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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Izumo sperm-egg fusion 1

Izumo, OBF
The sperm-specific protein Izumo, named for a Japanese shrine dedicated to marriage, is essential for sperm-egg plasma membrane binding and fusion (Inoue et al., 2005 [PubMed 15759005]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: OCA-B, OCT, Oct-2, GPR15, Oct-1
Papers on Izumo
Vaccination with an Epitope Peptide of IZUMO1 to Induce Contraception in Female Mice.
Xu et al., Shanghai, China. In Am J Reprod Immunol, Feb 2016
IZUMO1 plays an important role in the fusion of the sperm and ovum during fertilization.
Identification of novel alternative splicing transcript and expression analysis of bovine TMEM95 gene.
Lan et al., China. In Gene, Feb 2016
Bioinformatics predicted that TMEM95-SV1 has a leucine-rich repeat C-terminal domain and a Pfam: IZUMO.
Forward Genetics Identifies a Requirement for the Izumo-like Immunoglobulin Superfamily spe-45 Gene in Caenorhabditis elegans Fertilization.
Singson et al., United States. In Curr Biol, Jan 2016
The only cognate ligand-receptor pair identified in the context of fertilization is sperm-surface Izumo and egg-surface Juno in the mouse [1].
NF-κB-dependent signals control BOB.1/OBF.1 and Oct2 transcriptional activity in B cells.
Brunner et al., Ulm, Germany. In Eur J Immunol, Dec 2015
The transcriptional co-activator BOB.1/OBF.1 is crucial for Octamer-driven transcription in B cells.
[Effects of blood flow properties on ocular hemodynamics].
Kakunina et al., In Vestn Oftalmol, May 2015
AIM: to study the effects of blood rheology on ocular blood flow (OBF) parameters and estimated individual normal range of intraocular pressure (IOP).
Vaccine for human contraception targeting sperm Izumo protein and YLP12 dodecamer peptide.
Naz, Morgantown, United States. In Protein Sci, 2014
In this article, we will review two sperm-specific proteins, namely Izumo protein and YLP12 dodecamer peptide.
Juno is the egg Izumo receptor and is essential for mammalian fertilization.
Wright et al., Cambridge, United Kingdom. In Nature, 2014
Izumo1 is an essential sperm cell-surface protein, but its receptor on the egg has not been described.
Unstable oxygen supply and glaucoma.
Henrich et al., Basel, Switzerland. In Klin Monbl Augenheilkd, 2014
The major cause of fluctuations in the local oxygen tension is an unstable ocular blood flow (OBF).
New insights in the pathogenesis and treatment of normal tension glaucoma.
Flammer et al., Basel, Switzerland. In Curr Opin Pharmacol, 2013
A common cause for a disturbed OBF autoregulation is a primary vascular dysregulation (PVD) frequently observed in normal tension glaucoma patients.
Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins.
Primakoff et al., Davis, United States. In Reproduction, 2011
co-localization of TMEM190 with IZUMO1 and complex formation with other sperm proteins.
Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm.
Primakoff et al., Davis, United States. In Mol Reprod Dev, 2009
Results suggest that Izumo 1 might be involved in organizing or stabilizing a multiprotein complex essential for the function of the membrane fusion machinery.
Identification and disruption of sperm-specific angiotensin converting enzyme-3 (ACE3) in mouse.
Okabe et al., Ōsaka, Japan. In Plos One, 2009
identified an IZUMO1-interacting protein in sperm, which was identified as testis specific ACE homologue ACE3.
Immunocontraceptive potential of the Ig-like domain of Izumo.
Xu et al., Shanghai, China. In Mol Reprod Dev, 2009
Data indicate that the Ig-like domain of Izumo plays an important role in the fertilization process, as verified by the dose-dependent reduction in fertilization rates in mouse IVF trials and mouse mating assay.
In vitro and in vivo studies evaluating recombinant plasmid pCXN2-mIzumo as a potential immunocontraceptive antigen.
Chen et al., Shantou, China. In Am J Reprod Immunol, 2009
pCXN2-mIzumo plasmid possesses appreciable anti-fertility potential.
[Key sperm membrane proteins in sperm-egg fusion].
Huang et al., Shantou, China. In Zhonghua Nan Ke Xue, 2009
This article presents a detailed review of some of the key sperm membrane proteins closely related with fertilization, such as the Izumo, the ADAMs gene family and the Crisp gene family proteins, which is of practical significance for deeper insights into the mechanisms of sperm-egg fusion, as well as for the improvement of clinical diagnosis of male infertility and development of novel contraceptive drugs.
Sperm-egg adhesion and fusion in mammals.
Sutovsky, Columbia, United States. In Expert Rev Mol Med, 2008
At least two plasma membrane proteins essential for sperm-oolemma fusion--IZUMO and CD9 on the male and female gametes, respectively--have been identified recently by classical cell biology approaches and confirmed by gene deletion.
The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs.
Okabe et al., Suita, Japan. In Nature, 2005
identification of a mouse sperm fusion-related antigen and show that the antigen is a novel immunoglobulin superfamily protein
OcaB is required for normal transcription and V(D)J recombination of a subset of immunoglobulin kappa genes.
Nussenzweig et al., New York City, United States. In Cell, 2002
OcaB, a transcriptional coactivator also known as Bob-1 or OBF-1, was isolated on the basis of its ability to enhance transcription of immunoglobulin (Ig) genes in vitro.
Direct visualization of protein interactions in plant cells.
Brisson et al., Montréal, Canada. In Nat Biotechnol, 2001
The protein NPR1/NIM1 is required for the induction of systemic acquired resistance (SAR) in plants and has been shown to interact with members of the TGA/OBF family of basic leucine zipper (bZIP) transcription factors.
Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration.
Schöler et al., United States. In Cell, 2001
The POU dimer formed on the PORE (ATTTGAAATGCAAAT) can recruit the transcriptional coactivator OBF-1, whereas POU dimers formed on the consensus MORE (ATGCATATGCAT) or on MOREs from immunoglobulin heavy chain promoters (AT[G/A][C/A]ATATGCAA) fail to interact.
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