[NMR paper] Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Altered Domain Structure of the Prion Protein Caused by Cu2+ Binding and Functionally Relevant Mutations: Analysis by Cross-Linking, MS/MS, and NMR.
Structure. 2019 Mar 28;:
Authors: McDonald AJ, Leon DR, Markham KA, Wu B, Heckendorf CF, Schilling K, Showalter HD,...
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04-09-2019 11:33 PM
[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00552
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07-06-2018 09:40 AM
[ASAP] Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
Alanine Scanning of YbdZ, an MbtH-like Protein, Reveals Essential Residues for Functional Interactions with Its Nonribosomal Peptide Synthetase Partner EntF
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00552/20180703/images/medium/bi-2018-005525_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00552
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07-06-2018 09:40 AM
[NMR paper] NMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
NMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
Related Articles NMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
Sci Rep. 2018 Apr 03;8(1):5490
Authors: Chatterjee D, Zhiping LL, Tan SM, Bhattacharjya S
Abstract
Integrins are transmembrane proteins that mediate cell adhesion and migration. Each integrin is a heterodimer formed by an ? and a ? subunit. A large number of cytoplasmic proteins interact with the...
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04-05-2018 01:42 PM
[NMR paper] Reversible DNA-protein cross-linking at epigenetic DNA marks
Reversible DNA-protein cross-linking at epigenetic DNA marks
5-Formylcytosine (5fC) is an endogenous DNA modification frequently found within regulatory elements of mammalian genes. Although 5fC is an oxidation product of 5-methylcytosine (5mC), the two epigenetic marks show distinct genome-wide distributions and protein affinities, suggesting that they perform different functions in epigenetic signaling. A unique feature of 5fC is the presence of a potentially reactive aldehyde group in its structure. Here, we show that 5fC bases in DNA readily form Schiff base conjugates with Lys side...
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09-12-2017 01:45 PM
G Protein-Coupled Receptors Directly Bind FilaminA with High Affinity and Promote Filamin Phosphorylation
G Protein-Coupled Receptors Directly Bind FilaminA with High Affinity and Promote Filamin Phosphorylation
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00975/20151020/images/medium/bi-2015-00975p_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00975
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11-09-2015 05:03 PM
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Langerin–HeparinInteraction: Two Binding Sitesfor Small and Large Ligands As Revealed by a Combination of NMR Spectroscopyand Cross-Linking Mapping Experiments
Juan C. Mun?oz-Garci?a, Eric Chabrol, Romain R. Vive?s, Aline Thomas, Jose? L. de Paz, Javier Rojo, Anne Imberty, Franck Fieschi, Pedro M. Nieto and Jesu?s Angulo
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja511529x/20150319/images/medium/ja-2014-11529x_0009.gif
Journal of the American Chemical Society
DOI: 10.1021/ja511529x...
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03-23-2015 08:22 PM
[NMR paper] Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
Related Articles Langerin-Heparin Interaction: Two Binding Sites for Small and Large Ligands as revealed by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments.
J Am Chem Soc. 2015 Mar 6;
Authors: Muñoz-García JC, Chabrol E, Vives RR, Thomas A, de Paz JL, Rojo J, Imberty A, Fieschi F, Nieto PM, Angulo J
Abstract
Langerin is a C-type lectin present...
![[ASAP] Identification of Filamin A Mechanobinding Partner II: Fimbacin Is a Novel Actin Cross-Linking and Filamin A Binding Protein](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-identification-filamin-mechanobinding-partner-ii-fimbacin-novel-actin-cross-linking-filamin-binding-protein_ltr.gif)
[ASAP] Identification of Filamin A Mechanobinding Partner II: Fimbacin Is a Novel Actin Cross-Linking and Filamin A Binding Protein
Linear Mode
