K
K. Hun Mok
Researcher at Trinity College, Dublin
Publications - 25
Citations - 2289
K. Hun Mok is an academic researcher from Trinity College, Dublin. The author has contributed to research in topics: CIDNP & Protein structure. The author has an hindex of 15, co-authored 25 publications receiving 2109 citations. Previous affiliations of K. Hun Mok include Lund University & University College Dublin.
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Journal ArticleDOI
Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
Seth L. Masters,Aisling Dunne,Shoba L. Subramanian,Rebecca L. Hull,Gillian M. Tannahill,Fiona A. Sharp,Christine Becker,Luigi Franchi,Eiji Yoshihara,Zhe Chen,Niamh Mullooly,Lisa A. Mielke,James Harris,Rebecca C. Coll,Kingston H. G. Mills,K. Hun Mok,Philip Newsholme,Gabriel Núñez,Junji Yodoi,Steven E. Kahn,Ed C. Lavelle,Luke A. J. O'Neill +21 more
TL;DR: It is shown that oligomers of islet amyloid polypeptide (IAPP), a protein that formsAmyloid deposits in the pancreas during type 2 diabetes, triggered the NLRP3 inflammasome and generated mature IL-1β.
Journal ArticleDOI
Local structural elements in the mostly unstructured transcriptional activation domain of human p53.
Hyun Lee,K. Hun Mok,Ranjith Muhandiram,Kyu Hwan Park,Jae Eun Suk,Do Hyung Kim,Jun Chang,Young Chul Sung,Kwan Yong Choi,Kyou-Hoon Han +9 more
TL;DR: It is revealed that an unbound full-length p53 transactivation domain, although similar to the recently discovered group of loosely folded proteins in that it does not have tertiary structure, is nevertheless populated by an amphipathic helix and two nascent turns, suggesting that such local structures are general features of acidic transactivation domains and may represent “specificity determinants” that are important for transcriptional activity.
Journal ArticleDOI
A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein
K. Hun Mok,K. Hun Mok,Lars T. Kuhn,Martin Goez,Iain J. Day,Iain J. Day,Jasper C. Lin,Niels H. Andersen,P. J. Hore +8 more
TL;DR: It is found that there is residual structure due to hydrophobic collapse in the unfolded state of this small protein, and prior structuring, even with the formation of non-native rather than native contacts, may be a feature associated with fast folding events in proteins.
Journal ArticleDOI
Rapid Sample-Mixing Technique for Transient NMR and Photo-CIDNP Spectroscopy: Applications to Real-Time Protein Folding
K. Hun Mok,Toshio Nagashima,Iain J. Day,Jonathan A. Jones,Charles J. V. Jones,Christopher M. Dobson,P. J. Hore +6 more
TL;DR: The development and application of a novel rapid sample-mixing technique for real-time NMR (nuclear magnetic resonance) spectroscopy, which provides evidence for the remarkable persistence of nativelike elements of structure under conditions in which the protein is partially denatured and aggregation prone is described.
Journal ArticleDOI
HAMLET, protein folding, and tumor cell death.
TL;DR: This review summarizes the current state of knowledge in this area based on the presentations made at the First International HAMLET Symposium in 2006.