ArticleEuropean journal of oral sciences2011
Structure and function of ameloblastin as an extracellular matrix protein: adhesion, calcium binding, and CD63 interaction in human and mouse.
Article in European journal of oral sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- A microglia-containing cerebral organoid model to study early life immune challenges.Brain, behavior, and immunity · 2025Article
- Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
- A microglia-containing cerebral organoid model to study early life immune challenges.bioRxiv : the preprint server for biology · 2024Article
- Regulation of Hydroxyapatite Nucleation In Vitro through Ameloblastin-Amelogenin Interactions.ACS biomaterials science & engineering · 2023Article
- The Dynamic Interactions of a Multitargeting Domain in Ameloblastin Protein with Amelogenin and Membrane.International journal of molecular sciences · 2023Article
- Article
- New insight into dental epithelial stem cells: Identification, regulation, and function in tooth homeostasis and repair.World journal of stem cells · 2020Review
- An Evolutionarily Conserved Helix Mediates Ameloblastin-Cell Interaction.Journal of dental research · 2020Article
- Co-Immunoprecipitation Reveals Interactions Between Amelogenin and AmeloblastinFrontiers in physiology · 2020Article
- Ameloblastin Binds to Phospholipid Bilayers via a Helix-Forming Motif within the Sequence Encoded by Exon 5.ACS omega · 2019Article
- Article
- Bone physiology as inspiration for tissue regenerative therapies.Biomaterials · 2018Review
- Ameloblastin induces tumor suppressive phenotype and enhances chemosensitivity to doxorubicin via Src-Stat3 inactivation in osteosarcoma.Scientific reports · 2017Article
- Phosphorylation Modulates Ameloblastin Self-assembly and CaFrontiers in physiology · 2017Article
- Amelogenesis Imperfecta; Genes, Proteins, and Pathways.Frontiers in physiology · 2017Review
- A targeted next-generation sequencing assay for the molecular diagnosis of genetic disorders with orodental involvement.Journal of medical genetics · 2016Article
- Evolutionary analysis of selective constraints identifies ameloblastin (AMBN) as a potential candidate for amelogenesis imperfecta.BMC evolutionary biology · 2015Article
- Article
- Ameloblastin inhibits cranial suture closure by modulating MSX2 expression and proliferation.PloS one · 2013Article
- Ameloblastin regulates cell attachment and proliferation through RhoA and p27.European journal of oral sciences · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The functional significance of extracellular matrix proteins in the life of vertebrates is underscored by a high level of sequence variability in tandem with a substantial degree of conservation in terms of cell-cell and cell-matrix adhesion interactions. Many extracellular matrix proteins feature multiple adhesion domains for successful attachment to substrates, such as integrin, CD63, and heparin. Here we have used homology and ab initio modeling algorithms to compare mouse ameloblastin (mAMBN) and human ameloblastin (hABMN) isoforms and to analyze their potential for cell adhesion and interaction with other matrix molecules as well as calcium binding. Sequence comparison between mAMBN and hAMBN revealed a 26-amino-acid deletion in mAMBN, corresponding to a helix-loop-helix frameshift. The human AMBN domain (174Q-201G), homologous to the mAMBN 157E-178I helix-loop-helix region, formed a helix-loop motif with an extended loop, suggesting a higher degree of flexibility of hAMBN compared with mAMBN, as confirmed by molecular dynamics simulation. Heparin-binding domains, CD63-interaction domains, and calcium-binding sites in both hAMBN and mAMBN support the concept of AMBN as an extracellular matrix protein. The high level of conservation between AMBN functional domains related to adhesion and differentiation was remarkable when compared with only 61% amino acid sequence homology.
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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.