease domain and a disintegrin domain: structural, functional, and evolutionary implications","volume":"90","author":"Wolfsberg","year":"1993","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"2023122622160427300_JOCES_108_10_3267C56","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1006\/dbio.1995.1152","article-title":"ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloproteinase domain","volume":"169","author":"Wolfsberg","year":"1995","journal-title":"Dev. Biol"},{"key":"2023122622160427300_JOCES_108_10_3267C57","doi-asserted-by":"publisher","first-page":"949","DOI":"10.1095\/biolreprod19.5.949","article-title":"Calcium requirement for sperm-egg fusion in mammals","volume":"19","author":"Yanagimachi","year":"1978","journal-title":"Biol. Reprod"},{"key":"2023122622160427300_JOCES_108_10_3267C58","doi-asserted-by":"publisher","first-page":"323","DOI":"10.1002\/mrd.1120050404","article-title":"Requirement of extracellular calcium ions for various stages of fertilization and fertilization-related phenomena in the hamster","volume":"5","author":"Yanagimachi","year":"1987","journal-title":"Gamete Res"},{"key":"2023122622160427300_JOCES_108_10_3267C59","article-title":"Mammalian fertilization","volume-title":"In The Physiology of Reproduction","author":"Yanagimachi","year":"1994"},{"key":"2023122622160427300_JOCES_108_10_3267C60","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1093\/intimm\/2.6.585","article-title":"Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage","volume":"2","author":"Yoshida","year":"1990","journal-title":"Int. Immunol"},{"key":"2023122622160427300_JOCES_108_10_3267C61","first-page":"1050","article-title":"Cloning of 5\u2032 cDNA regions by inverse PCR","volume":"17","author":"Zeiner","year":"1994","journal-title":"Biotechniques"}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/108\/10\/3267\/3328796\/joces_108_10_3267.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/108\/10\/3267\/3328796\/joces_108_10_3267.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,12,26]],"date-time":"2023-12-26T22:16:22Z","timestamp":1703628982000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/108\/10\/3267\/24226\/Mouse-sperm-egg-plasma-membrane-interactions"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1995,10,1]]},"references-count":61,"journal-issue":{"issue":"10","published-print":{"date-parts":[[1995,10,1]]}},"URL":"https:\/\/doi.org\/10.1242\/jcs.108.10.3267","relation":{},"ISSN":["0021-9533","1477-9137"],"issn-type":[{"value":"0021-9533","type":"print"},{"value":"1477-9137","type":"electronic"}],"subject":[],"published":{"date-parts":[[1995,10,1]]}}}