Page 180 - Haematologica June
P. 180

K. Kurakula et al.
Biophys Acta. 2013;1833(3):613-621.
14. Sen M, Herzik M, Craft JW, et al. Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region. Open
Spectrosc J. 2009;3:58-64.
15. Dorfleutner A, Ruf W. Regulation of tissue
factor cytoplasmic domain phosphoryla- tion by palmitoylation. Blood. 2003; 102(12):3998-4005.
16. Rothmeier AS, Liu E, Chakrabarty S, et al. Identification of the integrin-binding site on coagulation factor VIIa required for proangiogenic PAR2 signaling. Blood. 2018; 131(6):674-685.
17. Ranganathan R, Lu KP, Hunter T, Noel JP. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell. 1997;89(6):875-886.
18. Joseph JD, Yeh ES, Swenson KI, Means AR. The peptidyl-prolyl isomerase Pin1. Prog Cell Cycle Res. 2003;5:477-487.
19. Wulf G, Finn G, Suizu F, Lu KP. Phosphorylation-specific prolyl isomeriza- tion: is there an underlying theme? Nat Cell Biol. 2005;7(5):435-441.
20. Lu KP, Zhou XZ. The prolyl isomerase PIN1: a pivotal new twist in phosphoryla- tion signalling and disease. Nat Rev Mol Cell Biol. 2007;8(11):904-916.
21. Fujimoto Y, Shiraki T, Horiuchi Y, et al. Proline cis/trans-isomerase Pin1 regulates peroxisome proliferator-activated receptor gamma activity through the direct binding to the activation function-1 domain. J Biol Chem. 2010;285(5):3126-3132.
22. van Tiel CM, Kurakula K, Koenis DS, van der Wal E, de Vries CJ. Dual function of Pin1 in NR4A nuclear receptor activation:
enhanced activity of NR4As and increased domains. Nat Struct Biol. 2000;7(8):639- Nur77 protein stability. Biochim Biophys 643.
Acta. 2012;1823(10):1894-1904. 31. Ettelaie C, Collier MEW, Featherby S,
23. Melis E, Moons L, De Mol M, et al. Greenman J, Maraveyas A. Peptidyl-prolyl Targeted deletion of the cytosolic domain isomerase 1 (Pin1) preserves the phospho- of tissue factor in mice does not affect rylation state of tissue factor and prolongs development. Biochem Biophys Res its release within microvesicles. Biochim Commun. 2001;286(3):580-586. Biophys Acta. 2018;1865(1):12-24.
24. Oeth P, Parry GC, Mackman N. Regulation 32. Wintjens R, Wieruszeski JM, Drobecq H, et of the tissue factor gene in human mono- al. 1H NMR study on the binding of Pin1 cytic cells. Role of AP-1, NF-kappa B/Rel, Trp-Trp domain with phosphothreonine and Sp1 proteins in uninduced and peptides. J Biol Chem. 2001;276(27):25150- lipopolysaccharide-induced expression. 25156.
Arterioscler Thromb Vasc Biol. 1997;17(2): 33. Helander S, Montecchio M, Pilstål R, et al.
365-374. Pre-Anchoring of Pin1 to 25. Johnson BA. Using NMRView to visualize Unphosphorylated c-Myc in a Fuzzy and analyze the NMR spectra of macro- Complex Regulates c-Myc Activity.
molecules. Methods Mol Biol. 2004; Structure. 2015;23(12):2267-2279.
278:313-352. 34. Macias MJ, Gervais V, Civera C, Oschkinat 26. Delaglio F, Grzesiek S, Vuister GW, Zhu G, H. Structural analysis of WW-domains and Pfeifer J, Bax A. NMRPipe: a multidimen- design of a WW prototype. Nat Struct Biol.
sional spectral processing system based on 2000;7(5):375-379.
UNIX pipes. J Biomol NMR. 1995;6(3):277- 35. Nechama M, Lin CL, Richter JD. An unusu- 293. al two-step control of CPEB destruction by
27. van den Hengel LG, Osanto S, Reitsma PH, Pin1. Mol Cell Biol. 2013;33(1):48-58. Versteeg HH. Murine tissue factor coagu- 36. Schelhorn C, Martin-Malpartida P, Sunol lant activity is critically dependent on the D, Macias MJ. Structural Analysis of the presence of an intact allosteric disulfide. Pin1-CPEB1 interaction and its potential Haematologica. 2013;98(1):153-158. role in CPEB1 degradation. Sci Rep.
28. Hennig L, Christner C, Kipping M, et al. 2015;5:14990.
Selective inactivation of parvulin-like pep- 37. Innes BT, Bailey ML, Brandl CJ, Shilton BH, tidyl-prolyl cis/trans isomerases by juglone. Litchfield DW. Non-catalytic participation Biochemistry. 1998;37(17):5953-5960. of the Pin1 peptidyl-prolyl isomerase
29. Zhou XZ, Kops O, Werner A, et al. Pin1- domain in target binding. Front Physiol. dependent prolyl isomerization regulates 2013;4:18.
dephosphorylation of Cdc25C and tau pro- 38. Liou YC, Ryo A, Huang HK, et al. Loss of teins. Mol Cell. 2000;6(4):873-883. Pin1 function in the mouse causes pheno-
30. Verdecia MA, Bowman ME, Lu KP, Hunter types resembling cyclin D1-null pheno- T, Noel JP. Structural basis for phosphoser- types. Proc Natl Acad Sci USA. 2002; ine-proline recognition by group IV WW- 99(3):1335-1340.
1082
haematologica | 2018; 103(6)


































































































   178   179   180   181   182