Zobrazeno 1 - 10
of 235
pro vyhledávání: '"Hue-Sun Chan"'
Autor:
Zeyu Shen, Bowen Jia, Yang Xu, Jonas Wessén, Tanmoy Pal, Hue Sun Chan, Shengwang Du, Mingjie Zhang
Publikováno v:
eLife, Vol 12 (2023)
Formation of membraneless organelles or biological condensates via phase separation and related processes hugely expands the cellular organelle repertoire. Biological condensates are dense and viscoelastic soft matters instead of canonical dilute sol
Externí odkaz:
https://doaj.org/article/d17640f6818249c999c7232c2ea5218c
Autor:
Veronika Csizmok, Stephen Orlicky, Jing Cheng, Jianhui Song, Alaji Bah, Neda Delgoshaie, Hong Lin, Tanja Mittag, Frank Sicheri, Hue Sun Chan, Mike Tyers, Julie D. Forman-Kay
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereb
Externí odkaz:
https://doaj.org/article/3ceb544c2e084e38929cafb11be01401
Publikováno v:
Biophysical Journal. 121:157-171
The assembly of functional biomolecular condensates often involves liquid-liquid phase separation (LLPS) of proteins with multiple modular domains, which can be folded or conformationally disordered to various degrees. To understand the LLPS-driving
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd1c708ead98ad83865c05f3cc59b039
https://doi.org/10.1016/j.bpj.2021.10.008
https://doi.org/10.1016/j.bpj.2021.10.008
Publikováno v:
The journal of physical chemistry. B. 126(45)
A theory for sequence dependent liquid-liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) in the study of biomolecular condensates is formulated by extending the random phase approximation (RPA) and field-theoretic simulation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1eabe4e536be676b05c26f82782f0ad
https://pubmed.ncbi.nlm.nih.gov/36343363
https://pubmed.ncbi.nlm.nih.gov/36343363
Autor:
Yi-Hsuan Lin, Tae Hun Kim, Suman Das, Tanmoy Pal, Jonas Wessen, Lewis E. Kay, Julie D. Forman-Kay, Hue Sun Chan
Publikováno v:
Biophysical Journal. 122:158a-159a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::46dd04ca8a7a33e310e88da7b358cf67
https://doi.org/10.1016/j.bpj.2022.11.965
https://doi.org/10.1016/j.bpj.2022.11.965
Publikováno v:
PLoS Computational Biology, Vol 13, Iss 12, p e1005909 (2017)
Biomolecular recognition entails attractive forces for the functional native states and discrimination against potential nonnative interactions that favor alternate stable configurations. The challenge posed by the competition of nonnative stabilizat
Externí odkaz:
https://doaj.org/article/f66797b325b2422e98c89c32b6db7892
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2563
Biomolecular condensates, physically underpinned to a significant extent by liquid-liquid phase separation (LLPS), are now widely recognized by numerous experimental studies to be of fundamental biological, biomedical, and biophysical importance. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::51a2b3730086292b753adb5bccd3a2e1
https://pubmed.ncbi.nlm.nih.gov/36227468
https://pubmed.ncbi.nlm.nih.gov/36227468
Autor:
Zeyu Shen, Bowen Jia, Yang Xu, Jonas Wessén, Tanmoy Pal, Hue Sun Chan, Shengwang Du, Mingjie Zhang
Formation of membraneless organelles or biological condensates via phase separation hugely expands cellular organelle repertoire. Biological condensates are dense and viscoelastic soft matters instead of canonical dilute solutions. Unlike discoveries
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9b5c8f7589a9951e939d4ce43ee63d86
https://doi.org/10.1101/2022.07.20.500769
https://doi.org/10.1101/2022.07.20.500769
Publikováno v:
Methods in Molecular Biology ISBN: 9781071626627
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6c8c5383f058097f8604baae0b14b8ab
https://doi.org/10.1007/978-1-0716-2663-4_3
https://doi.org/10.1007/978-1-0716-2663-4_3
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 6, p e1004960 (2016)
Deciphering the effects of nonsynonymous mutations on protein structure is central to many areas of biomedical research and is of fundamental importance to the study of molecular evolution. Much of the investigation of protein evolution has focused o
Externí odkaz:
https://doaj.org/article/516fa2438732494c8291dc77f36e2836