Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.

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Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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Amyloid fibrils embodying dist ...... exhibit diverse morphologies.

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Amyloid fibrils embodying dist ...... exhibit diverse morphologies.

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Amyloid fibrils embodying dist ...... exhibit diverse morphologies.

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Amyloid fibrils embodying dist ...... exhibit diverse morphologies.

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Amyloid fibrils embodying dist ...... exhibit diverse morphologies.

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Amyloid fibrils embodying dist ...... exhibit diverse morphologies.

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P1476

Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies

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P2093

Jijun Dong

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Joe Wall

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Rupam Ghosh

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P2860

Prion Protein Biology

Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

A yeast prion provides a mechanism for genetic variation and phenotypic diversity

Prions as adaptive conduits of memory and inheritance

Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus

Optical trapping with high forces reveals unexpected behaviors of prion fibrils.

Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.

Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.

Intrinsic linear heterogeneity of amyloid β protein fibrils revealed by higher resolution mass-per-length determinations.

P31

scholarly article

P356

10.1093/FEMSYR/FOY059

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P433

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P478

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Kendra K Frederick

P577

2018-09-01T00:00:00Z

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P698

29846554

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P932

6001884

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