Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Shruti Sahay"'
Autor:
Smriti Sangwan, Shruti Sahay, Kevin A Murray, Sophie Morgan, Elizabeth L Guenther, Lin Jiang, Christopher K Williams, Harry V Vinters, Michel Goedert, David S Eisenberg
Publikováno v:
eLife, Vol 9 (2020)
Seeding, in the context of amyloid disease, is the sequential transfer of pathogenic protein aggregates from cell-to-cell within affected tissues. The structure of pathogenic seeds provides the molecular basis and enables rapid conversion of soluble
Externí odkaz:
https://doaj.org/article/28a8e57e2eee4c3c8246bb0a5890354f
Autor:
Sarah L Griner, Paul Seidler, Jeannette Bowler, Kevin A Murray, Tianxiao Peter Yang, Shruti Sahay, Michael R Sawaya, Duilio Cascio, Jose A Rodriguez, Stephan Philipp, Justyna Sosna, Charles G Glabe, Tamir Gonen, David S Eisenberg
Publikováno v:
eLife, Vol 8 (2019)
Alzheimer’s disease (AD) pathology is characterized by plaques of amyloid beta (Aβ) and neurofibrillary tangles of tau. Aβ aggregation is thought to occur at early stages of the disease, and ultimately gives way to the formation of tau tangles wh
Externí odkaz:
https://doaj.org/article/b2be6583aeff446ab32b99c277fc5857
Publikováno v:
Acta Scientific Dental Scienecs. 6:81-87
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::caf3e55afceae2b956da2697613eda87
https://doi.org/10.31080/asds.2022.06.1325
https://doi.org/10.31080/asds.2022.06.1325
Autor:
Pradeep K Singh, Dhiman Ghosh, Debanjan Tewari, Ganesh M Mohite, Edmund Carvalho, Narendra Nath Jha, Reeba S Jacob, Shruti Sahay, Rinti Banerjee, Amal K Bera, Samir K Maji
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0120346 (2015)
Conversion of amyloid fibrils by many peptides/proteins involves cytotoxic helix-rich oligomers. However, their toxicity and biophysical studies remain largely unknown due to their highly dynamic nature. To address this, we chose two helical peptides
Externí odkaz:
https://doaj.org/article/23f758e6065b4ad68684dd502e60c701
Autor:
Shruti Sahay, Michel Goedert, Harry V. Vinters, Christopher Williams, Kevin A. Murray, E.L. Guenther, Smriti Sangwan, Lin Jiang, David Eisenberg, Sophie A. Morgan
Publikováno v:
eLife
eLife, Vol 9 (2020)
eLife, Vol 9 (2020)
Seeding, in the context of amyloid disease, is the sequential transfer of pathogenic protein aggregates from cell-to-cell within affected tissues. The structure of pathogenic seeds provides the molecular basis and enables rapid conversion of soluble
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b823e50ecf853458d29a71bce99a5236
https://escholarship.org/uc/item/7mq2t05x
https://escholarship.org/uc/item/7mq2t05x
Publikováno v:
Current Protein & Peptide Science. 18:656-676
α-Synuclein (α-Syn) aggregation is directly associated with Parkinson's disease (PD) pathogenesis. In vitro aggregation and in vivo animal model studies of α-Syn recapitulate many features of the disease pathogenesis. Six familial PD associated mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80fc0c75a23f1ed026cdaa1e28d349f2
https://doi.org/10.2174/1389203717666160314151706
https://doi.org/10.2174/1389203717666160314151706
Autor:
Sophie A. Morgan, Kevin A. Murray, Smriti Sangwan, Lin Jiang, E.L. Guenther, Shruti Sahay, Christopher Williams, Harry V. Vinters, David Eisenberg, Michel Goedert
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bdd94e55413e4c924545d3d028e0c0b8
https://doi.org/10.7554/elife.46775.sa2
https://doi.org/10.7554/elife.46775.sa2
Author response: Structure-based inhibitors of amyloid beta core suggest a common interface with tau
Autor:
Stephan Philipp, Sarah Griner, David Eisenberg, Duilio Cascio, Jose A. Rodriguez, Shruti Sahay, Kevin A. Murray, Tamir Gonen, Paul M. Seidler, Justyna Sosna, Jeannette Bowler, Charles G. Glabe, Michael R. Sawaya, Tianxiao Peter Yang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7f527b40639f1befa3978d36938b4a65
https://doi.org/10.7554/elife.46924.036
https://doi.org/10.7554/elife.46924.036
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1867(10)
α-Synuclein (α-Syn) has been extensively studied for its structural and biophysical properties owing to its pathophysiological role in Parkinson's disease (PD). Lewy bodies and Lewy neurites are the pathological hallmarks of PD and contain α-Syn a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61fb4c8d939e8f64bdab3c043e7b3591
https://pubmed.ncbi.nlm.nih.gov/30853581
https://pubmed.ncbi.nlm.nih.gov/30853581
Autor:
Narendra Nath Jha, Rakesh Kumar, Dhiman Ghosh, Samir K. Maji, Ambuja Navalkar, Ashutosh Kumar, Mrityunjoy Mondal, Rajlaxmi Panigrahi, Shruti Sahay
Publikováno v:
ACS chemical neuroscience. 8(12)
Aggregation of α-synuclein (α-Syn) into toxic oligomers and fibrils leads to Parkinson's disease (PD) pathogenesis. Molecules that can inhibit the fibrillization and oligomerization of α-Syn have potential therapeutic value. Here, we studied four
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9968f4cd620456b4f16a78c68574a40f
https://pubmed.ncbi.nlm.nih.gov/28872299
https://pubmed.ncbi.nlm.nih.gov/28872299