Fu H - Search Results

1

Isolation of high-affinity peptide antagonists of 14-3-3 proteins by phage display.

Wang B, Yang H, Liu YC, Jelinek T, Zhang L, Ruoslahti E, Fu H. Wang B, et al. Among authors: fu h. Biochemistry. 1999 Sep 21;38(38):12499-504. doi: 10.1021/bi991353h. Biochemistry. 1999. PMID: 10493820

2

Interaction of 14-3-3 with a nonphosphorylated protein ligand, exoenzyme S of Pseudomonas aeruginosa.

Masters SC, Pederson KJ, Zhang L, Barbieri JT, Fu H. Masters SC, et al. Among authors: fu h. Biochemistry. 1999 Apr 20;38(16):5216-21. doi: 10.1021/bi982492m. Biochemistry. 1999. PMID: 10213629

3

Residues of 14-3-3 zeta required for activation of exoenzyme S of Pseudomonas aeruginosa.

Zhang L, Wang H, Masters SC, Wang B, Barbieri JT, Fu H. Zhang L, et al. Among authors: fu h. Biochemistry. 1999 Sep 14;38(37):12159-64. doi: 10.1021/bi991019l. Biochemistry. 1999. PMID: 10508420

4

The proapoptotic protein Bad binds the amphipathic groove of 14-3-3zeta.

Yang H, Masters SC, Wang H, Fu H. Yang H, et al. Among authors: fu h. Biochim Biophys Acta. 2001 Jun 11;1547(2):313-9. doi: 10.1016/s0167-4838(01)00202-3. Biochim Biophys Acta. 2001. PMID: 11410287

5

Raf-1 kinase and exoenzyme S interact with 14-3-3zeta through a common site involving lysine 49.

Zhang L, Wang H, Liu D, Liddington R, Fu H. Zhang L, et al. Among authors: fu h. J Biol Chem. 1997 May 23;272(21):13717-24. doi: 10.1074/jbc.272.21.13717. J Biol Chem. 1997. PMID: 9153224 Free article.

Our solution of the crystal structure of 14-3-3zeta revealed a conserved amphipathic groove that may allow the association of 14-3-3 with diverse ligands (Liu, D., Bienkowska, J., Petosa, C., Collier, R. J., Fu, H., and Liddington, R. (1995) Nature 376, 191-194). He …

Our solution of the crystal structure of 14-3-3zeta revealed a conserved amphipathic groove that may allow the association of 14-3-3 with di …

6

Mutations in the hydrophobic surface of an amphipathic groove of 14-3-3zeta disrupt its interaction with Raf-1 kinase.

Wang H, Zhang L, Liddington R, Fu H. Wang H, et al. Among authors: fu h. J Biol Chem. 1998 Jun 26;273(26):16297-304. doi: 10.1074/jbc.273.26.16297. J Biol Chem. 1998. PMID: 9632690 Free article.

Consistently, mutations on the charged surface of the groove (Lys-49, Arg-56, and Arg-60) decrease the binding of 14-3-3zeta to the ligands tested (Zhang, L., Wang, H., Liu, D., Liddington, R., and Fu, H. (1997) J. Biol. Chem. 272, 13717-13724). ...

Consistently, mutations on the charged surface of the groove (Lys-49, Arg-56, and Arg-60) decrease the binding of 14-3-3zeta to the ligands …

7

Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins.

Zhang L, Chen J, Fu H. Zhang L, et al. Among authors: fu h. Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8511-5. doi: 10.1073/pnas.96.15.8511. Proc Natl Acad Sci U S A. 1999. PMID: 10411906 Free PMC article.

8

Role of the 14-3-3 C-terminal loop in ligand interaction.

Truong AB, Masters SC, Yang H, Fu H. Truong AB, et al. Among authors: fu h. Proteins. 2002 Nov 15;49(3):321-5. doi: 10.1002/prot.10210. Proteins. 2002. PMID: 12360521

9

14-3-3zeta binds a phosphorylated Raf peptide and an unphosphorylated peptide via its conserved amphipathic groove.

Petosa C, Masters SC, Bankston LA, Pohl J, Wang B, Fu H, Liddington RC. Petosa C, et al. Among authors: fu h. J Biol Chem. 1998 Jun 26;273(26):16305-10. doi: 10.1074/jbc.273.26.16305. J Biol Chem. 1998. PMID: 9632691 Free article.

10

A novel sphingosine-dependent protein kinase (SDK1) specifically phosphorylates certain isoforms of 14-3-3 protein.

Megidish T, Cooper J, Zhang L, Fu H, Hakomori S. Megidish T, et al. Among authors: fu h. J Biol Chem. 1998 Aug 21;273(34):21834-45. doi: 10.1074/jbc.273.34.21834. J Biol Chem. 1998. PMID: 9705322 Free article.

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