Skip to search formSkip to main contentSkip to account menu

SNIP1 gene

Known as: SNIP1, Smad nuclear interacting protein 1 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2016
2016
Smad Nuclear Interacting Protein 1 Acts as a Protective Regulator of Pressure Overload‐Induced Pathological Cardiac Hypertrophy
Background Smad nuclear interacting protein 1 (SNIP1) plays a critical role in cell proliferation, transformation of embryonic… 
2015
2015
Smad nuclear interacting protein, SNIP1, mediates the ecdysteroid signal transduction in red crayfish Procambarus clarkii.
A smad nuclear interacting protein 1 (SNIP1) homolog was identified in the crayfish Procambarus clarkii and this gene encoded a… 
2015
2015
Retraction Note to: Silencing of the Smad nuclear interacting protein 1 (SNIP1) by siRNA inhibits proliferation and induces apoptosis in pituitary adenoma cells
2014
2014
Sniff Nasal Inspiratory Pressure Does Not Decrease in Elderly Subjects
[Purpose] Measurements of inspiratory strength are critical for detecting inspiratory muscle weakness. Sniff nasal inspiratory… 
2013
2013
High expression of SNIP1 correlates with poor prognosis in non-small cell lung cancer and SNIP1 interferes with the recruitment of HDAC1 to RB in vitro.
2012
2012
Distinct gene structure and expression pattern of Smad nuclear interacting protein 1 in amphioxus and zebrafish.
2011
2011
SNIP1: a new activator of HSE signaling pathway
In the last 10 years, more and more attention has been focused on SNIP1 (Smad nuclear interacting protein 1), which functions as… 
2007
2007
Regulation of ATR-dependent pathways by the FHA domain containing protein SNIP1
The forkhead associated (FHA) domain-containing protein Smad nuclear interacting protein 1 (SNIP1) has multiple cellular… 
Highly Cited
2004
Highly Cited
2004
The FHA domain protein SNIP1 is a regulator of the cell cycle and cyclin D1 expression
Smad nuclear interacting protein 1 (SNIP1) is an evolutionarily conserved protein containing a forkhead-associated (FHA) domain… 
Highly Cited
2001
Highly Cited
2001
SNIP1 Inhibits NF-κB Signaling by Competing for Its Binding to the C/H1 Domain of CBP/p300 Transcriptional Co-activators*
SNIP1 is a 396-amino acid nuclear protein shown to be an inhibitor of the TGF-β signal transduction pathway and to be important… 
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)