Mutations in the Basic Region of the Mason-Pfizer Monkey Virus Nucleocapsid Protein Affect Reverse Transcription ... - Journal of Virology
Mutations in the Basic Region of the Mason-Pfizer Monkey Virus Nucleocapsid Protein Affect Reverse Transcription ... - Journal of Virology
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Mutations in the Basic Region of the Mason-Pfizer Monkey Virus Nucleocapsid Protein Affect Reverse Transcription ...
Journal of Virology
Importantly, in addition to gRNA incorporation, this basic region (KNKEK) at the N terminus of the nucleocapsid protein is crucial for the onset of reverse transcription. Mutations that change the positive charge of the region to a negative one ...
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04-28-2018 03:16 PM
The Vaccinia Virus H3 Envelope Protein, a Major Target of Neutralizing Antibodies, Exhibits a Glycosyltransferase ... - Journal of Virology
The Vaccinia Virus H3 Envelope Protein, a Major Target of Neutralizing Antibodies, Exhibits a Glycosyltransferase ... - Journal of Virology
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The Vaccinia Virus H3 Envelope Protein, a Major Target of Neutralizing Antibodies, Exhibits a Glycosyltransferase ...
Journal of Virology
Like glycosyltransferases, H3 binds UDP-glucose, as shown by saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy, and this binding requires Mg2+. Mutation of the glycosyltransferase-like metal ion binding motif in H3 ...
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04-30-2016 09:26 AM
pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine ... - Journal of Virology
pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine ... - Journal of Virology
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pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine ...
Journal of Virology
Remarkably, nuclear magnetic resonance (NMR) analyses revealed the same α-helical structures for pUL69 sequences encoding either the wild type R1/R2 boxes or a UAP56/PRMT6 binding-deficient derivative, thereby excluding the possibility that R/A ...
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08-20-2015 05:44 AM
Determinants of Dengue Virus NS4A Protein Oligomerization - Journal of Virology
Determinants of Dengue Virus NS4A Protein Oligomerization - Journal of Virology
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Determinants of Dengue Virus NS4A Protein Oligomerization
Journal of Virology
Nuclear magnetic resonance (NMR) analysis of NS4A amino acids 17 to 80 suggests that residues L31, L52, E53, G66, and G67 could participate in oligomerization. Ala substitution for 15 flavivirus conserved NS4A residues revealed that these amino acids ...
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05-16-2015 01:45 PM
[NMR paper] NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein.
NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein.
Related Articles NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein.
Viruses. 2015;7(5):2210-2229
Authors: Brown LA, Cox C, Baptiste J, Summers H, Button R, Bahlow K, Spurrier V, Kyser J, Luttge BG, Kuo L, Freed EO, Summers MF
Abstract
Membrane targeting by the Gag proteins of the human immunodeficiency viruses (HIV types-1 and -2) is mediated by Gag's N-terminally myristylated matrix (MA) domain and is dependent on...
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05-06-2015 11:59 AM
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus - Journal of Virology
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus - Journal of Virology
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Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus
Journal of Virology
Using nuclear magnetic resonance (NMR), we found that the isolated cytoplasmic loop of NS4B is flexible, with a tendency to form a three-turn α-helix and two short β-strands. Upon binding to the NS3 helicase, 12 amino acids within the cytoplasmic loop ...
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03-14-2015 06:49 AM
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus - Journal of Virology
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus - Journal of Virology
<img alt="" height="1" width="1">
Mapping the Interactions between the NS4B and NS3 Proteins of Dengue Virus
Journal of Virology
Using nuclear magnetic resonance (NMR), we found that the isolated cytoplasmic loop of NS4B is flexible, with a tendency to form a three-turn α-helix and two short β-strands. Upon binding to the NS3 helicase, 12 amino acids within the cytoplasmic loop ...
Read here
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03-10-2015 07:22 PM
NMR Studies of the Q5A, G6S Unmyristylated Feline Immunodeficiency Virus Matrix Protein
NMR Studies of the Q5A, G6S Unmyristylated Feline Immunodeficiency Virus Matrix Protein
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Vaughn R. Spurrier , Lola Brown , Michael Summers</br>
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