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Said A. Goueli

Researcher at Promega

Publications -  71
Citations -  1647

Said A. Goueli is an academic researcher from Promega. The author has contributed to research in topics: Kinase & Phosphorylation. The author has an hindex of 17, co-authored 62 publications receiving 1425 citations. Previous affiliations of Said A. Goueli include University of Wisconsin-Madison.

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Protein Kinase A-anchoring Inhibitor Peptides Arrest Mammalian Sperm Motility

TL;DR: Surprisingly, inhibition of PKA catalytic activity had little effect on basal motility or motility stimulated by agents previously thought to work via PKA activation, and disruption of this interaction using cell-permeable anchoring inhibitor peptides may form the basis of a sperm-targeted contraceptive.
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Sustained Activation of the Extracellular Signal-regulated Kinase/Mitogen-activated Protein Kinase Pathway Is Required for Megakaryocytic Differentiation of K562 Cells *

TL;DR: Experiments with conditioned media suggested that sustained activation of the ERK/MAP kinase pathway promoted the autocrine secretion of megakaryocytic lineage determination factors.
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ADP-Glo: A Bioluminescent and Homogeneous ADP Monitoring Assay for Kinases

TL;DR: ADP-Glo is a novel bioluminescent, homogeneous assay for monitoring ADP producing biochemical reactions and thus it is an ideal assay for detecting enzyme activity using a wide variety of substrates and is applicable to not only primary and secondary screening but also kinase profiling.
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Selective in vivo inhibition of mitogen-activated protein kinase activation using cell-permeable peptides.

TL;DR: Cell-permeable peptides developed based on a MEK1-derived peptide inhibited ERK-mediated activation of the transcriptional activity of ELK1 and did not have an inhibitory effect on the activity of two closely related classes of MAPKs, c-Jun amino-terminal kinase or p38 protein kinase.
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A tyrosine-phosphorylated 55-kilodalton motility-associated bovine sperm protein is regulated by cyclic adenosine 3',5'-monophosphates and calcium.

TL;DR: The identification of a soluble protein whose tyrosine phosphorylation varies directly with motility and suggest that motility regulation may involve cross talk between PKA, calcium, and tyrosinesine kinase pathways is suggested.