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Zhefeng Guo

Showing results (21-30 of 41) with videos related to

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Protein Science : a Publication of the Protein Society|December 22, 2007
Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 lysozymeZhefeng Guo, Duilio Cascio, Kálmán Hideg, et al.
Royal Society Open Science|May 7, 2021
Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2Emilie N Liu, Giovanna Park, Junsuke Nohara, et al.
Royal Society Open Science|August 16, 2018
Site-specific structural order in Alzheimer's Aβ42 fibrilsHongsu Wang, Yoon Kyung Lee, Christine Xue, et al.
FEBS Letters|December 17, 2016
Cross-seeding between Aβ40 and Aβ42 in Alzheimer's diseaseJoyce Tran, Dennis Chang, Frederick Hsu, et al.
The Analyst|May 2, 2023
A protein aggregation platform that distinguishes oligomers from amyloid fibrilsAmy Zhang, Diana Portugal Barron, Erica W Chen, et al.
Biochemical and Biophysical Research Communications|April 23, 2022
Static and dynamic disorder in Aβ40 fibrilsHui Xiao, Lan Duo, James Zhen, et al.
Plos One|October 19, 2012
Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR studySam Ngo, Vicky Chiang, Elaine Ho, et al.
Protein Science : a Publication of the Protein Society|May 3, 2007
Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozymeZhefeng Guo, Duilio Cascio, Kálmán Hideg, et al.
Royal Society Open Science|September 8, 2017
A mix-and-click method to measure amyloid-β concentration with sub-micromolar sensitivityChristine Xue, Yoon Kyung Lee, Joyce Tran, et al.
Royal Society Open Science|August 17, 2019
Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphismChristine Xue, Joyce Tran, Hongsu Wang, et al.
Pageof 5

Showing results (21-30 of 41) with videos related to

Sort By:
Pageof 5
Protein Science : a Publication of the Protein Society|December 22, 2007
Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 lysozymeZhefeng Guo, Duilio Cascio, Kálmán Hideg, et al.
Royal Society Open Science|May 7, 2021
Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2Emilie N Liu, Giovanna Park, Junsuke Nohara, et al.
Royal Society Open Science|August 16, 2018
Site-specific structural order in Alzheimer's Aβ42 fibrilsHongsu Wang, Yoon Kyung Lee, Christine Xue, et al.
FEBS Letters|December 17, 2016
Cross-seeding between Aβ40 and Aβ42 in Alzheimer's diseaseJoyce Tran, Dennis Chang, Frederick Hsu, et al.
The Analyst|May 2, 2023
A protein aggregation platform that distinguishes oligomers from amyloid fibrilsAmy Zhang, Diana Portugal Barron, Erica W Chen, et al.
Biochemical and Biophysical Research Communications|April 23, 2022
Static and dynamic disorder in Aβ40 fibrilsHui Xiao, Lan Duo, James Zhen, et al.
Plos One|October 19, 2012
Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR studySam Ngo, Vicky Chiang, Elaine Ho, et al.
Protein Science : a Publication of the Protein Society|May 3, 2007
Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozymeZhefeng Guo, Duilio Cascio, Kálmán Hideg, et al.
Royal Society Open Science|September 8, 2017
A mix-and-click method to measure amyloid-β concentration with sub-micromolar sensitivityChristine Xue, Yoon Kyung Lee, Joyce Tran, et al.
Royal Society Open Science|August 17, 2019
Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphismChristine Xue, Joyce Tran, Hongsu Wang, et al.
Pageof 5