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Barnalegt kaloría fóstureyðing clip 170 Bakið límmiða blýantur

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

biosights: October 26, 2015 - CLIP-170 tips its hand in viral transport -  YouTube
biosights: October 26, 2015 - CLIP-170 tips its hand in viral transport - YouTube

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

H. Goodson - Microtubule Plus-ends
H. Goodson - Microtubule Plus-ends

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

Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of  kinetochore–microtubule attachments | The EMBO Journal
Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal

Drosophila CLIP-190 and mammalian CLIP-170 display reduced microtubule plus  end association in the nervous system | Molecular Biology of the Cell
Drosophila CLIP-190 and mammalian CLIP-170 display reduced microtubule plus end association in the nervous system | Molecular Biology of the Cell

Characterizing interactions between the microtubule-binding protein CLIP-170  and F-actin | bioRxiv
Characterizing interactions between the microtubule-binding protein CLIP-170 and F-actin | bioRxiv

Interactions between CLIP-170, Tubulin, and Microtubules: Implications for  the Mechanism of CLIP-170 Plus-End Tracking Behavior | Molecular Biology of  the Cell
Interactions between CLIP-170, Tubulin, and Microtubules: Implications for the Mechanism of CLIP-170 Plus-End Tracking Behavior | Molecular Biology of the Cell

The CLIP-170 N-terminal domain binds directly to both F-actin and  microtubules in a mutually exclusive manner
The CLIP-170 N-terminal domain binds directly to both F-actin and microtubules in a mutually exclusive manner

Microtubule Capture: IQGAP and CLIP-170 Expand the Repertoire: Current  Biology
Microtubule Capture: IQGAP and CLIP-170 Expand the Repertoire: Current Biology

Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP  network superstructure consistent with a biomolecular
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular

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

CLIP-170 Antibody (F-3) | SCBT - Santa Cruz Biotechnology
CLIP-170 Antibody (F-3) | SCBT - Santa Cruz Biotechnology

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

A New Molecular Player Involved in T Cell Activation - Drug Discovery and  Development
A New Molecular Player Involved in T Cell Activation - Drug Discovery and Development

CLIP-170 and IQGAP1 Cooperatively Regulate Dendrite Morphology | Journal of  Neuroscience
CLIP-170 and IQGAP1 Cooperatively Regulate Dendrite Morphology | Journal of Neuroscience

Selective visualization of growing MT ends with CLIP170. CHO cells were...  | Download Scientific Diagram
Selective visualization of growing MT ends with CLIP170. CHO cells were... | Download Scientific Diagram

Microtubule plus-end tracking by CLIP-170 requires EB1 | PNAS
Microtubule plus-end tracking by CLIP-170 requires EB1 | PNAS

Quelle fonction pour la CLIP-170? : recherche de partenaires et nouveaux  outils d'investigation | Semantic Scholar
Quelle fonction pour la CLIP-170? : recherche de partenaires et nouveaux outils d'investigation | Semantic Scholar

Mapping multivalency in the CLIP-170–EB1 microtubule plus-end complex -  ScienceDirect
Mapping multivalency in the CLIP-170–EB1 microtubule plus-end complex - ScienceDirect

Conformational changes in CLIP-170 regulate its binding to microtubules and  dynactin localization. - Abstract - Europe PMC
Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. - Abstract - Europe PMC

Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP  network superstructure consistent with a biomolecular condensate | PLOS ONE
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | PLOS ONE

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

Cdc2-mediated Phosphorylation of CLIP-170 Is Essential for Its Inhibition  of Centrosome Reduplication*
Cdc2-mediated Phosphorylation of CLIP-170 Is Essential for Its Inhibition of Centrosome Reduplication*

Dynactin 1 negatively regulates HIV-1 infection by sequestering the host  cofactor CLIP170 | PNAS
Dynactin 1 negatively regulates HIV-1 infection by sequestering the host cofactor CLIP170 | PNAS

Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of  kinetochore–microtubule attachments | The EMBO Journal
Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal