Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Melissa D. Michelitsch"'
Autor:
Anthony L. Lau, Gulliver Timoteo, David Peretz, Alice Yam, Xuemei Wang, David Y. Chien, Angelica Medina-Selby, Doris Coit, Colin S. McCoin, Ping Wu, Robert J. Goodson, Melissa D. Michelitsch, Celine Hu, Bruce Phelps, Robert M. Shimizu, John L. Hall, Carol Man Gao
Publikováno v:
Proceedings of the National Academy of Sciences. 104:11551-11556
On our initial discovery that prion protein (PrP)-derived peptides were capable of capturing the pathogenic prion protein (PrP Sc ), we have been interested in how these peptides interact with PrP Sc . After screening peptides from the entire human P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a16e564690a4d0cbb4537319cbe5bb3f
https://doi.org/10.1073/pnas.0704260104
https://doi.org/10.1073/pnas.0704260104
Publikováno v:
Proceedings of the National Academy of Sciences. 95:12163-12168
The chaperonin GroEL is an oligomeric double ring structure that, together with the cochaperonin GroES, assists protein folding. Biochemical analyses indicate that folding occurs in a cis ternary complex in which substrate is sequestered within the G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::619353148528d817125a820875a68aa8
https://doi.org/10.1073/pnas.95.21.12163
https://doi.org/10.1073/pnas.95.21.12163
Autor:
Vincent Guénebaut, David A. Agard, Frederick Cohen, Stanley B. Prusiner, Ana Serban, Holger Wille, Surachai Supattapone, Melissa D. Michelitsch
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 99(6)
Because the insolubility of the scrapie prion protein (PrP Sc ) has frustrated structural studies by x-ray crystallography or NMR spectroscopy, we used electron crystallography to characterize the structure of two infectious variants of the prion pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5167c5de66053b820da803e586e851a
https://pubmed.ncbi.nlm.nih.gov/11891310
https://pubmed.ncbi.nlm.nih.gov/11891310
Glutamine/asparagine (Q/N)-rich domains have a high propensity to form self-propagating amyloid fibrils. This phenomenon underlies both prion-based inheritance in yeast and aggregation of a number of proteins involved in human neurodegenerative disea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fad0fa13511c0a28ca0842ea59c12560
https://europepmc.org/articles/PMC17268/
https://europepmc.org/articles/PMC17268/
