[ASAP] Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region
[ASAP] Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region
[NMR paper] Proline-Rich Region II (PRR2) Plays an Important Role in Tau-Glycan Interaction: An NMR Study
Proline-Rich Region II (PRR2) Plays an Important Role in Tau-Glycan Interaction: An NMR Study
(1) Background: Prion-like transcellular spreading of tau pathology in Alzheimer's disease (AD) is mediated by tau binding to the cell-surface glycan heparan sulfate (HS). However, the structural determinants for tau-HS interaction are not well understood. (2) Methods and Results: Binding-site mapping using NMR showed two major binding regions in full-length tau responsible for heparin interaction. Thus, two tau constructs, tau PRR2* and tau R2*, were designed to investigate the molecular...
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11-11-2022 09:45 PM
[NMR paper] Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.
Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.
Related Articles Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.
Methods Mol Biol. 2020;2141:793-817
Authors: Julien M, Bouguechtouli C, Alik A, Ghouil R, Zinn-Justin S, Theillet FX
Abstract
In line with their high accessibility, disordered proteins are exquisite targets of kinases. Eukaryotic organisms use the so-called intrinsically disordered proteins (IDPs) or intrinsically disordered regions of proteins (IDRs) as molecular switches...
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07-23-2020 11:23 PM
[NMR paper] Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Related Articles Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Biomol NMR Assign. 2020 Apr 20;:
Authors: Schulte T, Sala BM, Nilvebrant J, Nygren PÅ, Achour A, Shernyukov A, Agback T, Agback P
Abstract
The pneumococcal serine rich repeat protein (PsrP) is...
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04-22-2020 10:11 PM
[ASAP] Evaluation of Maltose Binding Protein-Tagged hATR Kinase Domain Catalytic Activity with p53 Ser-15 Phosphorylation
Evaluation of Maltose Binding Protein-Tagged hATR Kinase Domain Catalytic Activity with p53 Ser-15 Phosphorylation
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00845/20181112/images/medium/bi-2018-00845m_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00845
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11-25-2018 06:02 AM
[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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http://feeds.feedburner.com/~r/acs/bichaw/~4/0YhCYVxyXp8
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06-27-2018 01:51 AM
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00618/20170823/images/medium/bi-2017-006182_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00618
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08-24-2017 08:38 AM
[NMR paper] Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Sci Rep. 2013;3:2913
Authors: Ogura K, Okamura H
Abstract
Growth factor receptor-bound protein 2 (Grb2) is a small adapter protein composed of a single SH2 domain flanked by two SH3 domains. The...
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10-10-2013 09:38 PM
[NMR paper] Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) pept
Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.biochemj.org-images-bj_pubmed.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Multiple cis-trans conformers of the prolactin receptor proline-rich motif (PRM) peptide detected by reverse-phase HPLC, CD and NMR spectroscopy.
Biochem J. 1996 May 1;315 ( Pt 3):833-44
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[ASAP] Conformation and Affinity Modulations by Multiple Phosphorylation Occurring in the BIN1 SH3 Domain Binding Site of the Tau Protein Proline-Rich Region
Linear Mode
