Results 41 to 50 of about 3,692,701 (303)
Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain. [PDF]
Scaffold proteins have an important role in the regulation of signal propagation. These proteins do not possess any enzymatic activity but can contribute to the formation of multiprotein complexes.
Roopesh Udupa +16 more
core +1 more source
Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
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
Degeneration of cortical and spinal motor neurons is the typical feature of amyotrophic lateral sclerosis (ALS), a progressive neurodegenerative disease for which a pathogenetic role for the Cu/Zn superoxide dismutase (SOD1) has been demonstrated.
Cinzia Mallozzi +3 more
doaj +1 more source
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley +1 more source
Tyrosine Kinase Inhibitors as Antiangiogenic Drugs in Multiple Myeloma
Tyrosine kinase inhibitors are a new class of anticancer drugs, that are capable of directly interacting with the catalytic site of the target enzyme and thereby inhibiting catalysis. Therapeutically useful tyrosine kinase inhibitors are not specific for
Domenico Ribatti
doaj +1 more source
Characterization of the function of a novel protein tyrosine phophatase predicted by the genome sequence of Arabidopsis thaliana [PDF]
Covalent modification of proteins by reversible phosphorylation, catalysed by specific protein kinases and phosphatases, is an important mechanism for enzyme activity regulation in metabolism and signalling pathways.
Reignoux, Sabrina Natacha Aurore
core
Exploring downstream pathways of aberrantly activated kinases for targeted leukemia therapy [PDF]
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
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
Domain Architecture of the Nonreceptor Tyrosine Kinase Ack1
The nonreceptor tyrosine kinase (NRTK) Ack1 comprises a distinct arrangement of non-catalytic modules. Its SH3 domain has a C-terminal to the kinase domain (SH1), in contrast to the typical SH3-SH2-SH1 layout in NRTKs.
Yagmur Kan +3 more
doaj +1 more source
The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains [PDF]
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

