Zobrazeno 1 - 10
of 49
pro vyhledávání: '"David R. Boyer"'
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
Autor:
Rebeccah A. Warmack, David R. Boyer, Chih-Te Zee, Logan S. Richards, Michael R. Sawaya, Duilio Cascio, Tamir Gonen, David S. Eisenberg, Steven G. Clarke
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
In patients with sporadic Alzheimer’s disease part of the Asp23 residues are isomerized to L-isoaspartate (L-isoAsp23). Here the authors present the MicroED structures of wild-type and L-isoAsp23 Aβ 20–34 amyloid fibrils that both form tightly p
Externí odkaz:
https://doaj.org/article/13816496598043ba832e0e479cc32bd3
Autor:
Binsen Li, Peng Ge, Kevin A. Murray, Phorum Sheth, Meng Zhang, Gayatri Nair, Michael R. Sawaya, Woo Shik Shin, David R. Boyer, Shulin Ye, David S. Eisenberg, Z. Hong Zhou, Lin Jiang
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
The intrinsically disordered protein alpha-synuclein (aSyn) forms polymorphic fibrils. Here the authors provide molecular insights into aSyn fibril polymorphism and present the cryo-EM structures of the two predominant species, a rod and a twister bo
Externí odkaz:
https://doaj.org/article/7d6d7834f70b4294ba675d175de06cd2
Autor:
Bryan D. Ryder, David R. Boyer, Elizaveta Ustyantseva, Ayde Mendoza-Oliva, Mikołaj I. Kuska, Paweł M. Wydorski, Michael Sawaya, Marc I. Diamond, David S. Eisenberg, Harm H. Kampinga, Lukasz A. Joachimiak
Publikováno v:
bioRxiv
SUMMARYJ-domain protein (JDP) molecular chaperones have emerged as central players that maintain a healthy proteome. The diverse members of the JDP family function as monomers/dimers and a small subset assemble into micron-sized oligomers. The oligom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f39ea3ae54a9c077e9e5cb89ad458eb7
https://doi.org/10.1101/2023.03.06.531355
https://doi.org/10.1101/2023.03.06.531355
Autor:
Kevin A. Murray, Jiahui Lu, David Eisenberg, Binh Nguyen, Qin Cao, David R. Boyer, Fouad Kandeel, Michael R. Sawaya, Lorena Saelices, Romany Abskharon
Publikováno v:
Nature Structural & Molecular Biology. 28:724-730
Amyloidosis of human islet amyloid polypeptide (hIAPP) is a pathological hallmark of type II diabetes (T2D), an epidemic afflicting nearly 10% of the world’s population. To visualize disease-relevant hIAPP fibrils, we extracted amyloid fibrils from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa1869e9ad95630f181a4fc7176f68f8
https://doi.org/10.1038/s41594-021-00646-x
https://doi.org/10.1038/s41594-021-00646-x
Autor:
Jeannette T. Bowler, Michael R. Sawaya, David R. Boyer, Duilio Cascio, Manya Bali, David S. Eisenberg
Publikováno v:
The Journal of biological chemistry, vol 298, iss 10
Amyloid protein aggregation is commonly associated with progressive neurodegenerative diseases, however not all amyloid fibrils are pathogenic. The neuronal cytoplasmic polyadenylation element binding protein is a regulator of synaptic mRNA translati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6a2c28d737dbc00e9fce6c95e3e8ce1
https://escholarship.org/uc/item/4fh6t5c9
https://escholarship.org/uc/item/4fh6t5c9
Autor:
Romany Abskharon, Michael R. Sawaya, David R. Boyer, Qin Cao, Binh A. Nguyen, Duilio Cascio, David S. Eisenberg
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 119, iss 15
In neurodegenerative diseases including Alzheimer’s and ALS, proteins that bind RNA are found in aggregated forms in autopsied brains. Evidence suggests that RNA aids nucleation of these pathological aggregates; however, the mechanism has not been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29450e31814314df6d24ebe0bd8a1103
https://doi.org/10.1073/pnas.2119952119
https://doi.org/10.1073/pnas.2119952119
Publikováno v:
Nature structural & molecular biology
Nature structural & molecular biology, vol 27, iss 7
Nature structural & molecular biology, vol 27, iss 7
Human islet amyloid polypeptide (hIAPP, or amylin) is a 37 amino acid hormone secreted by pancreatic islet β-cells. Aggregation of hIAPP into amyloid fibrils is found in more than 90% of Type-II Diabetes (T2D) patients and is considered to be associ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ccb17f7b42eada27b73a2c8fbe1da68
http://europepmc.org/articles/PMC8579859
http://europepmc.org/articles/PMC8579859