Zobrazeno 1 - 10
of 20
pro vyhledávání: '"R D, Moir"'
Autor:
Patrick McGeer, StJohn Crean, Rudolph E. Tanzi, George L. W. Perry, Carl W. Cotman, Judith Miklossy, Tamas Fulop, Matthew Richard Chapman, Herbert B. Allen, R. D. Moir, Kilmer McCully
Publikováno v:
Frontiers Research Topics ISBN: 9782889639038
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d69bb9adbb117c536855e88dd495ff3c
https://doi.org/10.3389/978-2-88963-903-8
https://doi.org/10.3389/978-2-88963-903-8
Publikováno v:
Current Bioactive Compounds. 4:140-149
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d34a07e20c1208942228371ffdb95590
https://doi.org/10.2174/157340708786305989
https://doi.org/10.2174/157340708786305989
Autor:
R. D. Moir, Rudolph E. Tanzi, Craig S. Atwood, Xudong Huang, Donna M. Romano, Jonathan D. Smith, Maxwell H. Laurans, Ashley I. Bush
Publikováno v:
Biochemistry. 38:4595-4603
The epsilon 4 allele of apolipoprotein E (APOE) has been found to be a risk factor for late-onset Alzheimer's disease (AD). While the pathogenic mechanism of APOE in AD is not yet clear, APOE isoforms appear to differentially influence the aggregatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e35e1a8f74c726d5b79a595cabd6afae
https://doi.org/10.1021/bi982437d
https://doi.org/10.1021/bi982437d
Autor:
R D, Moir, R D, Goldman
Publikováno v:
Current Opinion in Cell Biology. 5:408-411
Nuclear lamins form a highly insoluble structure, the nuclear lamina, which is associated with the nuclear envelope. Recent results suggest, however, that the lamins are more dynamic than originally thought. They accumulate in nucleoplasmic foci in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5004739d34c39730eaabd4b70646b576
https://doi.org/10.1016/0955-0674(93)90004-a
https://doi.org/10.1016/0955-0674(93)90004-a
Publikováno v:
Neuron. 43(5)
The amyloid hypothesis of Alzheimer's disease (AD) maintains that the accumulation of the amyloid beta protein (Abeta) is a critical event in disease pathogenesis. A great deal of both academic and commercial research has focused on the mechanisms by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::613c3f480d971e32880fc8b9045f3e99
https://pubmed.ncbi.nlm.nih.gov/15339642
https://pubmed.ncbi.nlm.nih.gov/15339642
Autor:
C S, Atwood, X, Huang, A, Khatri, R C, Scarpa, Y S, Kim, R D, Moir, R E, Tanzi, A E, Roher, A I, Bush
Publikováno v:
Cellular and molecular biology (Noisy-le-Grand, France). 46(4)
Abeta derived from amyloid plaques of Alzheimer's disease-affected brain contain several oxidative posttranslational modifications. In this study we have characterized the amino acid content of human amyloid-derived Abeta and compared it with that of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d550349ace36f0d52c98a2c4360a5a6c
https://pubmed.ncbi.nlm.nih.gov/10875439
https://pubmed.ncbi.nlm.nih.gov/10875439
Publikováno v:
The Journal of biological chemistry. 275(34)
In the transcription of tRNA and 5 S genes by RNA polymerase III, recruitment of the transcription factor (TF)IIIB is mediated by the promoter-bound assembly factor TFIIIC. A critical limiting step in this process is the interaction between the tetra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::28648b0ebcf3a756be0ab1c11d6ed511
https://pubmed.ncbi.nlm.nih.gov/10859316
https://pubmed.ncbi.nlm.nih.gov/10859316
Autor:
X, Huang, M P, Cuajungco, C S, Atwood, M A, Hartshorn, J D, Tyndall, G R, Hanson, K C, Stokes, M, Leopold, G, Multhaup, L E, Goldstein, R C, Scarpa, A J, Saunders, J, Lim, R D, Moir, C, Glabe, E F, Bowden, C L, Masters, D P, Fairlie, R E, Tanzi, A I, Bush
Publikováno v:
The Journal of biological chemistry. 274(52)
Oxidative stress markers as well as high concentrations of copper are found in the vicinity of Abeta amyloid deposits in Alzheimer's disease. The neurotoxicity of Abeta in cell culture has been linked to H(2)O(2) generation by an unknown mechanism. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bcd56325c22eac0a588a6687831d51f9
https://pubmed.ncbi.nlm.nih.gov/10601271
https://pubmed.ncbi.nlm.nih.gov/10601271
Publikováno v:
Metal ions in biological systems. 36
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9bb84b0f25128e73d602b581e561a3a4
https://pubmed.ncbi.nlm.nih.gov/10093929
https://pubmed.ncbi.nlm.nih.gov/10093929
Autor:
Warren H. Pettingell, Dora M. Kovacs, R. D. Moir, Tae-Wan Kim, Wilma Wasco, Ronald Mancini, J. Henderson, Rudolph E. Tanzi
Publikováno v:
Presenilins and Alzheimer’s Disease ISBN: 9783642721052
Familial Alzheimer’s disease (FAD) is a genetically heterogeneous neurodegenerative disorder which can be caused by defects in at least three early-onset (< 60 yr.) genes located on chromosomes 1 (presenilin 2, PS2; Levy-Lahad et al. 1995), 14 (Pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::918309a1024736f38c47a64815f4dcfc
https://doi.org/10.1007/978-3-642-72103-8_3
https://doi.org/10.1007/978-3-642-72103-8_3