نتایج جستجو برای: 14 3 3

تعداد نتایج: 2034820  

Journal: :The Journal of neuroscience : the official journal of the Society for Neuroscience 2001
N Philip S F Acevedo E M Skoulakis

Members of the ubiquitous 14-3-3 family of proteins are abundantly expressed in metazoan neurons. The Drosophila 14-3-3zeta gene leonardo is preferentially expressed in adult mushroom bodies, centers of insect learning and memory. Mutants exhibit defects in olfactory learning and memory and physiological neuroplasticity at the neuromuscular junction. Because strong mutations in this gene are le...

2015
Ketaki Ganti Justyna Broniarczyk Wiem Manoubi Paola Massimi Suruchi Mittal David Pim Anita Szalmas Jayashree Thatte Miranda Thomas Vjekoslav Tomaić Lawrence Banks Joanna Parish

Cancer-causing HPV E6 oncoproteins are characterized by the presence of a PDZ binding motif (PBM) at their extreme carboxy terminus. It was long thought that this region of E6 had a sole function to confer interaction with a defined set of cellular substrates. However, more recent studies have shown that the E6 PBM has a complex pattern of regulation, whereby phosphorylation within the PBM can ...

Journal: :Biophysical journal 2012
Lenka Rezabkova Miroslava Kacirova Miroslav Sulc Petr Herman Jaroslav Vecer Miroslav Stepanek Veronika Obsilova Tomas Obsil

Phosducin (Pdc), a highly conserved phosphoprotein, plays an important role in the regulation of G protein signaling, transcriptional control, and modulation of blood pressure. Pdc is negatively regulated by phosphorylation followed by binding to the 14-3-3 protein, whose role is still unclear. To gain insight into the role of 14-3-3 in the regulation of Pdc function, we studied structural chan...

Journal: :Cell 1996
Anthony J Muslin J.William Tanner Paul M Allen Andrey S Shaw

The highly conserved and ubiquitously expressed 14-3-3 family of proteins bind to a variety of proteins involved in signal transduction and cell cycle regulation. The nature and specificity of 14-3-3 binding is, however, not known. Here we show that 14-3-3 is a specific phosphoserine-binding protein. Using a panel of phosphorylated peptides based on Raf-1, we have defined the 14-3-3 binding mot...

2015
Fábio Madeira Michele Tinti Gavuthami Murugesan Emily Berrett Margaret Stafford Rachel Toth Christian Cole Carol MacKintosh Geoffrey J. Barton

MOTIVATION The 14-3-3 family of phosphoprotein-binding proteins regulates many cellular processes by docking onto pairs of phosphorylated Ser and Thr residues in a constellation of intracellular targets. Therefore, there is a pressing need to develop new prediction methods that use an updated set of 14-3-3-binding motifs for the identification of new 14-3-3 targets and to prioritize the downstr...

Journal: :Plastic and Reconstructive Surgery - Global Open 2019

Journal: :Seminars in Cell & Developmental Biology 2011

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