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Ian S. Millett
Researcher at Stanford University
Publications - 31
Citations - 4662
Ian S. Millett is an academic researcher from Stanford University. The author has contributed to research in topics: Protein folding & Folding (chemistry). The author has an hindex of 26, co-authored 31 publications receiving 4376 citations. Previous affiliations of Ian S. Millett include California Polytechnic State University & University of California, Santa Cruz.
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Journal ArticleDOI
Random-coil behavior and the dimensions of chemically unfolded proteins
Jonathan E. Kohn,Ian S. Millett,Jaby Jacob,Jaby Jacob,Bojan Zagrovic,Thomas M. Dillon,Nikolina Cingel,Robin S. Dothager,Soenke Seifert,Pappannan Thiyagarajan,Tobin R. Sosnick,M. Zahid Hasan,Vijay S. Pande,Ingo Ruczinski,Sebastian Doniach,Kevin W. Plaxco +15 more
TL;DR: It appears that the mean dimensions of the large majority of chemically denatured proteins are effectively indistinguishable from themean dimensions of a random-coil ensemble.
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Biophysical Properties of the Synucleins and Their Propensities to Fibrillate INHIBITION OF α-SYNUCLEIN ASSEMBLY BY β- AND γ-SYNUCLEINS
Vladimir N. Uversky,Vladimir N. Uversky,Jie Li,Pierre O. Souillac,Ian S. Millett,Sebastian Doniach,Ross Jakes,Michel Goedert,Anthony L. Fink +8 more
TL;DR: In this paper, the authors showed that β-synuclein fibrillation was inhibited by β-and γ-Synuclein, which exhibited the properties of a random coil, whereas α- and γ -synucleins were slightly more compact and structured.
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Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates.
Ritu Khurana,Joel R. Gillespie,Anupam Talapatra,Lauren J. Minert,Cristian Ionescu-Zanetti,Ian S. Millett,Anthony L. Fink +6 more
TL;DR: The data support the hypothesis that amyloid fibril formation involves the ordered self-assembly of partially folded species that are critical soluble precursors of fibrils.
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Nuclear Localization of α-Synuclein and Its Interaction with Histones†
John Goers,Amy B. Manning-Boğ,Alison L. McCormack,Ian S. Millett,Sebastian Doniach,Donato A. Di Monte,Vladimir N. Uversky,Anthony L. Fink +7 more
TL;DR: The aggregation of α-synuclein is believed to play an important role in the pathogenesis of Parkinson's disease as well as other neurodegenerative disorders (“ synucleinopathies”).
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Exploring the folding landscape of a structured RNA.
Rick Russell,Xiaowei Zhuang,Hazen P. Babcock,Ian S. Millett,Sebastian Doniach,Steven Chu,Daniel Herschlag +6 more
TL;DR: In this paper, the folding landscape of the Tetrahymena ribozyme is investigated by using a powerful approach: the folding of single ribo-zyme molecules is followed beginning from distinct regions of the fold landscape, and it is shown that the landscape contains discrete folding pathways.