Zobrazeno 1 - 10
of 89
pro vyhledávání: '"Grant A. Krafft"'
ACU193: An Immunotherapeutic Poised to Test the Amyloid β Oligomer Hypothesis of Alzheimer’s Disease
Publikováno v:
Frontiers in Neuroscience, Vol 16 (2022)
Alzheimer’s disease (AD) is an age-related neurodegenerative disease that affects 50 million people worldwide, with 10 million new cases occurring each year. The emotional and economic impacts of AD on patients and families are devastating. Approve
Externí odkaz:
https://doaj.org/article/4971a750ae7b43df80daa863a1f35673
Autor:
William L. Klein, Wei Qin Zhao, Pascale N. Lacor, Hui Chen, Michael J. Quon, Grant A. Krafft, Mary P. Lambert
Publikováno v:
Journal of Biological Chemistry. 284:18742-18753
Accumulation of amyloid beta (Abeta) oligomers in the brain is toxic to synapses and may play an important role in memory loss in Alzheimer disease. However, how these toxins are built up in the brain is not understood. In this study we investigate w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f8eff4b2b66ead76e0575cafc24297e
https://doi.org/10.1074/jbc.m109.011015
https://doi.org/10.1074/jbc.m109.011015
Autor:
Caleb E. Finch, Kirsten L. Viola, Mary P. Lambert, Lei Chang, Jiaxin Yu, Todd E. Morgan, Brett A. Chromy, Duane L. Venton, William L. Klein, Grant A. Krafft
Publikováno v:
Journal of Neurochemistry. 79:595-605
In recent studies of transgenic models of Alzheimer's disease (AD), it has been reported that antibodies to aged beta amyloid peptide 1-42 (Abeta(1-42)) solutions (mixtures of Abeta monomers, oligomers and amyloid fibrils) cause conspicuous reduction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::96098a176f10436a2a383b9568dfcf66
https://doi.org/10.1046/j.1471-4159.2001.00592.x
https://doi.org/10.1046/j.1471-4159.2001.00592.x
Autor:
Raymond Lowe, Jean-Claude R. Breach, Todd Pray, Michele McEntee, Hsiu-Mei Wu, Catherine M. Hironaka, Lily Ruslim-Litrus, Sue Zhang, David Summa, Susan M. Catalano, Gary C. Look, Jasna Jerecic, Walter J. Crosier, Lev Igoudin, Diana B. Cherbavaz, William F. Goure, Grant A. Krafft
Publikováno v:
Current Alzheimer Research. 4:562-567
Amyloid beta-derived diffusible ligands (ADDLs) comprise the neurotoxic subset of soluble Abeta(1-42) oligomers, now widely considered to be the molecular cause of memory malfunction and neurodegeneration in Alzheimer's disease (AD). We have develope
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3db0afa4f0f31c5abbedaaa031bf9029
https://doi.org/10.2174/156720507783018271
https://doi.org/10.2174/156720507783018271
Autor:
Pauline T. Velasco, Daliya Khuon, Pascale N. Lacor, Eileen H. Bigio, Yuesong Gong, Pamela L Shaw, Grant A. Krafft, Fernanda G. De Felice, Lei Chang, Sara J. Fernandez, Kirsten L. Viola, Mary P. Lambert, William L. Klein
Publikováno v:
Journal of Neurochemistry. 100:23-35
Amyloid beta (Abeta) immunotherapy for Alzheimer's disease has shown initial success in mouse models of Alzheimer's disease and in human patients. However, because of meningoencephalitis in clinical trials of active vaccination, approaches using ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e258430f3eae3f2fab01c32c59526fa
https://doi.org/10.1111/j.1471-4159.2006.04157.x
https://doi.org/10.1111/j.1471-4159.2006.04157.x
Autor:
Elizabeth Chen Dodson, Susan M. Catalano, Darrell A. Henze, Gene G. Kinney, Grant A. Krafft, Joseph G. Joyce
Publikováno v:
Current Topics in Medicinal Chemistry. 6:597-608
The amyloid-beta (Abeta) cascade hypothesis of Alzheimer's disease (AD) has dominated research and subsequent therapeutic drug development for over two decades. Central to this hypothesis is the observation that Abeta is elevated in AD patients and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93b2f845392c2d4932389951cdbfeae7
https://doi.org/10.2174/156802606776743066
https://doi.org/10.2174/156802606776743066
Autor:
Grant A. Krafft, William L. Klein, Lei Chang, Bryan W. Jones, Pascale N. Lacor, Sara J. Fernandez, Kirsten L. Viola, Brett A. Chromy, Peleg M. Horowitz, Mary P. Lambert, Caleb E. Finch, Richard Nowak, Pauline T. Velasco
Publikováno v:
Biochemistry. 42:12749-12760
Amyloid beta 1-42 (Abeta(1-42)) is a self-associating peptide that becomes neurotoxic upon aggregation. Toxicity originally was attributed to the presence of large, readily formed Abeta fibrils, but a variety of other toxic species are now known. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2744812cb68e7c0bc2200daa3327690f
https://doi.org/10.1021/bi030029q
https://doi.org/10.1021/bi030029q
Autor:
Mary Jo LaDu, Arlene M. Manelli, Grant A. Krafft, W. Blaine Stine, Lorinda K. Baker, Karie N. Dahlgren
Publikováno v:
Journal of Biological Chemistry. 277:32046-32053
Genetic evidence predicts a causative role for amyloid-beta (A beta) in Alzheimer's disease. Recent debate has focused on whether fibrils (amyloid) or soluble oligomers of A beta are the active species that contribute to neurodegeneration and dementi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a50c189ded797f00907380a7e5d363ce
https://doi.org/10.1074/jbc.m201750200
https://doi.org/10.1074/jbc.m201750200
Publikováno v:
Trends in Neurosciences. 24:219-224
Amyloid beta (Abeta) is a small self-aggregating peptide produced at low levels by normal brain metabolism. In Alzheimer's disease (AD), self-aggregation of Abeta becomes rampant, manifested most strikingly as the amyloid fibrils of senile plaques. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e30aeead5157463e6999e3750b0913e9
https://doi.org/10.1016/s0166-2236(00)01749-5
https://doi.org/10.1016/s0166-2236(00)01749-5
Publikováno v:
Journal of Biological Chemistry. 274:24431-24437
The Saccharomyces cerevisiae YPS2 (formerly MKC7) gene product is a glycosylphosphatidylinositol-linked aspartyl protease that functions as a yeast secretase. Here, the glycosylphosphatidylinositol-linked form of yapsin 2 (Mkc7p) was purified to homo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d51bdbadd9f162e90473eb75589669d9
https://doi.org/10.1074/jbc.274.34.24431
https://doi.org/10.1074/jbc.274.34.24431