Skip to search formSkip to main contentSkip to account menu

RANBP10 gene

Known as: RANBP10, RAN binding protein 10, KIAA1464 
National Institutes of Health

Related topics

Related topics

1 relation

Broader (1)

Genes

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2018
Review
2018
Scorpins in the DNA Damage Response
The DNA Damage Response (DDR) is a complex signaling network that comes into play when cells experience genotoxic stress. Upon… 
2017
2017
miR-196 a Enhances Neuronal Morphology through Suppressing RANBP 10 to Provide Neuroprotection in Huntington ’ s Disease
MicroRNAs (miRNAs) play important roles in several neurobiological processes, including the development and progression of… 
2013
2013
lacking RanBP10 Altered microtubule equilibrium and impaired thrombus stability in mice
2012
2012
Altered microtubule equilibrium and impaired thrombus stability in mice lacking RanBP10.
The crucial function of blood platelets in hemostasis is to prevent blood loss by stable thrombus formation. This process is… 
2009
2009
Getting in shape with RanBP10.
In this issue of Blood , Kunert and colleagues have characterized mice lacking RanBP10, demonstrating an essential role for this… 
Highly Cited
2008
Highly Cited
2008
RanBP10 Is a Cytoplasmic Guanine Nucleotide Exchange Factor That Modulates Noncentrosomal Microtubules*
Microtubule spindle assembly in mitosis is stimulated by Ran·GTP, which is generated along condensed chromosomes by the guanine… 
2008
2008
RanBP10 acts as a novel coactivator for the androgen receptor.
Highly Cited
2005
Highly Cited
2005
The SPRY Domain-containing SOCS Box Protein 1 (SSB-1) Interacts with MET and Enhances the Hepatocyte Growth Factor-induced Erk-Elk-1-Serum Response Element Pathway*
The suppressor of cytokine signaling (SOCS) protein family includes a SPRY (repeats in splA and RyR) domain-containing SOCS box… 
2005
2005
RanBP10 Is a Cytoplasmic GDP/GTP Exchange Factor That Modulates Microtubule Dynamics in Late Megakaryocytes.
Megakaryocytes are large cells within the bone marrow that undergo complex fragmentation to release up to thousands of virtually… 
2004
2004
A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling.
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)