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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

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

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

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

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

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

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

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

Linking cortical microtubule attachment and... | F1000Research
Linking cortical microtubule attachment and... | F1000Research

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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