Addgene - Jeff Wrana Lab Plasmids

The Jeff Wrana Lab has deposited plasmids at Addgene for distribution to academic researchers. Addgene is a non-profit plasmid repository dedicated to improving life science research.

Learn more about research in the Jeff Wrana Lab.

Browse by Plasmid

Title	Authors
The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates.	Ogunjimi et al
Regulation of planar cell polarity by Smurf ubiquitin ligases.	Narimatsu et al
TAZ controls Smad nucleocytoplasmic shuttling and regulates human embryonic stem-cell self-renewal.	Varelas et al
Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity.	Ozdamar et al
Regulation of cell polarity and protrusion formation by targeting RhoA for degradation.	Wang et al
Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation.	Kavsak et al
A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation.	Zhu et al
SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor.	Tsukazaki et al
Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2.	Macias-Silva et al
Smad2 and Smad3 positively and negatively regulate TGF beta-dependent transcription through the forkhead DNA-binding protein FAST2.	Labbe et al
The Tlx-2 homeobox gene is a downstream target of BMP signalling and is required for mouse mesoderm development.	Tang et al
The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling.	Hayashi et al
MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling.	Macias-Silva et al
MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma.	Eppert et al
MADR1, a MAD-related protein that functions in BMP2 signaling pathways.	Hoodless et al
GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex.	Wieser et al
TGF beta signals through a heteromeric protein kinase receptor complex.	Wrana et al
pAR3-L ux
HA-TBRII