1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1
Author:
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/content/pdf/10.1007/s12104-008-9142-4.pdf
Reference12 articles.
1. Delaglio F, Grzesiek S et al (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293. doi: 10.1007/BF00197809
2. Eghbalnia HR, Bahrami A et al (2005) Probabilistic identification of spin systems and their assignments including coil-helix interference as output (PISTACHIO). J Biomol NMR 32:219–233. doi: 10.1007/s10858-005-7944-6
3. Goddard TD, Kneller DG (2004) SPARKY 3. University of California, San Francisco
4. Jeong DG, Kim SJ et al (2005) Trimeric structure of the PRL-1 phosphatase reveals an active enzyme conformation and regulation mechanisms. J Mol Biol 345:401–413. doi: 10.1016/j.jmb.2004.10.061
5. Kozlov G, Cheng J et al (2002) Letter to the Editor: 1H, 13C and 15N resonance assignments of the human phosphatase PRL-3. J Biomol NMR 24:169–170. doi: 10.1023/A:1020937316065
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