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Ujjayini Ghosh

Showing results (1-10 of 16) with videos related to

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Biochimica Et Biophysica Acta. Biomembranes|June 26, 2020
<sup>2</sup>H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pHUjjayini Ghosh, David P Weliky
Biochemistry|August 26, 2021
Rapid <sup>2</sup>H NMR Transverse Relaxation of Perdeuterated Lipid Acyl Chains of Membrane with Bound Viral Fusion Peptide Supports Large-Amplitude Motions of These Chains That Can Catalyze Membrane FusionUjjayini Ghosh, David P Weliky
Chemical Communications (Cambridge, England)|May 1, 2018
Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissueUjjayini Ghosh, Wai-Ming Yau, Robert Tycko
Journal of Biomolecular NMR|January 19, 2013
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMRUjjayini Ghosh, Li Xie, David P Weliky
Proceedings of the National Academy of Sciences of the United States of America|November 2, 2021
Structural differences in amyloid-β fibrils from brains of nondemented elderly individuals and Alzheimer's disease patientsUjjayini Ghosh, Wai-Ming Yau, John Collinge, et al.
Journal of Biomolecular NMR|December 11, 2012
Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMRLi Xie, Ujjayini Ghosh, Scott D Schmick, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 12, 2021
Molecular structure of a prevalent amyloid-β fibril polymorph from Alzheimer's disease brain tissueUjjayini Ghosh, Kent R Thurber, Wai-Ming Yau, et al.
Nature Communications|November 13, 2020
Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUSMyungwoon Lee, Ujjayini Ghosh, Kent R Thurber, et al.
Journal of the American Chemical Society|June 4, 2015
Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion CatalysisUjjayini Ghosh, Li Xie, Lihui Jia, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 2, 2024
Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infectionYijin Zhang, Scott D Schmick, Li Xie, et al.
Pageof 2

Showing results (1-10 of 16) with videos related to

Sort By:
Pageof 2
Biochimica Et Biophysica Acta. Biomembranes|June 26, 2020
<sup>2</sup>H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pHUjjayini Ghosh, David P Weliky
Biochemistry|August 26, 2021
Rapid <sup>2</sup>H NMR Transverse Relaxation of Perdeuterated Lipid Acyl Chains of Membrane with Bound Viral Fusion Peptide Supports Large-Amplitude Motions of These Chains That Can Catalyze Membrane FusionUjjayini Ghosh, David P Weliky
Chemical Communications (Cambridge, England)|May 1, 2018
Coexisting order and disorder within a common 40-residue amyloid-β fibril structure in Alzheimer's disease brain tissueUjjayini Ghosh, Wai-Ming Yau, Robert Tycko
Journal of Biomolecular NMR|January 19, 2013
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMRUjjayini Ghosh, Li Xie, David P Weliky
Proceedings of the National Academy of Sciences of the United States of America|November 2, 2021
Structural differences in amyloid-β fibrils from brains of nondemented elderly individuals and Alzheimer's disease patientsUjjayini Ghosh, Wai-Ming Yau, John Collinge, et al.
Journal of Biomolecular NMR|December 11, 2012
Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMRLi Xie, Ujjayini Ghosh, Scott D Schmick, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 12, 2021
Molecular structure of a prevalent amyloid-β fibril polymorph from Alzheimer's disease brain tissueUjjayini Ghosh, Kent R Thurber, Wai-Ming Yau, et al.
Nature Communications|November 13, 2020
Molecular structure and interactions within amyloid-like fibrils formed by a low-complexity protein sequence from FUSMyungwoon Lee, Ujjayini Ghosh, Kent R Thurber, et al.
Journal of the American Chemical Society|June 4, 2015
Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion CatalysisUjjayini Ghosh, Li Xie, Lihui Jia, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 2, 2024
Very broad distribution of β sheet registries of the HIV gp41 fusion peptide supports mutational robustness for fusion and infectionYijin Zhang, Scott D Schmick, Li Xie, et al.
Pageof 2