![Potential mechanisms of microtubule plus-end tracking. (A) Motor-driven... | Download Scientific Diagram Potential mechanisms of microtubule plus-end tracking. (A) Motor-driven... | Download Scientific Diagram](https://www.researchgate.net/profile/Holly-Goodson/publication/7639362/figure/fig1/AS:277698808172555@1443219964047/Potential-mechanisms-of-microtubule-plus-end-tracking-A-Motor-driven-transport_Q320.jpg)
Potential mechanisms of microtubule plus-end tracking. (A) Motor-driven... | Download Scientific Diagram
CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engageme
![The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner - Journal of Biological Chemistry The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner - Journal of Biological Chemistry](https://www.jbc.org/cms/asset/d288be60-eda7-4724-b70d-4624167f26bb/gr3.jpg)
The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner - Journal of Biological Chemistry
![Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | bioRxiv Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | bioRxiv](https://www.biorxiv.org/content/biorxiv/early/2021/01/01/2021.01.01.424687/F4.large.jpg)
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | bioRxiv
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | PLOS ONE
![Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition | PNAS Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition | PNAS](https://www.pnas.org/cms/10.1073/pnas.0703876104/asset/3765d2dd-d473-4171-92c9-89cf8d9785e6/assets/graphic/zpq0230766060002.jpeg)
Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition | PNAS
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 engagement - ScienceDirect CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engagement - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S153458072100767X-fx1.jpg)
CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engagement - ScienceDirect
![The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis](https://genesdev.cshlp.org/content/19/20/2501/F4.large.jpg)
The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis
![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)
Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes - ScienceDirect
![Ubiquitination of CLIP-170 family protein restrains polarized growth upon DNA replication stress | Nature Communications Ubiquitination of CLIP-170 family protein restrains polarized growth upon DNA replication stress | Nature Communications](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41467-022-33311-y/MediaObjects/41467_2022_33311_Fig1_HTML.png)
Ubiquitination of CLIP-170 family protein restrains polarized growth upon DNA replication stress | Nature Communications
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | PLOS ONE
![The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis](https://genesdev.cshlp.org/content/19/20/2501/F3.large.jpg)
The microtubule plus-end-tracking protein CLIP-170 associates with the spermatid manchette and is essential for spermatogenesis
![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
![Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration | Cell Death & Disease Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration | Cell Death & Disease](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41419-022-05306-6/MediaObjects/41419_2022_5306_Fig1_HTML.png)