Zobrazeno 1 - 10
of 15
pro vyhledávání: '"A L, Brunkan"'
Publikováno v:
Neurobiology of Disease, Vol 15, Iss 3, Pp 654-666 (2004)
Generation of Aβ from the β-amyloid precursor protein (APP) requires a series of proteolytic processes, including an intramembranous cleavage catalyzed by an aspartyl protease, γ-secretase. Two aspartates in presenilins (PS) are required for γ-se
Externí odkaz:
https://doaj.org/article/8b81a50ee0cb4804bbce0399d136ab74
Autor:
Yan Zhou, Wanjiang Zhang, Rachael Easton, James W. Ray, Patricia Lampe, Zhihong Jiang, Anne L. Brunkan, Alison Goate, Eugene M. Johnson, Jane Y. Wu
Publikováno v:
Neurobiology of Disease, Vol 9, Iss 2, Pp 126-138 (2002)
Mutations in the presenilin-1 (PS-1) gene account for a significant fraction of familial Alzheimer's disease. The biological function of PS-1 is not well understood. We report here that the proliferation-associated gene (PAG) product, a protein of th
Externí odkaz:
https://doaj.org/article/ef6fa62f406e4ba9bd34e97cfda4e6b2
Publikováno v:
Molecular and Cellular Neuroscience. 29:65-73
Mutations in the presenilin genes (PS) account for most cases of familial Alzheimer's disease. PS contain the active site of the gamma-secretase complex that cleaves within the transmembrane domain of beta-amyloid precursor protein (APP). Full-length
Autor:
Alison Goate, Anne L. Brunkan
Publikováno v:
Journal of Neurochemistry. 93:769-792
Alzheimer's disease (AD) is the most common form of dementia and is characterized pathologically by the accumulation of beta-amyloid (Abeta) plaques and neurofibrillary tangles in the brain. Genetic studies of AD first highlighted the importance of t
Publikováno v:
Journal of Neurochemistry. 92:1158-1169
The structural requirements for presenilin (PS) to produce active presenilinase and γ-secretase enzymes are poorly understood. Here we investigate the role the cytoplasmic C-terminal region of PS1 plays in PS1 activity. Deletion or addition of resid
Autor:
Anne L. Brunkan-LaMontagne, Richard F. Collins, Chris Whitfield, Robert C. Ford, Robert J. Harris, James H. Naismith, Bradley R. Clarke
Publikováno v:
Journal of structural biology. 166(2)
The outer membrane protein Wza, from Escherichia coli K30, forms an octameric complex that is essential for capsular polysaccharide export. Homologs of Wza are widespread in gram-negative bacterial pathogens where capsules are critical virulence dete
Autor:
Jutta Nesper, Bradley R. Clarke, James H. Naismith, Changjiang Dong, Chris Whitfield, Anne L. Brunkan-LaMontagne, Konstantinos Beis
Publikováno v:
Nature. 444(7116)
Pathogenic bacteria frequently cloak themselves with a capsular polysaccharide layer. Escherichia coli group 1 capsules are formed from repeat-unit polysaccharides with molecular weights exceeding 100 kDa. The export of such a large polar molecule ac
Autor:
Jennifer X. Wang, Anne L. Brunkan, Dirk Beher, Mark S. Shearman, Maribel Martinez, Alison Goate, Emily S. Walker
Publikováno v:
Journal of neurochemistry. 94(5)
Presenilins (PS) are thought to contain the active site for presenilinase endoproteolysis of PS and gamma-secretase cleavage of substrates. The structural requirements for PS incorporation into the gamma-secretase enzyme complex, complex stability an
Publikováno v:
Journal of neurochemistry. 92(5)
The structural requirements for presenilin (PS) to produce active presenilinase and gamma-secretase enzymes are poorly understood. Here we investigate the role the cytoplasmic C-terminal region of PS1 plays in PS1 activity. Deletion or addition of re
Publikováno v:
Journal of neurochemistry. 92(2)
Gene knockout studies in mice suggest that presenilin 1 (PS1) is the major gamma-secretase and that it contributes disproportionately to amyloid beta (Abeta) peptide generation from beta-amyloid precursor protein (APP), whereas PS2 plays a more minor