Cdc2-mediated Phosphorylation of CLIP-170 Is Essential for Its Inhibition of Centrosome Reduplication*
Subcellular distribution of CLIP-170 throughout the mitotic cycle of... | Download Scientific Diagram
CLIP-170S is a microtubule +TIP variant that confers resistance to taxanes by impairing drug-target engagement - ScienceDirect
Quelle fonction pour la CLIP-170? : recherche de partenaires et nouveaux outils d'investigation | Semantic Scholar
Characterizing interactions between the microtubule-binding protein CLIP-170 and F-actin | bioRxiv
Domain architecture of CLIP-170 and EB1. A, domain architecture of EB1... | Download Scientific Diagram
Microtubule Capture: IQGAP and CLIP-170 Expand the Repertoire: Current Biology
α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect
Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal
CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration - Zaoui - 2019 - Traffic - Wiley Online Library
CLIP-170 and IQGAP1 Cooperatively Regulate Dendrite Morphology | Journal of Neuroscience
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular
Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration | Cell Death & Disease
CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports
CLIP-170 and IQGAP1 Cooperatively Regulate Dendrite Morphology | Journal of Neuroscience
Drosophila CLIP-190 and mammalian CLIP-170 display reduced microtubule plus end association in the nervous system | Molecular Biology of the Cell
Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition | PNAS
PS1 as an anchor of vesicles for CLIP-170. A) Diagrammatic... | Download Scientific Diagram
CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | PLOS ONE
The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner
RCSB PDB - 2E3I: Crystal structure of the CLIP-170 CAP-Gly domain 1
