[ASAP] The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
The Human Amyloid Precursor Protein Binds Copper Ions Dominated by a Picomolar-Affinity Site in the Helix-Rich E2 Domain
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00572/20180626/images/medium/bi-2018-00572h_0012.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00572
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nmrlearner
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06-27-2018 01:51 AM
Identification of a Novel Complex between the Nucleoproteinand PA(1–27) of Influenza A Virus Polymerase
Identification of a Novel Complex between the Nucleoproteinand PA(1–27) of Influenza A Virus Polymerase
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00514/20160728/images/medium/bi-2016-00514m_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00514
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nmrlearner
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07-29-2016 01:18 AM
[NMR paper] (19)F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus.
(19)F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus.
Related Articles (19)F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus.
Structure. 2014 Feb 25;
Authors: Aramini JM, Hamilton K, Ma LC, Swapna GV, Leonard PG, Ladbury JE, Krug RM, Montelione GT
Abstract
Nonstructural protein 1 of influenza A virus (NS1A) is a*conserved virulence factor comprised of an N-terminal double-stranded...
nmrlearner
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03-04-2014 06:37 PM
19F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus
19F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus
Publication date: Available online 27 February 2014
Source:Structure</br>
Author(s): James*M. Aramini , Keith Hamilton , Li-Chung Ma , G.V.T. Swapna , Paul*G. Leonard , John*E. Ladbury , Robert*M. Krug , Gaetano*T. Montelione</br>
Nonstructural protein 1 of influenza A virus (NS1A) is a*conserved virulence factor comprised of an N-terminal double-stranded RNA (dsRNA)-binding domain and a multifunctional C-terminal effector domain...
nmrlearner
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02-28-2014 06:08 AM
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane helix and an adjacent amphipathic helix, the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using two-dimensional (2D) magic-angle-spinning solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
nmrlearner
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10-07-2013 08:31 AM
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Conformational analysis of the full-length M2 protein of the influenza a virus using solid-state NMR
Abstract
The influenza A M2 protein forms a proton channel for virus infection and mediates virus assembly and budding. While extensive structural information is known about the transmembrane (TM) helix and an adjacent amphipathic helix (AH), the conformation of the N-terminal ectodomain and the C-terminal cytoplasmic tail remains largely unknown. Using 2D magic-angle-spinning (MAS) solid-state NMR, we have investigated the secondary structure and dynamics of full-length M2 (M2FL) and...
nmrlearner
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09-10-2013 08:44 PM
[NMR paper] Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)
Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Related Articles Transmembrane domain of M2 protein from influenza A virus studied by solid-state (15)N polarization inversion spin exchange at magic angle NMR.
Biophys J. 2000 Aug;79(2):767-75
Authors: Song Z, Kovacs FA, Wang J, Denny JK, Shekar SC, Quine JR, Cross TA
The M2 protein from the influenza A virus forms a proton channel in the virion that is essential for infection. This tetrameric protein...