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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

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

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

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

CLIP1/CLIP170 Antibody | Cell Signaling Technology
CLIP1/CLIP170 Antibody | Cell Signaling Technology

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

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

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

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

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

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

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

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

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-170 protein interactions are regulated in an... | Download Scientific  Diagram
CLIP-170 protein interactions are regulated in an... | Download Scientific Diagram

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

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

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

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

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

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

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

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

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