Zobrazeno 1 - 10
of 447
pro vyhledávání: '"Jeffery W. Kelly"'
Autor:
Frederick L. Ruberg, William S. Blaner, Codruta Chiuzan, Lawreen H. Connors, Andrew J. Einstein, Denise Fine, Stephen Helmke, Damian Kurian, Shivda Pandey, Farbod Raiszadeh, Carlos Rodriguez, Natalia Sabogal, Sergio Teruya, Morgan Winburn, Wendy K. Chung, Elizabeth Cohn, Edward J. Miller, Jeffery W. Kelly, Mathew S. Maurer
Publikováno v:
Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, Vol 12, Iss 8 (2023)
Background Transthyretin amyloid cardiomyopathy (ATTR‐CM) is an important cause of heart failure in older individuals. Misfolding and deposition of transthyretin or prealbumin protein causes ATTR‐CM in the context of a normal (wild‐type) or var
Externí odkaz:
https://doaj.org/article/b9c1a2b8e2904079929f27ab244cfe0a
Autor:
Meng Wang, Edmund Cotter, Ya-Juan Wang, Xu Fu, Angela L. Whittsette, Joseph W. Lynch, R. Luke Wiseman, Jeffery W. Kelly, Angelo Keramidas, Ting-Wei Mu
Publikováno v:
Cell & Bioscience, Vol 12, Iss 1, Pp 1-20 (2022)
Abstract Background Genetic variants in the subunits of the gamma-aminobutyric acid type A (GABAA) receptors are implicated in the onset of multiple pathologic conditions including genetic epilepsy. Previous work showed that pathogenic GABAA subunits
Externí odkaz:
https://doaj.org/article/569f39d2a4334662858040e0811c4d49
Publikováno v:
Hemato, Vol 2, Iss 4, Pp 645-659 (2021)
Non-native immunoglobulin light chain conformations, including aggregates, appear to cause light chain amyloidosis pathology. Despite significant progress in pharmacological eradication of the neoplastic plasma cells that secrete these light chains,
Externí odkaz:
https://doaj.org/article/aea9c56e4bab45b592bded4784b3adcc
Autor:
Erik A. Blackwood, Khalid Azizi, Donna J. Thuerauf, Ryan J. Paxman, Lars Plate, Jeffery W. Kelly, R. Luke Wiseman, Christopher C. Glembotski
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
Imbalanced proteostasis is associated with diverse diseases, including ischemia/reperfusion injury in the heart. Here the authors show that the ATF6 arm of the unfolded protein response can be pharmacologically activated with a small molecule in vivo
Externí odkaz:
https://doaj.org/article/3ba71f4e4b844e449ec46f1e2075895f
Autor:
Jaleh S. Mesgarzadeh, Isabelle C. Romine, Ethan M. Smith-Cohen, Julia M. D. Grandjean, Jeffery W. Kelly, Joseph C. Genereux, R. Luke Wiseman
Publikováno v:
Cells, Vol 11, Iss 10, p 1661 (2022)
The extracellular aggregation of destabilized transthyretin (TTR) variants is implicated in the onset and pathogenesis of familial TTR-related amyloid diseases. One strategy to reduce the toxic, extracellular aggregation of TTR is to decrease the pop
Externí odkaz:
https://doaj.org/article/f3fc60b872b44c86b916574de21b8382
Autor:
Casimir Bamberger, Salvador Martínez-Bartolomé, Miranda Montgomery, Sandra Pankow, John D. Hulleman, Jeffery W. Kelly, John R. Yates
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
An accurate quantitation of different proteoforms remains challenging due to incomplete protein sequence coverage in mass spectrometry datasets. Here the authors describe a method to facilitate the discovery of proteoforms that may otherwise not be c
Externí odkaz:
https://doaj.org/article/47f96cf6a5c54801b5fbbaa897a69399
Autor:
Jeffrey N. Savas, Yi-Zhi Wang, Laura A. DeNardo, Salvador Martinez-Bartolome, Daniel B. McClatchy, Timothy J. Hark, Natalie F. Shanks, Kira A. Cozzolino, Mathieu Lavallée-Adam, Samuel N. Smukowski, Sung Kyu Park, Jeffery W. Kelly, Edward H. Koo, Terunaga Nakagawa, Eliezer Masliah, Anirvan Ghosh, John R. Yates, III
Publikováno v:
Cell Reports, Vol 21, Iss 9, Pp 2614-2627 (2017)
Amyloid beta (Aβ) peptides impair multiple cellular pathways and play a causative role in Alzheimer’s disease (AD) pathology, but how the brain proteome is remodeled by this process is unknown. To identify protein networks associated with AD-like
Externí odkaz:
https://doaj.org/article/3ed0ac7651364a66abb65df3cf5d0391
Autor:
Younhee Cho, Xin Zhang, Kristine Faye R. Pobre, Yu Liu, David L. Powers, Jeffery W. Kelly, Lila M. Gierasch, Evan T. Powers
Publikováno v:
Cell Reports, Vol 11, Iss 2, Pp 321-333 (2015)
The folding fate of a protein in vivo is determined by the interplay between a protein’s folding energy landscape and the actions of the proteostasis network, including molecular chaperones and degradation enzymes. The mechanisms of individual comp
Externí odkaz:
https://doaj.org/article/91b493a5c85e427482a2079d643a323c
Autor:
Matthew D. Shoulders, Lisa M. Ryno, Joseph C. Genereux, James J. Moresco, Patricia G. Tu, Chunlei Wu, John R. Yates, III, Andrew I. Su, Jeffery W. Kelly, R. Luke Wiseman
Publikováno v:
Cell Reports, Vol 3, Iss 4, Pp 1279-1292 (2013)
The unfolded protein response (UPR) maintains endoplasmic reticulum (ER) proteostasis through the activation of transcription factors such as XBP1s and ATF6. The functional consequences of these transcription factors for ER proteostasis remain poorly
Externí odkaz:
https://doaj.org/article/7fe6e7d4d578476c93671cd01d2aea31
Publikováno v:
Amyloid. :1-11