Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Slawomir P. Wojcik"'
Autor:
Sunil Kumar, Melissa Birol, Diana E. Schlamadinger, Slawomir P. Wojcik, Elizabeth Rhoades, Andrew D. Miranker
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Intrinsically disordered proteins that form amyloid fibrils are hard to target with traditional therapeutic approaches. Here, the authors report on an oligoquinoline derivative that binds the human islet amyloid polypeptide, stabilising an alpha-heli
Externí odkaz:
https://doaj.org/article/665697c8a506443f9f23cfe44a5d3983
Publikováno v:
PLoS Biology, Vol 17, Iss 6, p e3000318 (2019)
PLoS Biology
PLoS Biology
Cell-to-cell transmission of toxic forms of α-Synuclein (αS) is thought to underlie disease progression in Parkinson disease. αS in humans is constitutively N-terminally acetylated (αSacetyl), although the impact of this modification is relativel
Intrinsically disordered proteins (IDPs) and regions (IDRs) make up a significant part of the proteome and facilitate a wide range of physiological and pathological functions that are only beginning to be understood. As such, they are highly attracti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2e1e12abaeaef97605abf927bfbc5919
https://doi.org/10.1016/bs.mie.2018.09.036
https://doi.org/10.1016/bs.mie.2018.09.036
Publikováno v:
Biophysical Journal. 116:495a
Fibrillar deposits of α-Synuclein (αS) are the hallmark of Parkinson9s disease. Recent evidence suggests that disease may propagate through cell-to-cell transmission of toxic forms of αS. Rele-vant to this mechanism, here we report the discovery t
Autor:
Diana E. Schlamadinger, Melissa Birol, Sunil Kumar, Andrew D. Miranker, Elizabeth Rhoades, Slawomir P. Wojcik
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Disordered proteins, such as those central to Alzheimer's and Parkinson's, are particularly intractable for structure-targeted therapeutic design. Here we demonstrate the capacity of a synthetic foldamer to capture structure in a disease relevant pep