Results 71 to 80 of about 1,166,192 (319)

Phosphorylation by Akt within the ST loop of AMPK-α1 down-regulates its activation in tumour cells [PDF]

open access: yes, 2014
The insulin/IGF-1 (insulin-like growth factor 1)-activated protein kinase Akt (also known as protein kinase B) phosphorylates Ser487 in the ‘ST loop’ (serine/threonine-rich loop) within the C-terminal domain of AMPK-a1 (AMP-activated protein kinase-a1 ...
Leslie, Nicholas R.   +6 more
core   +1 more source

Phosphorylation-linked complex profiling identifies assemblies required for Hippo signal integration. [PDF]

open access: yes, 2023
While several computational methods have been developed to predict the functional relevance of phosphorylation sites, experimental analysis of the interdependency between protein phosphorylation and Protein-Protein Interactions (PPIs) remains challenging.
Martin Mehnert (15146901)   +13 more
core   +1 more source

PROTAC-mediated conditional degradation of the WRN helicase as a potential strategy for selective killing of cancer cells with microsatellite instability

open access: yesScientific Reports
Multiple studies have demonstrated that cancer cells with microsatellite instability (MSI) are intolerant to loss of the Werner syndrome helicase (WRN), whereas microsatellite-stable (MSS) cancer cells are not.
Vikram Tejwani   +7 more
doaj   +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

βTrCP-mediated proteolysis of NF-kB1 p105 requires phosphorylation of p105 serines 927 and 932 [PDF]

open access: yes, 2003
This work was supported by the U.K. Medical Research Council, the Arthritis Research Campaign (project grant L0536 to V.L.), and the AINP consortium, EC—5th framework.NF-κB1 p105 functions both as a precursor of NF-κB1 p50 and as a cytoplasmic inhibitor ...
Ben-Neriah, Yinon   +9 more
core   +1 more source

Localization-Dependent and -Independent Roles of SLX4 in Regulating Telomeres

open access: yesCell Reports, 2013
SLX4, a scaffold for structure-specific DNA repair nucleases, is important for several types of DNA repair. Many repair proteins bind to sites of DNA damage, resulting in subnuclear “foci,” but SLX4 forms foci in human cells even without DNA damage ...
Jamie S.J. Wilson   +5 more
doaj   +1 more source

On the Control of TCR Phosphorylation [PDF]

open access: yesFrontiers in Immunology, 2012
The T-cell receptor (TCR) is responsible first of all for recognizing small peptides embedded in major histocompatibility complex molecules (pMHC). The information that a complex has thus formed is then transduced across the membrane via “triggering” of the TCR.
Fernandes, R   +4 more
openaire   +3 more sources

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
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

Genome-wide analysis to predict protein sequence variations that change phosphorylation sites or their corresponding kinases [PDF]

open access: yes, 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
core   +1 more source

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

open access: yesFEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

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