Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Desiree Watson"'
Autor:
Dean C. Luehrs, Sangram S. Sisodia, Alex E. Roher, Mark R. Emmerling, M. Desiree Watson, Daniel C. Brune, Tyler A. Kokjohn, Yu Min Kuo, Walter M. Kalback, Nicole Weiss, Matthias Staufenbiel, John Lopez
Publikováno v:
Biochemistry. 41:922-928
The amyloid (Abeta) peptides generated in Hsiao's APP Tg2576 transgenic (Tg) mice are physically and chemically distinct from those characteristic of Alzheimer's disease (AD). Transgenic mouse Abeta peptides were purified using sequential size-exclus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::73349e873c59d201dbecca3566e70d24
https://doi.org/10.1021/bi015685+
https://doi.org/10.1021/bi015685+
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1502(1):158-171
Complement proteins are integral components of amyloid plaques and cerebral vascular amyloid in Alzheimer brains. They can be found at the earliest stages of amyloid deposition and their activation coincides with the clinical expression of Alzheimer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48a91b7d63d01b6bbd15267f5d42d144
Autor:
Walter Michael, Cuiman Cai, M. Desiree Watson, Lori M. Evans, Kevin K.W. Wang, Mark R. Emmerling, John L. Gilmore, Sheryl J. Hays, Lakshmi S. Narasimhan, Juan C. Jaen, Janet S. Plummer, Rathna Nath
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 9:815-820
A series of 2-sulfonyl-4H-3,1-benzoxazinones was prepared that inhibit C1r protease in vitro. Several compounds were found to be selective for C1r verses the related serine protease trypsin. Selected compounds demonstrated functional activity in a he
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e738565a315f9d0c187febdcfe15521a
https://doi.org/10.1016/s0960-894x(99)00095-5
https://doi.org/10.1016/s0960-894x(99)00095-5
Autor:
Desiree Watson, John L. Gilmore, Juan C. Jaen, Daniel Stafford, Nilam Amin, Rathna Nath, Ravi Nadimpalli, Kevin K.W. Wang, Bradley William Caprathe, Sheryl J. Hays, Kadee J. Raser, Walter Michael, Mark R. Emmerling
Publikováno v:
Journal of Medicinal Chemistry. 41:1060-1067
A series of 2-amino-4H-3,1-benzoxazin-4-ones have been synthesized and evaluated as inhibitors of the complement enzyme C1r. C1r is a serine protease at the beginning of the complement cascade, and complement activation by beta-amyloid may represent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::806e519321a1a2f2fc9825d26ce2597b
https://doi.org/10.1021/jm970394d
https://doi.org/10.1021/jm970394d
Publikováno v:
Amyloid. 4:147-156
Complement activation and its deposition on β-amyloid plaques in Alzheimer's Disease (AD) brains correlates with the development of AD dementia. Results from immunocytochemical studies suggest that the appearance of complement activation in AD brain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bec95f801384bcf64a3bb88dbe4fd9f6
https://doi.org/10.3109/13506129709014379
https://doi.org/10.3109/13506129709014379
Autor:
Mark R. Emmerling, W. Blaine Stine, Linda M. Rowse, Chera Esh, Tyler A. Kokjohn, Eduardo M. Castaño, E. Sander Connolly, Dean C. Luehrs, Yu Min Kuo, Desiree Watson, David J. Pinsky, Yuri L. Lyubchenko, Alex E. Roher
Publikováno v:
Neurological research. 27(8)
Extracellular fibrillar amyloid deposits are prominent and universal Alzheimer's disease (AD) features, but senile plaque abundance does not always correlate directly with the degree of dementia exhibited by AD patients. The mechanism(s) and dynamics
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::806ed8f2b442e34a21a5e3275ad04a7e
https://pubmed.ncbi.nlm.nih.gov/16354549
https://pubmed.ncbi.nlm.nih.gov/16354549
Autor:
Alex E. Roher, Tyler A. Kokjohn, Douglas G. Walker, Jacqueline Anthony, Yu Min Kuo, Walter M. Kalback, Nicole Weiss, Desiree Watson, Thomas G. Beach, Dean C. Luehrs, Lucia I. Sue, Mark R. Emmerling, Warren J. Goux
Publikováno v:
Biochemistry. 41(37)
Relative to the gray matter, there is a paucity of information regarding white matter biochemical alterations and their contribution to Alzheimer's disease (AD). Biochemical analyses of AD white matter combining size-exclusion, normal phase, and gas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be2660a122607d90f7f1c9168819663c
https://pubmed.ncbi.nlm.nih.gov/12220172
https://pubmed.ncbi.nlm.nih.gov/12220172
Autor:
Walter, Kalback, M Desiree, Watson, Tyler A, Kokjohn, Yu-Min, Kuo, Nicole, Weiss, Dean C, Luehrs, John, Lopez, Daniel, Brune, Sangram S, Sisodia, Matthias, Staufenbiel, Mark, Emmerling, Alex E, Roher
Publikováno v:
Biochemistry. 41(3)
The amyloid (Abeta) peptides generated in Hsiao's APP Tg2576 transgenic (Tg) mice are physically and chemically distinct from those characteristic of Alzheimer's disease (AD). Transgenic mouse Abeta peptides were purified using sequential size-exclus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ec94f3d80cdf5c0254220badb4445a80
https://pubmed.ncbi.nlm.nih.gov/11790115
https://pubmed.ncbi.nlm.nih.gov/11790115
Autor:
Tyler A. Kokjohn, Mark R. Emmerling, M. Desiree Watson, Amina S. Woods, Yu Min Kuo, Walter M. Kalback, Robert J. Cotter, Lucia I. Sue, Thomas G. Beach, Alex E. Roher
The levels of amyloid-beta40 (Abeta40) and Abeta42 peptides were quantified in temporalis muscles and brain of neuropathologically diagnosed Alzheimer disease (AD) and of nondemented individuals. This was achieved by using a novel analytical approach
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abfb29d133c9d0badb5789fb3b0eef4f
https://europepmc.org/articles/PMC1876838/
https://europepmc.org/articles/PMC1876838/
Autor:
Karl L. Brown, Taraneh Haske, M. Desiree Watson, Kathryn Spiegel, Charlotte Raby, Harry LeVine, Mark R. Emmerling, Lori M. Evans
Publikováno v:
Neurobiology of Aging. 21:90
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eab4daacc28b3d6b590a422a2e943c6e
https://doi.org/10.1016/s0197-4580(00)82630-5
https://doi.org/10.1016/s0197-4580(00)82630-5