Results 91 to 100 of about 554,867 (317)
Exploring downstream pathways of aberrantly activated kinases for targeted leukemia therapy [PDF]
, 2008 Genetic alterations resulting in uncontrolled protein tyrosine kinases (PTKs) activity are frequently found in leukemia and in human solid cancers. Although the development of small molecule kinase inhibitors has revolutionized therapy for PTKinduced ...
Gasser, Christelle
core +1 more source
Phosphoinositides and inositol phosphates as molecular glues
FEBS Letters, EarlyView.Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry +9 more
wiley +1 more source
BMC Genomics, 2009 Background Protein kinases are involved in diverse spectrum of cellular processes. Availability of draft version of the human genomic data in the year 2001 enabled recognition of repertoire of protein kinases.
Anamika Krishanpal +2 more
doaj +1 more source
FEBS Letters, EarlyView.Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley +1 more source
Novel approaches to targeting protein tyrosine kinases
, 2015 Protein kinases, a diverse group of cellular enzymes, play fundamental roles in maintaining normal cellular functions such as growth, cell cycle control, proliferation, differentiation, migration, cellular survival and apoptotic induction.
McCullough, D., Trim, C.
core
Parasite, 2000 Little is known about signalling in Toxoplasma gondii, but it is likely that protein kinases might play a key role in the parasite proliferation, differentiation and probably invasion.
Robert-Gangneux F. +3 more
doaj +1 more source
FEBS Letters, EarlyView.CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens +8 more
wiley +1 more source
FEBS Letters, EarlyView.Protein aggregates threaten proteostasis and cell health. In human cells, Hsp70–J‐domain protein‐based disaggregases remove aggregates, but how they assemble remains unclear. Our biochemical findings show that DNAJA2‐ and DNAJB1‐containing disaggregase scaffolds enhance luciferase aggregate targeting, and that Hsp70 recruitment by both J‐domain ...
Anna Szlachcic, Nadinath B. Nillegoda
wiley +1 more source
Reconstructing enzyme evolution by protein engineering
FEBS Letters, EarlyView.Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler +2 more
wiley +1 more source
, 2008 We define phosphovariants as genetic variations that change phosphorylation sites or their interacting kinases. Considering the essential role of phosphorylation in protein functions, it is highly likely that phosphovariants change protein functions and ...
Pamela Song +4 more
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