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Results: 1 to 20 of 108

Similar articles for PubMed (Select 16091624)

1.

14-3-3 proteins: a number of functions for a numbered protein.

Bridges D, Moorhead GB.

Sci STKE. 2005 Aug 9;2005(296):re10. Review.

PMID:
16091624
2.

14-3-3 proteins: a number of functions for a numbered protein.

Bridges D, Moorhead GB.

Sci STKE. 2004 Jul 13;2004(242):re10. Review.

PMID:
15266103
3.

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine.

Muslin AJ, Tanner JW, Allen PM, Shaw AS.

Cell. 1996 Mar 22;84(6):889-97.

4.

Can we infer peptide recognition specificity mediated by SH3 domains?

Cesareni G, Panni S, Nardelli G, Castagnoli L.

FEBS Lett. 2002 Feb 20;513(1):38-44.

PMID:
11911878
5.

Does isoform diversity explain functional differences in the 14-3-3 protein family?

Kjarland E, Keen TJ, Kleppe R.

Curr Pharm Biotechnol. 2006 Jun;7(3):217-23. Review.

PMID:
16789906
6.

Function of WW domains as phosphoserine- or phosphothreonine-binding modules.

Lu PJ, Zhou XZ, Shen M, Lu KP.

Science. 1999 Feb 26;283(5406):1325-8.

7.
8.

PhosphoSerine/threonine binding domains: you can't pSERious?

Yaffe MB, Smerdon SJ.

Structure. 2001 Mar 7;9(3):R33-8. Review.

PMID:
11286893
9.

Structure and sites of phosphorylation of 14-3-3 protein: role in coordinating signal transduction pathways.

Dubois T, Howell S, Amess B, Kerai P, Learmonth M, Madrazo J, Chaudhri M, Rittinger K, Scarabel M, Soneji Y, Aitken A.

J Protein Chem. 1997 Jul;16(5):513-22.

PMID:
9246637
10.

Equivalent binding sites reveal convergently evolved interaction motifs.

Henschel A, Kim WK, Schroeder M.

Bioinformatics. 2006 Mar 1;22(5):550-5. Epub 2005 Nov 15.

11.

The diversity of ubiquitin recognition: hot spots and varied specificity.

Winget JM, Mayor T.

Mol Cell. 2010 Jun 11;38(5):627-35. doi: 10.1016/j.molcel.2010.05.003. Review.

12.

FHA domains as phospho-threonine binding modules in cell signaling.

Hammet A, Pike BL, McNees CJ, Conlan LA, Tenis N, Heierhorst J.

IUBMB Life. 2003 Jan;55(1):23-7. Review.

PMID:
12716058
13.

The Giardia duodenalis 14-3-3 protein is post-translationally modified by phosphorylation and polyglycylation of the C-terminal tail.

Lalle M, Salzano AM, Crescenzi M, Pozio E.

J Biol Chem. 2006 Feb 24;281(8):5137-48. Epub 2005 Dec 20.

14.

Phosphoserine/threonine-binding domains.

Yaffe MB, Elia AE.

Curr Opin Cell Biol. 2001 Apr;13(2):131-8. Review.

PMID:
11248545
15.

The structural basis for 14-3-3:phosphopeptide binding specificity.

Yaffe MB, Rittinger K, Volinia S, Caron PR, Aitken A, Leffers H, Gamblin SJ, Smerdon SJ, Cantley LC.

Cell. 1997 Dec 26;91(7):961-71.

17.

Role of 14-3-3 proteins in eukaryotic signaling and development.

Darling DL, Yingling J, Wynshaw-Boris A.

Curr Top Dev Biol. 2005;68:281-315. Review.

PMID:
16125003
18.

Delineation of exoenzyme S residues that mediate the interaction with 14-3-3 and its biological activity.

Yasmin L, Jansson AL, Panahandeh T, Palmer RH, Francis MS, Hallberg B.

FEBS J. 2006 Feb;273(3):638-46.

PMID:
16420486
19.

Affinity methods for phosphorylation-dependent interactions.

Moorhead G, MacKintosh C.

Methods Mol Biol. 2004;261:469-78. Review.

PMID:
15064476
20.

The many faces of SAM.

Qiao F, Bowie JU.

Sci STKE. 2005 May 31;2005(286):re7. Review.

PMID:
15928333
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