Zobrazeno 1 - 10
of 37
pro vyhledávání: '"David S. Eisenberg"'
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:
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:
Vasantha Basavalingappa, Santu Bera, Bin Xue, Ido Azuri, Yiming Tang, Kai Tao, Linda J. W. Shimon, Michael R. Sawaya, Sofiya Kolusheva, David S. Eisenberg, Leeor Kronik, Yi Cao, Guanghong Wei, Ehud Gazit
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
DNA is an attractive nanomaterial, yet limited compared to polyamides due to low stability and mechanical issues. Here, the authors combine polyamide and DNA characteristics to form mechanically rigid self-assembled peptide nucleic acid based materia
Externí odkaz:
https://doaj.org/article/fe1796cb54ed4a099a3b5e137059ad29
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
Publikováno v:
Neurobiology of Disease, Vol 120, Iss , Pp 118-125 (2018)
Transthyretin amyloidosis (ATTR) is a fatal disease caused by the systemic aggregation and deposition of transthyretin (TTR), a blood transporter that is mainly produced in the liver. TTR deposits are made of elongated amyloid fibrils that interfere
Externí odkaz:
https://doaj.org/article/10aeca6256464b0295afeedb6260400e
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:
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