Results 51 to 60 of about 1,406,847 (366)

Protein phosphorylation in cyanobacteria [PDF]

Microbiology, 1994
The post-translational modification of proteins by phosphorylation may take a variety of forms, but in essence it is always a component of a process of adaptation that enables cells to sense and respond to changes in their external or internal environments.
openaire   +2 more sources

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

FEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

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

Cell 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, Virginia De Cesare, Julien Peltier, Axel Knebel, Yosua Adi Kristaryianto, Daniel T. Rogerson, Yogesh Kulathu, Matthias Trost, Jason W. Chin   +8 more
doaj   +1 more source

Phosphoproteins associated with cyclic nucleotide stimulation of ciliary motility in Paramecium [PDF]

, 1990
Permeabilized, MgATP-reactivated cells of Paramecium (models) respond to cyclic AMP and cyclic GMP by increasing forward swimming speed. In association with the motile response, cyclic AMP and 8-bromo-cyclic GMP (8-Br-cyclic GMP) stimulated protein ...
Bonini, Nancy M., Nelson, David L.
core  

N-site phosphorylation systems with 2N-1 steady states

, 2014
Multisite protein phosphorylation plays a prominent role in intracellular processes like signal transduction, cell-cycle control and nuclear signal integration.
Conradi, Carsten, Flockerzi, Dietrich, Holstein, Katharina   +2 more
core   +1 more source

Charge environments around phosphorylation sites in proteins [PDF]

, 2008
Background: Phosphorylation is a central feature in many biological processes. Structural analyses have identified the importance of charge-charge interactions, for example mediating phosphorylation-driven allosteric change and protein binding to ...
Kitchen, James, Saunders, Rebecca E., Warwicker, Jim   +2 more
core   +2 more sources

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

FEBS 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, Tanmay Kumar Mohanty, Rashna Bhandari, Dorothea Fiedler   +3 more
wiley   +1 more source

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

Scientific 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, Thomas Carroll, Thomas Macartney, Susanne Bandau, Constance Alabert, Giulia Saredi, Rachel Toth, John Rouse   +7 more
doaj   +1 more source

Determination of Cellular Phosphatidylinositol-3-phosphate (PI3P) Levels Using a Fluorescently Labelled Selective PI3P Binding Domain (PX)

Bio-Protocol, 2016
The lipid Phosphatidylinositol-3-phosphate [PtdIns3P or PI(3)P] plays many membrane trafficking roles and is primarily produced by the Class III PI3K, VPS34. Determining the level of cellular PI(3)P however can be complex.
Michael Munson, Ian Ganley
doaj   +1 more source

Activation of Ciona sperm motility: phosphorylation of dynein polypeptides and effects of a tyrosine kinase inhibitor [PDF]

, 1991
A high molecular mass dynein ATPase polypeptide and a 18–20 kDa dynein light chain of Ciona sperm flagella are phosphorylated during in vivo activation of motility or in vitro activation of motility by incubation with cyclic AMP.
Brokaw, Charles J., Dey, Chinmoy S.
core