A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.

Autor: Raimund Jung, Marie C Lechler, Ana Fernandez-Villegas, Chyi Wei Chung, Harry C Jones, Yoon Hee Choi, Maximilian A Thompson, Christian Rödelsperger, Waltraud Röseler, Gabriele S Kaminski Schierle, Ralf J Sommer, Della C David

Publikováno v: PLoS Biology, Vol 21, Iss 9, p e3002284 (2023)

During aging, proteostasis capacity declines and distinct proteins become unstable and can accumulate as protein aggregates inside and outside of cells. Both in disease and during aging, proteins selectively aggregate in certain tissues and not other

Externí odkaz: https://doaj.org/article/6e413ad3f27943b5974f39bac00f3cda

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in Caenorhabditis elegans

Autor: Chaolie Huang, Sara Wagner-Valladolid, Amberley D Stephens, Raimund Jung, Chetan Poudel, Tessa Sinnige, Marie C Lechler, Nicole Schlörit, Meng Lu, Romain F Laine, Claire H Michel, Michele Vendruscolo, Clemens F Kaminski, Gabriele S Kaminski Schierle, Della C David

Publikováno v: eLife, Vol 8 (2019)

Reduced protein homeostasis leading to increased protein instability is a common molecular feature of aging, but it remains unclear whether this is a cause or consequence of the aging process. In neurodegenerative diseases and other amyloidoses, spec

Externí odkaz: https://doaj.org/article/d304ea99735c4d8ea67842213713ac7f

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans

Autor: Marie C. Lechler, Claire H. Michel, G. S. Kaminski Schierle, Chaolie Huang, Raimund Jung, Chetan Poudel, Clemens F. Kaminski, Della C. David, N. Schlörit, A.D. Stephens, Michele Vendruscolo, Romain F. Laine, Tessa Sinnige, Sara Wagner-Valladolid

Reduced protein homeostasis and increased protein instability is a common feature of aging. Yet it remains unclear whether protein instability is a cause of aging. In neurodegenerative diseases and amyloidoses, specific proteins self-assemble into am

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd3f0aaba92d0d8b1562dd9e98d11e31

Reduced Insulin/IGF-1 Signaling Restores the Dynamic Properties of Key Stress Granule Proteins during Aging

Autor: Janine Kirstein, Katja Widmaier, Jonathan C. Trinidad, Marie C. Lechler, Emily D. Crawford, Della C. David, Nicole Groh, Alma L. Burlingame, Raimund Jung

Publikováno v: Cell reports 18(2), 454-467 (2017). doi:10.1016/j.celrep.2016.12.033
Cell Reports
Cell reports, 18(2): 454–467
Cell Reports, Vol 18, Iss 2, Pp 454-467 (2017)

Summary Low-complexity “prion-like” domains in key RNA-binding proteins (RBPs) mediate the reversible assembly of RNA granules. Individual RBPs harboring these domains have been linked to specific neurodegenerative diseases. Although their aggreg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f5af5e2785ae020a809f32fa789c3e4

A safety mechanism enables tissue-specific resistance to protein aggregation during aging in C. elegans.

Autor: Jung, Raimund¹ (AUTHOR), Lechler, Marie C.^1,2 (AUTHOR), Fernandez-Villegas, Ana³ (AUTHOR), Chung, Chyi Wei³ (AUTHOR), Jones, Harry C.⁴ (AUTHOR), Choi, Yoon Hee⁴ (AUTHOR), Thompson, Maximilian A.⁴ (AUTHOR), Rödelsperger, Christian⁵ (AUTHOR), Röseler, Waltraud⁵ (AUTHOR), Kaminski Schierle, Gabriele S.³ (AUTHOR), Sommer, Ralf J.⁵ (AUTHOR), David, Della C.^1,4,6 (AUTHOR) della.david@babraham.ac.uk

Publikováno v: PLoS Biology. 9/14/2023, Vol. 21 Issue 9, p1-25. 25p. 4 Graphs.