Characterization of the Binding of Recombinant Mouse Sperm Fertilin α Subunit to Mouse Eggs: Evidence for Function as a Cell Adhesion Molecule in Sperm-Egg Binding (Q38344610)

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scientific article published on July 1, 1997

Language	Label	Description	Also known as
English	Characterization of the Binding of Recombinant Mouse Sperm Fertilin α Subunit to Mouse Eggs: Evidence for Function as a Cell Adhesion Molecule in Sperm-Egg Binding	scientific article published on July 1, 1997

Statements

scholarly article

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Europe PubMed Central

PubMed publication ID

2 September 2017

Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

Characterization of the Binding of Recombinant Mouse Sperm Fertilin α Subunit to Mouse Eggs: Evidence for Function as a Cell Adhesion Molecule in Sperm-Egg Binding (English)

1 reference

10.1006/DBIO.1997.8612

https://api.crossref.org/works/10.1006/DBIO.1997.8612

7 November 2024

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based on heuristic

inferred from title

sperm-ovum interaction

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9224677

7 November 2024

author name string

J. P. Evans

1

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7 November 2024

R. M. Schultz

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9224677

7 November 2024

G. S. Kopf

3

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7 November 2024

language of work or name

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publication date

1 July 1997

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2 September 2017

full work available at URL

https://doi.org/10.1006/dbio.1997.8612

online access status

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PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9224677

7 November 2024

https://api.elsevier.com/content/article/PII:S0012160697986127?httpAccept=text/xml

1 reference

10.1006/DBIO.1997.8612

https://api.crossref.org/works/10.1006/DBIO.1997.8612

7 November 2024

https://api.elsevier.com/content/article/PII:S0012160697986127?httpAccept=text/plain

1 reference

10.1006/DBIO.1997.8612

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7 November 2024

Developmental Biology

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2 September 2017

187

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Europe PubMed Central

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2 September 2017

1

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2 September 2017

94-106

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Europe PubMed Central

PubMed publication ID

2 September 2017

Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor.

2

1 reference

10.1006/DBIO.1997.8612

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Trophoblast/Leukocyte-Common Antigen is Expressed by Human Testicular Germ Cells and Appears on the Surface of Acrosome-Reacted Sperm1

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1 reference

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The role of complement component C3b and its receptors in sperm-oocyte interaction

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Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence

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A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion

6

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Enzymatic alteration of the ability of mouse egg plasma membrane to interact with sperm

8

1 reference

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7 November 2024

Evidence that an Arg-Gly-Asp adhesion sequence plays a role in mammalian fertilization

9

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Antibodies against epididymal glycoproteins block fertilizing ability in rat

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Identification and localization of integrin subunits in oocytes and eggs of the mouse

12

1 reference

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Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) β

13

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Characterization of the Binding of Recombinant Mouse Sperm Fertilin β Subunit to Mouse Eggs: Evidence for Adhesive Activity via an Egg β1Integrin-Mediated Interaction

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HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor

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Localization and characterization of the acrosomal antigen recognized by GB24 on human spermatozoa

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Complement component C1q and its receptor are involved in the interaction of human sperm with zona-free hamster eggs

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Vitronectin is an intrinsic protein of human spermatozoa released during the acrosome reaction

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Inhibition by anti-sperm monoclonal antibodies of the penetration of zona-free hamster oocytes by human spermatozoa

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Integrin-ligand interactions: a year in review

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Localization of fibronectin on the surface of human spermatozoa and relation to the sperm-egg interaction

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ADAMs and cell fusion

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Monoclonal antibodies against unfertilized zona-free mouse oocytes: characterization and effects on fertilization

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Delayed Translation and Posttranslational Processing of Cyritestin, an Integral Transmembrane Protein of the Mouse Acrosome

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Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion

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pH-dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of influenza virus hemagglutinin

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Molecular mechanisms of sperm-egg membrane binding and fusion in mammals

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Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion

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Effect of a monoclonal anti-mouse sperm antibody (OBF13) on the interaction of mouse sperm with zona-free mouse and hamster eggs

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A human sperm antigen possibly involved in binding and/or fusion with zona-free hamster eggs

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Cloning and analysis of monkey fertilin reveals novel alpha subunit isoforms

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Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion

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Mammalian sperm-egg fusion: the rat egg has complementary sites for a sperm protein that mediates gamete fusion

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Mouse sperm antigens that participate in fertilization. I. Inhibition of sperm fusion with the egg plasma membrane using monoclonal antibodies

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Expression patterns of novel genes during mouse preimplantation embryogenesis.

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Membrane fusion

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Integrins alpha v beta 3 and alpha v beta 5 promote adenovirus internalization but not virus attachment

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The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications

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ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

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Calcium Requirement for Sperm-Egg Fusion in Mammals

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Identifiers

10.1006/DBIO.1997.8612

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 September 2017

ResearchGate publication ID

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