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Originale rapina Affascinante clip 170 protein Ospite di rovinato Matematica

HIV‐1 capsids mimic a microtubule regulator to coordinate early stages of  infection | The EMBO Journal
HIV‐1 capsids mimic a microtubule regulator to coordinate early stages of infection | The EMBO Journal

RCSB PDB - 2E3H: Crystal structure of the CLIP-170 CAP-Gly domain 2
RCSB PDB - 2E3H: Crystal structure of the CLIP-170 CAP-Gly domain 2

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

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

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

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

AMPK controls the speed of microtubule polymerization and directional cell  migration through CLIP-170 phosphorylation | Nature Cell Biology
AMPK controls the speed of microtubule polymerization and directional cell migration through CLIP-170 phosphorylation | Nature Cell Biology

CLIP‐170 spatially modulates receptor tyrosine kinase recycling to  coordinate cell migration - Zaoui - 2019 - Traffic - Wiley Online Library
CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration - Zaoui - 2019 - Traffic - Wiley Online Library

CLIP170 Recombinant Rabbit Monoclonal Antibody [JE63-82] (HA721004) – HUABIO
CLIP170 Recombinant Rabbit Monoclonal Antibody [JE63-82] (HA721004) – HUABIO

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

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

Model for plus-end tracking activity of mammalian EB1 and CLIP-170. (A)...  | Download Scientific Diagram
Model for plus-end tracking activity of mammalian EB1 and CLIP-170. (A)... | Download Scientific Diagram

CLIP1 Antibodies & ELISA Kits, CLIP170 Proteins
CLIP1 Antibodies & ELISA Kits, CLIP170 Proteins

PS1 as an anchor of vesicles for CLIP-170. A) Diagrammatic... | Download  Scientific Diagram
PS1 as an anchor of vesicles for CLIP-170. A) Diagrammatic... | Download Scientific Diagram

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

RCSB PDB - 2E3I: Crystal structure of the CLIP-170 CAP-Gly domain 1
RCSB PDB - 2E3I: Crystal structure of the CLIP-170 CAP-Gly domain 1

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

LKB1 and AMP‐activated protein kinase: regulators of cell polarity - Nakano  - 2012 - Genes to Cells - Wiley Online Library
LKB1 and AMP‐activated protein kinase: regulators of cell polarity - Nakano - 2012 - Genes to Cells - Wiley Online Library

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

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

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

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

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

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

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

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

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

Microtubule “Plus-End-Tracking Proteins”: Cell
Microtubule “Plus-End-Tracking Proteins”: Cell

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