Results 91 to 100 of about 11,155,248 (357)

Synthesis of Isomeric Phosphoubiquitin Chains Reveals that Phosphorylation Controls Deubiquitinase Activity and Specificity

open access: yesCell Reports, 2016
Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and ...
Nicolas Huguenin-Dezot   +8 more
doaj   +1 more source

Rapid alteration of protein phosphorylation during postmortem: implication in the study of protein phosphorylation

open access: yesScientific Reports, 2015
Protein phosphorylation is an important post-translational modification of proteins. Postmortem tissues are widely being utilized in the biomedical studies, but the effects of postmortem on protein phosphorylation have not been received enough attention.
Yifan Wang   +6 more
semanticscholar   +1 more source

Functional analysis of the "Saccharomyces cerevisiae" Npr1 protein kinase [PDF]

open access: yes, 2007
The uptake and processing of nutrients is highly regulated. Cells adapt to changes of the availability of nutrients to provide a complete set of transporters and metabolizing enzymes for optimal use of the available nutrients.
Gander, Stefan
core   +1 more source

Ligand‐dependent transcriptional heterogeneity in cell cycle gene expression delays G1/S entry

open access: yesFEBS Letters, EarlyView.
EGF and HRG induce distinct G1/S progression programs in ErbB2‐amplified BT474 breast cancer cells. Despite activating the potent ErbB2–ErbB3 heterodimer, HRG does not accelerate cell‐cycle entry. Instead, EGF promotes earlier restriction‐point passage via ERK–FOS signaling, whereas HRG activates the AKT–MYC axis, driving transcriptional heterogeneity ...
Ririn Rahmala Febri   +5 more
wiley   +1 more source

FAF1 and FAF2 enhance unfolding by p97-UFD1-NPL4 complex enabling rational design of p97 activators

open access: yesThe EMBO Journal
VCP/p97 is an AAA+ ATPase that, together with its cofactors UFD1-NPL4 (p97-UN), unfolds ubiquitylated substrates to maintain cellular homeostasis. The human p97-UN complex associates with additional cofactors, but how these cofactors modulate p97-UN ...
Pritha Dasgupta   +8 more
doaj   +1 more source

Symposia on Plant (Protein) Phosphorylation [PDF]

open access: yesFrontiers in Plant Science, 2012
From September 14-16, 2011 the twelfth symposium on Plant Protein Phosphorylation was held in Tübingen, Germany. The topic is as broad as the name suggests and covers all aspects of this important means of protein modification in plants. I have had the pleasure of attending the 2007 and the 2011 symposia.
openaire   +4 more sources

Inhibition of forskolin-induced neurite outgrowth and protein phosphorylation by a newly synthesized selective inhibitor of cyclic AMP-dependent protein kinase, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H-89), of PC12D pheochromocytoma cells.

open access: yesJournal of Biological Chemistry, 1990
A newly synthesized isoquinolinesulfonamide, H-89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinoline-sulfonamide), was shown to have a potent and selective inhibitory action against cyclic AMP-dependent protein kinase (protein kinase A), with an ...
Chijiwa   +17 more
semanticscholar   +1 more source

Protein kinase A (PKA) phosphorylation of Shp2 inhibits its phosphatase activity and modulates ligand specificity. [PDF]

open access: yes, 2015
Pathological cardiac hypertrophy (an increase in cardiac mass resulting from stress-induced cardiac myocyte growth) is a major factor underlying heart failure.
O'Bryan, JP   +5 more
core  

RP1 is a phosphorylation target of CK2 and is involved in cell adhesion [PDF]

open access: yes, 2013
RP1 (synonym: MAPRE2, EB2) is a member of the microtubule binding EB1 protein family, which interacts with APC, a key regulatory molecule in the Wnt signalling pathway.
Renner, Christoph   +52 more
core   +2 more sources

Emerging experimental and computational methods for studying redox‐regulated structural transitions

open access: yesFEBS Letters, EarlyView.
Redox reactions can reshape proteins and alter how they behave in cells, with important consequences for health and disease. This review explores emerging experimental and computational approaches for discovering these redox‐sensitive protein switches, revealing their structural effects, and predicting their behavior, opening new opportunities to ...
Tasneem Rass   +2 more
wiley   +1 more source

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