Domain architecture of CLIP-170 and EB1. A, domain architecture of EB1... | Download Scientific Diagram
![Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology](https://royalsocietypublishing.org/cms/asset/56e22320-6bf0-4ef2-94c7-647a3ee7b687/rsob160274f12.jpg)
Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology
![CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41598-018-35593-z/MediaObjects/41598_2018_35593_Fig1_HTML.png)
CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports
CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engageme
CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engageme
![CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-018-35593-z/MediaObjects/41598_2018_35593_Fig4_HTML.png)
CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports
![α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S221112471630167X-fx1.jpg)
α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect
![Arsenic trioxide disturbs the LIS1/NDEL1/dynein microtubule dynamic complex by disrupting the CLIP170 zinc finger in head and neck cancer - ScienceDirect Arsenic trioxide disturbs the LIS1/NDEL1/dynein microtubule dynamic complex by disrupting the CLIP170 zinc finger in head and neck cancer - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0041008X20302842-gr8.jpg)
Arsenic trioxide disturbs the LIS1/NDEL1/dynein microtubule dynamic complex by disrupting the CLIP170 zinc finger in head and neck cancer - ScienceDirect
![CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-018-35593-z/MediaObjects/41598_2018_35593_Fig2_HTML.png)
CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports
![Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes - ScienceDirect Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0014579306001037-gr4.jpg)