Trichoketides A and B, two new protein tyrosine phosphatase 1B inhibitors from ... - Nature.com
Trichoketides A and B, two new protein tyrosine phosphatase 1B inhibitors from ... - Nature.com
Trichoketides A and B, two new protein tyrosine phosphatase 1B inhibitors from ... Nature.com
The 1H and 13C NMR spectra (in acetone-d6) showed 23 proton and 16 carbon signals (Table 1) that were classified into one methyl, eight sp3 methylene, two sp3 oxygenated methine, two sp2 methine, two sp2 quaternary and one carbonyl carbons through ...
[NMR paper] Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Nature of aryl-tyrosine interactions contribute to ?-hairpin scaffold stability: NMR evidence for alternate ring geometry.
Phys Chem Chem Phys. 2015 Jan 8;
Authors: Makwana KM, Mahalakshmi R
Abstract
The specific contribution of the acidic-aromatic ?-sheet favouring amino acid tyrosine to the stability of short octapeptide ?-hairpin structures is presented here. Solution NMR analysis in near-apolar...
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[NMR paper] NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
Related Articles NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.
Proc Natl Acad Sci U S A. 2013 Nov 4;
Authors: Skora L, Mestan J, Fabbro D, Jahnke W, Grzesiek S
Abstract
Successful treatment of chronic myelogenous leukemia is based on inhibitors binding to the ATP site of the deregulated breakpoint cluster region (Bcr)-Abelson tyrosine kinase (Abl)...
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A 1H NMR metabolic profiling to the assessment of protein tyrosine phosphatase 1B role in liver regeneration after partial hepatectomy
A 1H NMR metabolic profiling to the assessment of protein tyrosine phosphatase 1B role in liver regeneration after partial hepatectomy
Available online 12 December 2012
Publication year: 2012
Source:Biochimie</br>
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Protein tyrosine phosphatase 1B (PTP1B) is a negative regulator of the tyrosine kinase growth factor signaling pathway, which is involved in major physiological mechanisms such as liver regeneration. We investigate early hepatic metabolic events produced by partial hepatectomy (PHx) for PTP1B deficient (PTP1B KO) and wild type (WT) mice using proton...
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Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH.
Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH.
Design and NMR Studies of Cyclic Peptides Targeting the N-Terminal Domain of the Protein Tyrosine Phosphatase YopH.
Chem Biol Drug Des. 2010 Nov 30;
Authors: Leone M, Barile E, Dahl R, Pellecchia M
We report on the design and evaluation of novel cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH from Yersinia. Cyclic peptides have been designed based on a short sequence from the protein SKAP-HOM...
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[NMR paper] NMR assignments of a low molecular weight protein tyrosine phosphatase (PTPase) from
NMR assignments of a low molecular weight protein tyrosine phosphatase (PTPase) from Bacillus subtilis.
Related Articles NMR assignments of a low molecular weight protein tyrosine phosphatase (PTPase) from Bacillus subtilis.
J Biomol NMR. 2005 Apr;31(4):363
Authors: Xu H, Zhang P, Jin C
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[NMR paper] Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monom
Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding.
Related Articles Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding.
J Mol Biol. 2002 Sep 6;322(1):137-52
Authors: Akerud T, Thulin E, Van Etten RL, Akke M
Low molecular weight protein tyrosine phosphatase (LMW-PTP) dimerizes in the phosphate-bound...
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[NMR paper] Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosp
Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
Related Articles Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.
J Mol Biol. 2001 Dec 7;314(4):839-49
Authors: Ohki S, Eto M, Kariya E, Hayano T, Hayashi Y, Yazawa M, Brautigan D, Kainosho M
Contractility of vascular smooth muscle depends on phosphorylation of myosin light chains, and...
Trichoketides A and B, two new protein tyrosine phosphatase 1B inhibitors from ... - Nature.com
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