Paul H Wen
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Explore the profile of Paul H Wen including associated specialties, affiliations and a list of published articles.
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21
Citations
506
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Recent Articles
1.
Frohn M, Liu L, Siegmund A, Qian W, Amegadzie A, Chen N, et al.
Bioorg Med Chem Lett
. 2020 Jun;
30(14):127240.
PMID: 32527542
The (Z)-fluoro-olefin amide bioisosteric replacement is an effective tool for addressing various shortcomings of the parent amide. In an effort to fine tune ADME properties of BACE1 preclinical candidate AM-6494,...
2.
Pettus L, Bourbeau M, Bradley J, Bartberger M, Chen K, Hickman D, et al.
J Med Chem
. 2019 Oct;
63(5):2263-2281.
PMID: 31589043
β-Site amyloid precursor protein cleaving enzyme 1 (BACE1) is an aspartyl protease that plays a key role in the production of amyloid β (Aβ) in the brain and has been...
3.
Cheng Y, Brown J, Judd T, Lopez P, Qian W, Powers T, et al.
ACS Med Chem Lett
. 2015 Feb;
6(2):210-5.
PMID: 25699151
BACE1 inhibition to prevent Aβ peptide formation is considered to be a potential route to a disease-modifying treatment for Alzheimer's disease. Previous efforts in our laboratory using a combined structure-...
4.
Chen J, Liu Q, Yuan C, Gore V, Lopez P, Ma V, et al.
Bioorg Med Chem Lett
. 2015 Jan;
25(4):767-74.
PMID: 25613679
The β-site amyloid precursor protein (APP) cleaving enzyme 1 (BACE1) is one of the most hotly pursued targets for the treatment of Alzheimer's disease. We used a structure- and property-based...
5.
Epstein O, Bryan M, Cheng A, Derakhchan K, Dineen T, Hickman D, et al.
J Med Chem
. 2014 Nov;
57(23):9796-810.
PMID: 25389560
The optimization of a series of aminooxazoline xanthene inhibitors of β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is described. An early lead compound showed robust Aβ lowering activity in...
6.
Dineen T, Chen K, Cheng A, Derakhchan K, Epstein O, Esmay J, et al.
J Med Chem
. 2014 Nov;
57(23):9811-31.
PMID: 25363711
We have previously shown that the aminooxazoline xanthene scaffold can generate potent and orally efficacious BACE1 inhibitors although certain of these compounds exhibited potential hERG liabilities. In this article, we...
7.
Kaller M, Harried S, Albrecht B, Amarante P, Babu-Khan S, Bartberger M, et al.
ACS Med Chem Lett
. 2014 Jun;
3(11):886-91.
PMID: 24900403
β-Secretase inhibitors are potentially disease-modifying treatments for Alzheimer's disease. Previous efforts in our laboratory have resulted in hydroxyethylamine-derived inhibitors such as 1 with low nanomolar potency against β-site amyloid precursor...
8.
Chen J, Qian W, Biswas K, Yuan C, Amegadzie A, Liu Q, et al.
Bioorg Med Chem Lett
. 2013 Oct;
23(23):6447-54.
PMID: 24139583
γ-Secretase modulators (GSMs) are potentially disease-modifying treatments for Alzheimer's disease. They selectively lower pathogenic Aβ42 levels by shifting the enzyme cleavage sites without inhibiting γ-secretase activity, possibly avoiding known adverse...
9.
Huang H, La D, Cheng A, Whittington D, Patel V, Chen K, et al.
J Med Chem
. 2012 Aug;
55(21):9156-69.
PMID: 22928914
A structure- and property-based drug design approach was employed to identify aminooxazoline xanthenes as potent and selective human β-secretase inhibitors. These compounds exhibited good isolated enzyme, cell potency, and selectivity...
10.
Wood S, Wen P, Zhang J, Zhu L, Luo Y, Babu-Khan S, et al.
J Pharmacol Exp Ther
. 2012 Aug;
343(2):460-7.
PMID: 22911925
Sequential proteolytic cleavage of the amyloid precursor protein (APP) by β-site APP-cleaving enzyme 1 (BACE1) and the γ-secretase complex produces the amyloid-β peptide (Aβ), which is believed to play a...