(Q28214915)

1

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Madhavi J Rane

2

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Qingdan Chen

3

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Saurabh Singh

4

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Kenneth R McLeish

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

14 June 2002

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published in

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volume

277

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page(s)

21639-42

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issue

24

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cites work

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14-3-3 proteins; bringing new definitions to scaffolding

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

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Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

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Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1

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The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax

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Common amino acid sequence motifs in p53, 14-3-3 and Akt protein families

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Protein kinase C mu is negatively regulated by 14-3-3 signal transduction proteins

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14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: negative regulation by 14-3-3 phosphorylation

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

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14-3-3 is phosphorylated by casein kinase I on residue 233. Phosphorylation at this site in vivo regulates Raf/14-3-3 interaction

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A motif-based profile scanning approach for genome-wide prediction of signaling pathways

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p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils

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14-3-3Gamma interacts with and is phosphorylated by multiple protein kinase C isoforms in PDGF-stimulated human vascular smooth muscle cells

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Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function

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

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Differential Activation of PKC Isozymes by 14-3-3 ζ Protein

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Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C

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