ReviewFrontiers in cellular neuroscience2016
Structural Insights into Reelin Function: Present and Future.
Review in Frontiers in cellular neuroscience, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT06876051 (The Impact of Prenatal Stress Management Program on Maternal Breastfeeding and Neonatal Neurodevelopmental Parameters), which is not on this map. Cited by 14 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.
The Impact of Prenatal Stress Management Program on Maternal Breastfeeding and Neonatal Neurodevelopmental Parameters
Who cites it
14 citing papers in PubMed, 34 citations in OpenAlex.
- Drospondin, a glial glycoprotein with similarities to human Reelin/F-spondin, contributes toProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Local inflammation at the salmon louse (Lepeophtheirus salmonis) attachment site contributes to copepodid rejection in coho salmon (Oncorhynchus kisutch).Cell and tissue research · 2025Article
- Article
- Article
- Lipophorin receptors regulate mushroom body development and complex behaviors in Drosophila.BMC biology · 2022Article
- The CNS/PNS Extracellular Matrix Provides Instructive Guidance Cues to Neural Cells and Neuroregulatory Proteins in Neural Development and Repair.International journal of molecular sciences · 2021Review
- Neuroserpin Is Strongly Expressed in the Developing and Adult Mouse Neocortex but Its Absence Does Not Perturb Cortical Lamination and Synaptic Proteome.Frontiers in neuroanatomy · 2021Article
- Identification of RELN variant p.(Ser2486Gly) in an Iranian family with ankylosing spondylitis; the first association of RELN and AS.European journal of human genetics : EJHG · 2020Article
- The Reelin Receptors Apolipoprotein E receptor 2 (ApoER2) and VLDL Receptor.International journal of molecular sciences · 2018Review
- Modulation of the tick gut milieu by a secreted tick protein favors Borrelia burgdorferi colonization.Nature communications · 2017Article
- Shunts, channels and lipoprotein endosomal traffic: a new model of cholesterol homeostasis in the hepatocyte.Journal of biomedical research · 2017Article
- Caudal Fossa Ratio in Normal Dogs and Eurasier Dogs with VLDLR-Associated Genetic Cerebellar Hypoplasia.Frontiers in veterinary science · 2017Article
- Dab1 Contributes to Angiotensin II-Induced Apoptosis via p38 Signaling Pathway in Podocytes.BioMed research international · 2017Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Reelin is a neuronal glycoprotein secreted by the Cajal-Retzius cells in marginal regions of the cerebral cortex and the hippocampus where it plays important roles in the control of neuronal migration and the formation of cellular layers during brain development. This 3461 residue-long protein is composed of a signal peptide, an F-spondin-like domain, eight Reelin repeats (RR1-8), and a positively charged sequence at the C-terminus. Biochemical data indicate that the central region of Reelin binds to the low-density lipoprotein receptors apolipoprotein E receptor 2 (ApoER2) and the very-low-density lipoprotein receptor (VLDLR), leading to the phosphorylation of the intracellular adaptor protein Dab1. After secretion, Reelin is rapidly degraded in three major fragments, but the functional significance of this degradation is poorly understood. Probably due to its large mass and the complexity of its architecture, the high-resolution, three-dimensional structure of Reelin has never been determined. However, the crystal structures of some of the RRs have been solved, providing important insights into their fold and the interaction with the ApoER2 receptor. This review discusses the current findings on the structure of Reelin and its binding to the ApoER2 and VLDLR receptors, and we discuss some areas where proteomics and structural biology can help understanding Reelin function in brain development and human health.
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.