Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Elizabeth M Meiering"'
Autor:
Ashok Sekhar, Jessica AO Rumfeldt, Helen R Broom, Colleen M Doyle, Guillaume Bouvignies, Elizabeth M Meiering, Lewis E Kay
Publikováno v:
eLife, Vol 4 (2015)
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease involving cytotoxic conformations of Cu, Zn superoxide dismutase (SOD1). A major challenge in understanding ALS disease pathology has been the identification and atomic-le
Externí odkaz:
https://doaj.org/article/3e6f47c6b96f48569f57e0bce025c0fc
Autor:
Elizabeth M Meiering
Publikováno v:
PLoS Biology, Vol 6, Iss 7, p e193 (2008)
Externí odkaz:
https://doaj.org/article/8c0b085ef55f4232aa7a8abd24429090
Publikováno v:
Frontiers in Molecular Biosciences. 10
Kinetic stability, defined as the rate of protein unfolding, is central to determining the functional lifetime of proteins, both in nature and in wide-ranging medical and biotechnological applications. Further, high kinetic stability is generally cor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::699d72a5af4850f3694f9e140baa8ac3
https://doi.org/10.3389/fmolb.2023.1021733
https://doi.org/10.3389/fmolb.2023.1021733
Autor:
Duncan W. S. MacKenzie, Anna Schaefer, Julia Steckner, Christopher A. Leo, Dalia Naser, Efrosini Artikis, Aron Broom, Travis Ko, Purnank Shah, Mikaela Q. Ney, Elisa Tran, Martin T. J. Smith, Brian Fuglestad, A. Joshua Wand, Charles L. Brooks, Elizabeth M. Meiering
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(26)
Allostery is the phenomenon of coupling between distal binding sites in a protein. Such coupling is at the crux of protein function and regulation in a myriad of scenarios, yet determining the molecular mechanisms of coupling networks in proteins rem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f10fd9ff87b67f2d00a12c2f70002d74
https://pubmed.ncbi.nlm.nih.gov/35737838
https://pubmed.ncbi.nlm.nih.gov/35737838
Autor:
Dalia Naser, Michael V. Tarasca, Bruna Siebeneichler, Anna Schaefer, Harmeen K. Deol, Tyler G. B. Soule, Johnathan Almey, Susan Kelso, Gyana G. Mishra, Hilary Simon, Elizabeth M. Meiering
Publikováno v:
Angewandte Chemie International Edition. 61
Protein aggregation is central to aging, disease and biotechnology. While there has been recent progress in defining structural features of cellular protein aggregates, many aspects remain unclear due to heterogeneity of aggregates presenting obstacl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::111fbd285e9c0ef965d593e69533f398
https://doi.org/10.1002/anie.202112645
https://doi.org/10.1002/anie.202112645
Publikováno v:
Analytical Biochemistry. 652:114675
Inclusion bodies (IBs) are large, insoluble aggregates that often form during the overexpression of proteins in bacteria. These aggregates are of broad fundamental and practical significance, for recombinant protein preparation and due to their relev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b14fccbba193d7cc2d6c395a5d498eb
https://doi.org/10.1016/j.ab.2022.114675
https://doi.org/10.1016/j.ab.2022.114675
Autor:
Harmeen K, Deol, Helen R, Broom, Bruna, Siebeneichler, Brenda, Lee, Zoya, Leonenko, Elizabeth M, Meiering
Publikováno v:
Biophysical Chemistry. 288:106844
Protein misfolding and aggregation are hallmarks of many diseases, including amyotrophic lateral sclerosis (ALS). In familial ALS, aberrant self-association of mutant Cu,Zn-superoxide dismutase (SOD1) is implicated as a key contributor to disease. Mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a11f9dbf54f6424b84e51e0ecfc5f26
https://doi.org/10.1016/j.bpc.2022.106844
https://doi.org/10.1016/j.bpc.2022.106844
Publikováno v:
Journal of Biological Chemistry. 298:102197
Aggregation of proteins is at the nexus of molecular processes crucial to aging, disease, and employing proteins for biotechnology and medical applications. There has been much recent progress in determining the structural features of protein aggrega
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::394c7906045204f23561a4c11ea1abac
https://doi.org/10.1016/j.jbc.2022.102197
https://doi.org/10.1016/j.jbc.2022.102197
Autor:
Kyle Trainor, Colleen M. Doyle, Avril Metcalfe-Roach, Julia Steckner, Daša Lipovšek, Heather Malakian, David Langley, Stanley R. Krystek Jr., Elizabeth M. Meiering
Publikováno v:
Journal of molecular biology. 434(2)
Structural heterogeneity often constrains the characterization of aggregating proteins to indirect or low-resolution methods, obscuring mechanistic details of association. Here, we report progress in understanding the aggregation of Adnectins, engine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0fd766d18d2d7f0cef915629e8ecd02
https://pubmed.ncbi.nlm.nih.gov/34902431
https://pubmed.ncbi.nlm.nih.gov/34902431
Publikováno v:
Protein Science : A Publication of the Protein Society
Isotropic chemical shifts measured by solution nuclear magnetic resonance (NMR) spectroscopy offer extensive insights into protein structure and dynamics. Temperature dependences add a valuable dimension; notably, the temperature dependences of amide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb69d8d80117a8af0e4697f3fd972e1d
https://doi.org/10.1002/pro.3785
https://doi.org/10.1002/pro.3785