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1. Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.

Authors: Benoît Odaert; Isabelle Landrieu; Klaas Dijkstra; Gea Schuurman-Wolters; Peter Casteels; Jean-Michel Wieruszeski; Dirk Inze; Ruud Scheek; Guy Lippens
Journal: J Biol Chem Date: 2002-01-25 Impact factor: 5.157

2. Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.

Authors: Y Bourne; A S Arvai; S L Bernstein; M H Watson; S I Reed; J E Endicott; M E Noble; L N Johnson; J A Tainer
Journal: Proc Natl Acad Sci U S A Date: 1995-10-24 Impact factor: 11.205

3. Letter to the editor: sequence-specific 1H, 13C and 15N chemical shift backbone NMR assignment and secondary structure of the Arabidopsis thaliana PIN1At protein.

Authors: I Landrieu; J M Wieruszeski; B Odaert; D Inzé; S Grzesiek; G Lippen
Journal: J Biomol NMR Date: 2000-07 Impact factor: 2.835

4. Correlation of the 15N(i + 1), 13Calpha(i), and 1Halpha(i) Backbone Resonances in 13C/15N-Labeled Proteins by the (CO)N(CO)CAH Experiment

Authors:
Journal: J Magn Reson Date: 1997-03 Impact factor: 2.229

5. The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.

Authors: D Patra; S X Wang; A Kumagai; W G Dunphy
Journal: J Biol Chem Date: 1999-12-24 Impact factor: 5.157

6. Crystal structure of the yeast cell-cycle control protein, p13suc1, in a strand-exchanged dimer.

Authors: N Khazanovich; K Bateman; M Chernaia; M Michalak; M James
Journal: Structure Date: 1996-03-15 Impact factor: 5.006

7. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.

Authors: D S Wishart; B D Sykes
Journal: J Biomol NMR Date: 1994-03 Impact factor: 2.835

Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe.