ArticleACS chemical biology2009
Beta1 integrin is an adhesion protein for sperm binding to eggs.
Article in ACS chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Amino-Acid-Derived Anionic Polyacrylamides with Tailored Hydrophobicity-Physicochemical Properties and Cellular Interactions.ACS polymers Au · 2024Article
- Role of Integrins in Sperm Activation and Fertilization.International journal of molecular sciences · 2021Review
- Partial Sperm beta1 Integrin Subunit Deletion Proves its Involvement in Mouse Gamete Adhesion/Fusion.International journal of molecular sciences · 2020Article
- Chemoselective, Postpolymerization Modification of Bioactive, Degradable Polymers.Biomacromolecules · 2019Article
- Precision Synthesis of Alternating Copolymers via Ring-Opening Polymerization of 1-Substituted Cyclobutenes.Accounts of chemical research · 2016Article
- Multivalent Antigens for Promoting B and T Cell Activation.ACS chemical biology · 2015Article
- Identification of putative drug targets for human sperm-egg interaction defect using protein network approach.BMC systems biology · 2015Article
- Sperm-egg fusion: a molecular enigma of mammalian reproduction.International journal of molecular sciences · 2014Review
- Fucose, mannose, and β-N-acetylglucosamine glycopolymers initiate the mouse sperm acrosome reaction through convergent signaling pathways.ACS chemical biology · 2014Article
- Synthesis of functionalizable and degradable polymers by ring-opening metathesis polymerization.Angewandte Chemie (International ed. in English) · 2013Article
- Article
- The glycoprotein B disintegrin-like domain binds beta 1 integrin to mediate cytomegalovirus entry.Journal of virology · 2010Article
- A general glycomimetic strategy yields non-carbohydrate inhibitors of DC-SIGN.Chemical communications (Cambridge, England) · 2010Article
- Scope of the ring-opening metathesis polymerization (ROMP) reaction of 1-substituted cyclobutenes.Journal of the American Chemical Society · 2010Article
- ROMP from ROMP: A New Approach to Graft Copolymer Synthesis.Macromolecules · 2009Article
- Egg integrins: back in the game of mammalian fertilization.ACS chemical biology · 2009Article
Corrections and comments
- Commented on by
Authors and funding
3 authors.
Funding
Abstract
We investigated the role of beta(1) integrin in mammalian fertilization and the mode of inhibition of fertilinbeta-derived polymers. We determined that polymers displaying the Glu-Cys-Asp peptide from the fertilinbeta disintegrin domain mediate inhibition of mammalian fertilization through a beta(1) integrin receptor on the egg surface. Inhibition of fertilization is a consequence of competition with sperm binding to the cell surface, not activation of an egg-signaling pathway. The presence of the beta(1) integrin on the egg surface increases the rate of sperm attachment but does not alter the total number of sperm that can attach or fuse to the egg. We conclude that the presence of beta(1) integrin enhances the initial adhesion of sperm to the egg plasma membrane and that subsequent attachment and fusion are mediated by additional egg and sperm proteins present in the beta(1) integrin complex. Therefore, the mechanisms by which sperm fertilize wild-type and beta(1) knockout eggs are different.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.