[NMR paper] NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
Related Articles NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
Biochemistry. 2016 May 10;
Authors: Byeon IL, Byeon CH, Wu T, Mitra M, Singer D, Levin JG, Gronenborn AM
Abstract
Human APOBEC3B (A3B) is a member of the APOBEC3 (A3) family of cytidine deaminases, which function as DNA mutators and restrict viral pathogens and endogenous...
nmrlearner
Journal club
0
05-11-2016 08:04 PM
[NMR paper] The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.
The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-7315-19-Wiley_FullText_120x30_orange.png Related Articles The casein kinase 2-dependent phosphorylation of NS5A domain 3 from hepatitis C virus followed by time-resolved NMR.
Chembiochem. 2015 Dec 18;
...
nmrlearner
Journal club
0
12-28-2015 12:26 AM
[NMR paper] Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.
J Biomol NMR. 2013 Mar 2;
Authors: Smet-Nocca C, Launay H, Wieruszeski JM, Lippens G, Landrieu I
Abstract
The Pin1 protein plays a critical role in the functional regulation of the hyperphosphorylated neuronal Tau protein in Alzheimer's disease and is by itself regulated by phosphorylation. We have...
nmrlearner
Journal club
0
03-05-2013 03:25 PM
[NMR paper] NMR backbone assignment of a protein kinase catalytic domain by a combination of seve
NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase.
Related Articles NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: application to the catalytic subunit of cAMP-dependent protein kinase.
Chembiochem. 2004 Nov 5;5(11):1508-16
Authors: Langer T, Vogtherr M, Elshorst B, Betz M, Schieborr U, Saxena K, Schwalbe H
Protein phosphorylation is one of the most important mechanisms...
nmrlearner
Journal club
0
11-24-2010 10:03 PM
[NMR paper] The energetic cost of domain reorientation in maltose-binding protein as studied by N
The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy.
Related Articles The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy.
Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12700-5
Authors: Millet O, Hudson RP, Kay LE
Maltose-binding protein (MBP) is a two-domain protein that undergoes a ligand-mediated conformational rearrangement from an "open" to a "closed" structure on binding to maltooligosaccharides. To...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spec
Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Related Articles Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Biochemistry. 1995 Nov 21;34(46):15351-8
Authors: Boerner RJ, Consler TG, Gampe RT, Weigl D, Willard DH, Davis DG, Edison AM, Loganzo F, Kassel DB, Xu RX
During solution...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Related Articles Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Biochemistry. 1991 Jun 4;30(22):5524-31
Authors: Gehring K, Williams PG, Pelton JG, Morimoto H, Wemmer DE
Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied. Tritium NMR spectroscopy...
![[ASAP] Evaluation of Maltose Binding Protein-Tagged hATR Kinase Domain Catalytic Activity with p53 Ser-15 Phosphorylation](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-evaluation-maltose-binding-protein-tagged-hatr-kinase-domain-catalytic-activity-p53-ser-15-phosphorylation_ltr.gif)
[ASAP] Evaluation of Maltose Binding Protein-Tagged hATR Kinase Domain Catalytic Activity with p53 Ser-15 Phosphorylation
Linear Mode
