Results 31 to 40 of about 265,404 (307)

Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases

open access: yes, 2009
Background: The c-Cbl-associated protein (CAP), also known as ponsin, localizes to focal adhesions and stress fibers and is involved in signaling events.
Tomasovic, Ana   +11 more
core   +1 more source

Large‐scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis

open access: yesMolecular Systems Biology, 2008
Protein phosphorylation regulates a wide range of cellular processes. Here, we report the proteome‐wide mapping of in vivo phosphorylation sites in Arabidopsis by using complementary phosphopeptide enrichment techniques coupled with high‐accuracy mass ...
Naoyuki Sugiyama   +6 more
doaj   +1 more source

Differential maturation and chaperone dependence of the paralogous protein kinases DYRK1A and DYRK1B

open access: yesScientific Reports, 2022
The HSP90/CDC37 chaperone system not only assists the maturation of many protein kinases but also maintains their structural integrity after folding.
Marco Papenfuss   +6 more
doaj   +1 more source

Receptor-specific regulation of phosphatidylinositol 3'-kinase activation by the protein tyrosine phosphatase Shp2

open access: yes, 2002
Receptor tyrosine kinases (RTKs) play distinct roles in multiple biological systems. Many RTKs transmit similar signals, raising questions about how specificity is achieved.
Zhang, S.   +13 more
core   +1 more source

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

open access: yesFEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho   +3 more
wiley   +1 more source

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

Recent Advances in Discovery of New Tyrosine Kinase Inhibitors Using Computational Methods

open access: yesProceedings, 2019
Tyrosine–protein kinases catalyze chemical reactions that. [...]
Vesna Rastija
doaj   +1 more source

Neuroblastoma tyrosine kinase signaling networks involve FYN and LYN in endosomes and lipid rafts. [PDF]

open access: yesPLoS Computational Biology, 2015
Protein phosphorylation plays a central role in creating a highly dynamic network of interacting proteins that reads and responds to signals from growth factors in the cellular microenvironment.
Juan Palacios-Moreno   +7 more
doaj   +1 more source

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains [PDF]

open access: yes, 2007
Background The genomes of the three parasitic protozoa Trypanosoma cruzi, Trypanosoma brucei and Leishmania major are the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping
Szoor, Balazs; id_orcid   +26 more
core   +1 more source

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

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