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. The...
[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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[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] Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy.
J Biomol NMR. 2016 Feb 2;
Authors: Tang W, Bhatt A, Smith AN, Crowley PJ, Brady LJ, Long JR
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium...
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02-04-2016 11:46 AM
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Specific binding of a naturally occurring amyloidogenic fragment of Streptococcus mutans adhesin P1 to intact P1 on the cell surface characterized by solid state NMR spectroscopy
Abstract
The P1 adhesin (aka Antigen I/II or PAc) of the cariogenic bacterium Streptococcus mutans is a cell surface-localized protein involved in sucrose-independent adhesion and colonization of the tooth surface. The immunoreactive and adhesive properties of S. mutans suggest an unusual functional quaternary ultrastructure comprised of intact P1 covalently attached to the...
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02-02-2016 08:58 PM
[NMR paper] Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Related Articles Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.
Biomol NMR Assign. 2014 Feb 4;
Authors: Jean NL, Bougault C, Derouaux A, Callens G, Vollmer W, Simorre JP
Abstract
The peptidoglycan is a major component of the bacterial cell wall and is essential to maintain cellular integrity and cell shape. Penicillin-Binding Proteins (PBPs) catalyze the final...
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02-05-2014 06:08 PM
[NMR paper] Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Related Articles Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.
Biomol NMR Assign. 2013 Dec 24;
Authors: Peterson TA, Yu L, Piper RC
Abstract
Vps28 is one of four cytosolic proteins comprising the endosomal sorting complex required for transport I (ESCRT-I). ESCRT-I is involved in sorting ubiquitinated proteins to multivesicular bodies as well as in mediating budding of retroviruses. Here, we report the backbone...
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12-25-2013 03:39 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] 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...
Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1
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