Parvovirus B19 (B19V) is a human pathogen that is the causative agent of several diseases in infants and adults. Due to a lack of antivirals against this virus, treatment options are limited. The minor capsid protein of B19V has a unique N terminus, named VP1u, which is essential for infection. The VP1u encodes a receptor binding domain (RBD), necessary for host cell entry, and a phospholipase A2 (PLA(2)) domain, crucial for endosomal escape during cellular trafficking. Both domains are...
[NMR paper] --Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19
--Backbone NMR resonance assignments for the VP1u N-terminal receptor-binding domain of the human parvovirus pathogen B19
Parvovirus B19 (B19V) is a human pathogen that is the causative agent of several diseases in infants and adults. Due to a lack of antivirals against this virus, treatment options are limited. The minor capsid protein of B19V has a unique N terminus, named VP1u, which is essential for infection. The VP1u encodes a receptor binding domain (RBD), necessary for host cell entry, and a phospholipase A2 (PLA (2) ) domain, crucial for endosomal escape during cellular...
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06-17-2024 05:10 PM
[NMR paper] Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1
Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1
Adhesin P1 (aka AgI/II) plays a pivotal role in mediating Streptococcus mutans attachment in the oral cavity, as well as in regulating biofilm development and maturation. P1's naturally occurring truncation product, Antigen II (AgII), adopts both soluble, monomeric and insoluble, amyloidogenic forms within the bacterial life cycle. Monomers are involved in important quaternary interactions that promote cell adhesion and the functional amyloid form promotes detachment of mature biofilms....
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10-22-2023 11:46 AM
[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant
Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the misfolding and aggregation of the human prion protein (huPrP). Despite efforts into investigating the process of huPrP aggregation, the mechanisms triggering its misfolding remain elusive. A number of TSE-associated mutations of huPrP have been identified, but their role at the onset and progression of prion diseases is unclear. Here we report the NMR assignments of...
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02-24-2021 05:50 AM
[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
Biomol NMR Assign. 2021 Feb 15;:
Authors: Sanz-Hernández M, De Simone A
Abstract
Transmissible spongiform encephalopathies (TSEs) are fatal...
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02-18-2021 03:17 PM
[NMR paper] NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 3 in apo state and in complex with inhibitor PD173074.
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 3 in apo state and in complex with inhibitor PD173074.
Related Articles NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 3 in apo state and in complex with inhibitor PD173074.
Biomol NMR Assign. 2018 Mar 26;:
Authors: Sanfelice D, Koss H, Bunney TD, Thompson GS, Farrell B, Katan M, Breeze AL
Abstract
Fibroblast growth factors receptors (FGFR) are transmembrane protein tyrosine kinases...
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03-28-2018 02:16 PM
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.
Biomol NMR Assign. 2013 May 18;
Authors: Fonner BA, Tripet BP, Lui M, Zhu H, Lei B, Copié V
Abstract
Staphylococcus aureus is an opportunistic pathogen that...
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05-21-2013 02:34 PM
[NMR paper] NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
Biomol NMR Assign. 2013 Jan 17;
Authors: Vajpai N, Schott AK, Vogtherr M, Breeze AL
Abstract
Members of the fibroblast growth factor receptor tyrosine kinase family (FGFR1-4) play an important role in many...
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02-03-2013 10:19 AM
[NMR paper] Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in fold
Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
Related Articles Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.
J Biomol NMR. 1994 Nov;4(6):845-58
Authors: Zhang O, Kay LE, Olivier JP, Forman-Kay JD
The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter...