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Calmodulin regulated spectrin-associated protein 1

Camsap1, CAMSAP, calmodulin-regulated spectrin-associated protein 1
Top mentioned proteins: DLK, CAN, Glial Fibrillary Acidic Protein, KIAA1078, STEP
Papers on Camsap1
A six gene expression signature defines aggressive subtypes and predicts outcome in childhood and adult acute lymphoblastic leukemia.
Rousseaux et al., Shanghai, China. In Oncotarget, Jul 2015
Six genes whose expression in leukemic blasts was associated with prognosis were identified:three genes predicting poor prognosis (AK022211, FASTKD1 and STARD4) and three genes associated with a favorable outcome (CAMSAP1, PCGF6 and SH3RF3).
Microtubule minus-end-targeting proteins.
Hoogenraad et al., Utrecht, Netherlands. In Curr Biol, Mar 2015
The recent characterization of the CAMSAP/Patronin/Nezha family members as specific 'minus-end-targeting proteins' ('-TIPs') has provided important new insights into the mechanisms governing minus-end dynamics.
The microtubule minus-end-binding protein patronin/PTRN-1 is required for axon regeneration in C. elegans.
Chisholm et al., San Diego, United States. In Cell Rep, 2014
We report that PTRN-1, the C. elegans member of the Patronin/Nezha/calmodulin- and spectrin-associated protein (CAMSAP) family of microtubule minus-end-binding proteins, is critical for efficient axon regeneration in vivo.
Microtubule minus-end binding protein CAMSAP2 controls axon specification and dendrite development.
Hoogenraad et al., Utrecht, Netherlands. In Neuron, 2014
Using live-cell imaging, high-resolution microscopy, and laser-based microsurgery techniques, we show that the CAMSAP/Nezha/Patronin family protein CAMSAP2 specifically localizes to non-centrosomal microtubule minus-ends and is required for proper microtubule organization in neurons.
MicroRNA-126 modulates the tumor microenvironment by targeting calmodulin-regulated spectrin-associated protein 1 (Camsap1).
Gu et al., Shenyang, China. In Int J Oncol, 2014
The expression of Camsap1 mRNA and protein is higher in cancer tissues compared to that in normal tissues.
Regulation of microtubule minus-end dynamics by CAMSAPs and Patronin.
Vale et al., San Francisco, United States. In Proc Natl Acad Sci U S A, 2014
A variety of proteins act on MT ends to regulate their dynamics, including a recently described family of MT minus-end binding proteins called calmodulin-regulated spectrin-associated protein (CAMSAP)/Patronin/Nezha. Patronin, the single member of this family in Drosophila, was previously shown to stabilize MT minus-ends against depolymerization in vitro and in vivo.
Microtubule minus-end stabilization by polymerization-driven CAMSAP deposition.
Akhmanova et al., Utrecht, Netherlands. In Dev Cell, 2014
Here, we focus on the mechanisms underlying the regulation of microtubule minus-ends by the CAMSAP/Nezha/Patronin protein family.
CAMSAPs add to the growing microtubule minus-end story.
Cassimeris et al., Bethlehem, United States. In Dev Cell, 2014
(2014) in this issue of Developmental Cell shows how mammalian CAMSAP proteins stabilize minus ends, providing a key piece to the puzzle of how these minus ends are formed and stabilized.
A conserved sequence in calmodulin regulated spectrin-associated protein 1 links its interaction with spectrin and calmodulin to neurite outgrowth.
Baines et al., Kent, United States. In J Neurochem, 2014
Calmodulin regulated spectrin-associated protein 1 (CAMSAP1) is a vertebrate microtubule-binding protein, and a representative of a family of cytoskeletal proteins that arose with animals.
PTRN-1, a microtubule minus end-binding CAMSAP homolog, promotes microtubule function in Caenorhabditis elegans neurons.
Shen et al., Stanford, United States. In Elife, 2013
In this study, we used live fluorescence microscopy to show that the C. elegans CAMSAP protein PTRN-1 localizes to puncta along neuronal processes, stabilizes MT foci, and promotes MT polymerization in neurites.
The Caenorhabditis elegans microtubule minus-end binding homolog PTRN-1 stabilizes synapses and neurites.
Nonet et al., Saint Louis, United States. In Elife, 2013
CAMSAP homologs associate with microtubule minus-ends, and are important for the stability of epithelial cell adhesions.
Nezha/CAMSAP3 and CAMSAP2 cooperate in epithelial-specific organization of noncentrosomal microtubules.
Takeichi et al., Kōbe, Japan. In Proc Natl Acad Sci U S A, 2013
These two CAMSAP molecules coclustered at the minus ends of noncentrosomal microtubules and thereby stabilized them.
The astrocytic lineage marker calmodulin-regulated spectrin-associated protein 1 (Camsap1): phenotypic heterogeneity of newly born Camsap1-expressing cells in injured mouse brain.
Kawano et al., Tokyo, Japan. In J Comp Neurol, 2012
Calmodulin-regulated spectrin-associated protein 1 (Camsap1) has been recognized as a new marker for astrocytic lineage cells and is expressed on mature astrocytes in the adult brain (Yamamoto et al. [2009] J. Neurosci.
The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4 family of animal proteins.
Phillips et al., Canterbury, United Kingdom. In Mol Biol Evol, 2009
The CKK domain binds microtubules and represents a domain that evolved with the metazoa.
A new monoclonal antibody, A3B10, specific for astrocyte-lineage cells recognizes calmodulin-regulated spectrin-associated protein 1 (Camsap1).
Asou et al., Tokyo, Japan. In J Neurosci Res, 2009
Screening a cDNA library derived from rat embryonic brain has revealed that the antibody recognizes calmodulin-regulated spectrin-associated protein 1 (Camsap1).
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