Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Laura Trescott"'
Publikováno v:
Current Drug Targets. 16:945-950
PDZ domains play an essential role in a number of cellular processes by facilitating protein scaffolding and assembly of protein complexes. These domains consist of 80 to 90 amino acids and are found to recognize short C-terminal sequences of target
Autor:
Xiaobing Shi, Joshua Holcomb, Laura Trescott, Xi Zhang, Nualpun Sirinupong, Zhe Yang, Joseph S. Brunzelle, Yuanyuan Jiang
Publikováno v:
Journal of Molecular Biology. 426:3413-3425
Estrogen receptor (ER) signaling plays a pivotal role in many developmental processes and has been implicated in numerous diseases including cancers. We recently showed that direct ERα methylation by the multi-specificity histone lysine methyltransf
Autor:
Yuanyuan Jiang, Xiaoqing Guan, Chunying Li, Joshua Holcomb, Joseph S. Brunzelle, Zhe Yang, Nualpun Sirinupong, Yuning Hou, Laura Trescott, Shuo Wang
Publikováno v:
Biochemical and Biophysical Research Communications. 446:638-643
The formation of CXCR2–NHERF1–PLCβ3 macromolecular complex in pancreatic cancer cells regulates CXCR2 signaling activity and plays an important role in tumor proliferation and invasion. We previously have shown that disruption of the NHERF1-medi
Autor:
Guorong Lu, Joshua Holcomb, Nualpun Sirinupong, Anjaparavanda P. Naren, Laura Trescott, Chunying Li, Zhe Yang, Yuanyuan Jiang, Joseph S. Brunzelle
Publikováno v:
Biochemical and Biophysical Research Communications. 446:399-403
The formation of CFTR–NHERF2–LPA2 macromolecular complex in airway epithelia regulates CFTR channel function and plays an important role in compartmentalized cAMP signaling. We previously have shown that disruption of the PDZ-mediated NHERF2–LP
Autor:
Joshua Holcomb, Zhe Yang, Nicholas Spellmon, Chunying Li, Fei Sun, Leala Aljehane, Laura Trescott, Cathy Mcleod
Publikováno v:
Current drug targets. 16(9)
Cystic Fibrosis (CF) is a serious genetic condition caused by CF transmembrane conductance regulator (CFTR) mutation. CF patients have shortened lifespan due to airway obstruction, infection, and end-stage lung failure. However, recent development in
Autor:
Xiaoqing Guan, Chunying Li, Shuo Wang, Zhe Yang, Guorong Lu, Yuning Hou, Yuanyuan Jiang, Laura Trescott, Joseph S. Brunzelle, Nualpun Sirinupong, Joshua Holcomb
Publikováno v:
Biochemical and biophysical research communications. 448(2)
The formation of CXCR2–NHERF1–PLCβ2 macromolecular complex in neutrophils regulates CXCR2 signaling and plays a key role in neutrophil chemotaxis and transepithelial neutrophilic migration. However, NHERF1 by itself, with only two PDZ domains, h
Autor:
Xiaobing Shi, Yuanyuan Jiang, Joseph S. Brunzelle, Zhe Yang, Joshua Holcomb, Laura Trescott, Nualpun Sirinupong
Publikováno v:
The FASEB Journal. 28
Estrogen receptor (ER) signaling plays a pivotal role in many developmental processes and has been implicated in numerous diseases including cancers. We recently showed that direct ERα methylation by the multi-specificity histone lysine methyltransf
Autor:
Laura Trescott, Yuanyuan Jiang, Nualpun Sirinupong, Zhe Yang, Xiaoqing Guan, Yuning Hou, Shuo Wang, Angelique Stamenkovich, Guorong Lu, Chunying Li, Joseph S. Brunzelle
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 12, p e81904 (2013)
PLoS ONE, Vol 8, Iss 12, p e81904 (2013)
NHERF1 is a PDZ adaptor protein that scaffolds the assembly of diverse signaling complexes and has been implicated in many cancers. However, little is known about the mechanism responsible for its scaffolding promiscuity or its ability to bind to mul
Autor:
Spellmon, Nicholas1 nicholas.spellmon@wayne.edu, Holcomb, Joshua1 jholcomb@med.wayne.edu, Trescott, Laura1 ef6996@wayne.edu, Sirinupong, Nualpun2 nualpun.s@psu.ac.th, Zhe Yang1 zyang@med.wayne.edu
Publikováno v:
International Journal of Molecular Sciences. 2015, Vol. 16 Issue 1, p1406-1428. 23p. 8 Diagrams.
Autor:
Jiang, Yuanyuan, Trescott, Laura, Holcomb, Joshua, Brunzelle, Joseph, Sirinupong, Nualpun, Shi, Xiaobing, Yang, Zhe
Publikováno v:
FASEB Journal; Apr2014 Supplement S1, Vol. 28, pN.PAG-N.PAG, 1p