ArticleStructure (London, England : 1993)2011
Tandem SAM domain structure of human Caskin1: a presynaptic, self-assembling scaffold for CASK.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 31 citations in OpenAlex.
- CASKIN2 mediates PTPσ-orchestrated transsynaptic mechanisms at excitatory synapses.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring Male-Specific Synaptic Plasticity in Major Depressive Disorder: A Single-Nucleus Transcriptomic Analysis Using Bioinformatics Methods.International journal of molecular sciences · 2025Article
- A Deep Dive into the N-Terminus of STIM Proteins: Structure-Function Analysis and Evolutionary Significance of the Functional Domains.Biomolecules · 2024Review
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- Hunting for Novel Routes in Anticancer Drug Discovery: Peptides against Sam-Sam Interactions.International journal of molecular sciences · 2022Review
- Structural insights into selective interaction between type IIa receptor protein tyrosine phosphatases and Liprin-α.Nature communications · 2020Article
- Dendritic spine morphology and memory formation depend on postsynaptic Caskin proteins.Scientific reports · 2019Article
- Distribution of Caskin1 protein and phenotypic characterization of its knockout mice using a comprehensive behavioral test battery.Molecular brain · 2018Article
- A lack of peptide binding and decreased thermostability suggests that the CASKIN2 scaffolding protein SH3 domain may be vestigial.BMC structural biology · 2016Article
- Structural insights into SAM domain-mediated tankyrase oligomerization.Protein science : a publication of the Protein Society · 2016Article
- A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.Cell communication and signaling : CCS · 2016Article
- Tankyrase Requires SAM Domain-Dependent Polymerization to Support Wnt-β-Catenin Signaling.Molecular cell · 2016Article
- Article
- Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3.BMC structural biology · 2014Article
- Copy number variation in Han Chinese individuals with autism spectrum disorder.Journal of neurodevelopmental disorders · 2014Article
- Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights.Chembiochem : a European journal of chemical biology · 2013Article
- Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain.Cell communication and signaling : CCS · 2012Article
- Putative chitin synthases from Branchiostoma floridae show extracellular matrix-related domains and mosaic structures.Genomics, proteomics & bioinformatics · 2012Article
- Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor.Biochemistry · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The synaptic scaffolding proteins CASK and Caskin1 are part of the fibrous mesh of proteins that organize the active zones of neural synapses. CASK binds to a region of Caskin1 called the CASK interaction domain (CID). Adjacent to the CID, Caskin1 contains two tandem sterile α motif (SAM) domains. Many SAM domains form polymers so they are good candidates for forming the fibrous structures seen in the active zone. We show here that the SAM domains of Caskin1 form a new type of SAM helical polymer. The Caskin1 polymer interface exhibits a remarkable segregation of charged residues, resulting in a high sensitivity to ionic strength in vitro. The Caskin1 polymers can be decorated with CASK proteins, illustrating how these proteins may work together to organize the cytomatrix in active zones.
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.