Zobrazeno 1 - 10
of 36
pro vyhledávání: '"David S Eisenberg"'
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
Autor:
Pascal Krotee, Jose A Rodriguez, Michael R Sawaya, Duilio Cascio, Francis E Reyes, Dan Shi, Johan Hattne, Brent L Nannenga, Marie E Oskarsson, Stephan Philipp, Sarah Griner, Lin Jiang, Charles G Glabe, Gunilla T Westermark, Tamir Gonen, David S Eisenberg
Publikováno v:
eLife, Vol 6 (2017)
hIAPP fibrils are associated with Type-II Diabetes, but the link of hIAPP structure to islet cell death remains elusive. Here we observe that hIAPP fibrils are cytotoxic to cultured pancreatic β-cells, leading us to determine the structure and cytot
Externí odkaz:
https://doaj.org/article/f0207c5ac18e49debe0019586fe78051
Autor:
Boris Brumshtein, Shannon R Esswein, Lukasz Salwinski, Martin L Phillips, Alan T Ly, Duilio Cascio, Michael R Sawaya, David S Eisenberg
Publikováno v:
eLife, Vol 4 (2015)
Overproduction of immunoglobulin light chains leads to systemic amyloidosis, a lethal disease characterized by the formation of amyloid fibrils in patients' tissues. Excess light chains are in equilibrium between dimers and less stable monomers which
Externí odkaz:
https://doaj.org/article/13c7f8e63ae14a8ebae1d9de36a40291
Autor:
Binh An Nguyen, Virender Singh, Shumaila Afrin, Anna Yakubovska, Lanie Wang, Yasmin Ahmed, Rose Pedretti, Maria del Carmen Fernandez-Ramirez, Preeti Singh, Maja Pękała, Luis O. Cabrera Hernandez, Siddharth Kumar, Andrew Lemoff, Roman Gonzalez-Prieto, Michael R. Sawaya, David S. Eisenberg, Merrill Douglas Benson, Lorena Saelices
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract ATTR amyloidosis is caused by the deposition of transthyretin in the form of amyloid fibrils in virtually every organ of the body, including the heart. This systemic deposition leads to a phenotypic variability that has not been molecularly
Externí odkaz:
https://doaj.org/article/60a20b40007f4acdaf11442427648360
Autor:
Lin Jiang, Cong Liu, David Leibly, Meytal Landau, Minglei Zhao, Michael P Hughes, David S Eisenberg
Publikováno v:
eLife, Vol 2 (2013)
Amyloid protein aggregates are associated with dozens of devastating diseases including Alzheimer’s, Parkinson’s, ALS, and diabetes type 2. While structure-based discovery of compounds has been effective in combating numerous infectious and metab
Externí odkaz:
https://doaj.org/article/5a7cefc5de85489599727b82100f59f6
Autor:
Lin Jiang, Cong Liu, David Leibly, Meytal Landau, Minglei Zhao, Michael P Hughes, David S Eisenberg
Publikováno v:
eLife, Vol 2 (2013)
Externí odkaz:
https://doaj.org/article/83afdb2944cb4eb99ff9570ef34f0691
Autor:
Einav Tayeb-Fligelman, Jeannette T. Bowler, Christen E. Tai, Michael R. Sawaya, Yi Xiao Jiang, Gustavo Garcia, Sarah L. Griner, Xinyi Cheng, Lukasz Salwinski, Liisa Lutter, Paul M. Seidler, Jiahui Lu, Gregory M. Rosenberg, Ke Hou, Romany Abskharon, Hope Pan, Chih-Te Zee, David R. Boyer, Yan Li, Daniel H. Anderson, Kevin A. Murray, Genesis Falcon, Duilio Cascio, Lorena Saelices, Robert Damoiseaux, Vaithilingaraja Arumugaswami, Feng Guo, David S. Eisenberg
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-18 (2023)
Abstract The self-assembly of the Nucleocapsid protein (NCAP) of SARS-CoV-2 is crucial for its function. Computational analysis of the amino acid sequence of NCAP reveals low-complexity domains (LCDs) akin to LCDs in other proteins known to self-asse
Externí odkaz:
https://doaj.org/article/afcfb5ca25ff4981a1a88a2f530c23e4
Autor:
Paul M. Seidler, Kevin A. Murray, David R. Boyer, Peng Ge, Michael R. Sawaya, Carolyn J. Hu, Xinyi Cheng, Romany Abskharon, Hope Pan, Michael A. DeTure, Christopher K. Williams, Dennis W. Dickson, Harry V. Vinters, David S. Eisenberg
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Evidence suggests that fibrous aggregates of protein tau may be the proximal cause of Alzheimer’s disease. Here, using atomic structures of tau fibrils from brains of people with Alzheimer’s disease, the authors have found small-molecule drug lea
Externí odkaz:
https://doaj.org/article/a6336cf0b0264ed0a047acb9ca2994cf
Autor:
Jiahui Lu, Qin Cao, Michael P. Hughes, Michael R. Sawaya, David R. Boyer, Duilio Cascio, David S. Eisenberg
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
hnRNPA2 is involved in RNA metabolism and can form both functional amyloid-like fibrils in membraneless organelles, and pathogenic fibrils in neurodegenerative conditions. Here, the authors present the cryo-EM fibril structure of the wild-type hnRNPA
Externí odkaz:
https://doaj.org/article/ebd048782b074d139ebdf2478999499b