|1.||Kim, Won Tae: 2 articles (02/2007 - 02/2006)|
|2.||Lee, Dae-Weon: 2 articles (02/2007 - 02/2006)|
|3.||Boo, Kyung Saeng: 2 articles (02/2007 - 02/2006)|
|4.||Olafson, Pia U: 1 article (08/2010)|
|5.||Temeyer, Kevin B: 1 article (08/2010)|
|6.||Pruett, John H: 1 article (08/2010)|
|7.||Song, Jong Tae: 1 article (02/2007)|
|8.||Chung, Bu Keun: 1 article (02/2007)|
|9.||Koh, Young Ho: 1 article (02/2007)|
|10.||Choi, Jae Young: 1 article (02/2007)|
02/16/2007 - "The biochemical properties of expressed AChEs showed substrate specificity for acetylthiocholine iodide and inhibitor specificity for BW284C51 and eserine. "
02/01/2006 - "The biochemical properties of purified proteins by affinity chromatography showed substrate specificity for acetylthiocholine iodide, and inhibitor specificity for BW284C51 and eserine and their peptide sequences partially identified by a MALDI-TOF mass spectrometer demonstrated that two Ha-AChEs were expressed in vivo."
05/23/1997 - "AChE inhibitors acting at the active site (edrophonium, tacrine) and at the peripheral site (propidium, fasciculin), as well as bis-quaternary ligands (BW284C51, decamethonium), were tested against the venom AChEs from 11 different species. "
08/27/2010 - "Biochemical characterization of the recombinant proteins supports classification of rBmAChE1, rBmAChE2, and rBmAChE3 as AChEs (E.C.220.127.116.11), as evidenced by (i) substrate preference for acetylthiocholine, (ii) inhibition by eserine, BW284c51, and the organophosphates (OPs) malaoxon and paraoxon, (iii) insensitivity to iso-OMPA, and (iv) rapid hydrolysis of acetyl-beta-methyl-thiocholine. "
05/19/1999 - "We have observed that the specific acetylcholinesterase peripheral anionic site inhibitors, BW284c51 and propidium iodide, abrogated cell-substrate adhesion in three human neuroblastoma cell lines. "
04/25/1981 - "The cellular localization of the molecular forms of acetylcholinesterase was explored in chick sympathetic neurons and in mouse T28 cells (neuroblastoma X sympathetic ganglion cell hybrids) using the reversible, poorly lipid-soluble inhibitor of acetylcholinesterase, BW284C51, to protect cell surface activity while inactivating cytoplasmic activity with DFP, an irreversible, lipid-soluble inhibitor. "
|3.||Demyelinating Diseases (Demyelinating Disease)
|4.||Alzheimer Disease (Alzheimer's Disease)
|4.||Propidium (Propidium Iodide)
|10.||Proteins (Proteins, Gene)