Mechanism of selective stabilization of extrinsic polypeptides in PSII particles by glycinebetaine

1998 ◽  
Vol 41 (3) ◽  
pp. 278-285
Author(s):  
Caixia Hou ◽  
Xinjian Yu ◽  
Rong Li ◽  
Zhangcheng Tang ◽  
Yungang Shen ◽  
...  
Keyword(s):  
Selective Stabilization ◽  
Extrinsic Polypeptides

Selective stabilization supports phosphatase targeting in cancer

2020 ◽  
Vol 19 (6) ◽  
pp. 387-387
Author(s):  
Joseph Willson
Keyword(s):  
Selective Stabilization

Selective Stabilization and Destabilization of Protein Domains in Tissue-Type Plasminogen Activator Using Formulation Excipients

2018 ◽  
Vol 16 (2) ◽  
pp. 744-755 ◽  
Author(s):  
Mathew J. Robinson ◽  
Paul Matejtschuk ◽  
Colin Longstaff ◽  
Paul A. Dalby
Keyword(s):  
Plasminogen Activator ◽  
Protein Domains ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Selective Stabilization ◽  
Type Plasminogen Activator

RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: evidence for selective stabilization of RyR1 channel

2004 ◽  
Vol 287 (1) ◽  
pp. C36-C45 ◽  
Author(s):  
Takashi Murayama ◽  
Yasuo Ogawa
Keyword(s):  
Binding Sites ◽  
Skeletal Muscles ◽  
Specific Activity ◽  
Adenine Nucleotides ◽  
Minor Effect ◽  
Mammalian Skeletal Muscle ◽  
Selective Stabilization ◽  
Underlying Mechanisms ◽  
A Minor

We showed that frog α-ryanodine receptor (α-RyR) had a lower gain of Ca2+-induced Ca2+ release (CICR) activity than β-RyR in sarcoplasmic reticulum (SR) vesicles, indicating selective “stabilization” of the former isoform (Murayama T and Ogawa Y. J Biol Chem 276: 2953–2960, 2001). To know whether this is also the case with mammalian RyR1, we determined [3H]ryanodine binding of RyR1 and RyR3 in bovine diaphragm SR vesicles. The value of [3H]ryanodine binding (B) was normalized by the number of maximal binding sites (Bmax), whereby the specific activity of each isoform was expressed. This B/Bmax expression demonstrated that ryanodine binding of individual channels for RyR1 was <15% that for RyR3. Responses to Ca2+, Mg2+, adenine nucleotides, and caffeine were not substantially different between in situ and purified isoforms. These results suggest that the gain of CICR activity of RyR1 is markedly lower than that of RyR3 in mammalian skeletal muscle, indicating selective stabilization of RyR1 as is true of frog α-RyR. The stabilization was partly eliminated by FK506 and partly by solubilization of the vesicles with CHAPS, each of which was additive to the other. In contrast, high salt, which greatly enhances [3H]ryanodine binding, caused only a minor effect on the stabilization of RyR1. None of the T-tubule components, coexisting RyR3, or calmodulin was the cause. The CHAPS-sensitive intra- and intermolecular interactions that are common between mammalian and frog skeletal muscles and the isoform-specific inhibition by FKBP12, which is characteristic of mammals, are likely to be the underlying mechanisms.

Selective stabilization of images acquired by unmanned ground vehicles

1997 ◽  
Vol 13 (5) ◽  
pp. 693-708 ◽  
Author(s):  
Y.S. Yao ◽  
R. Chellapa
Keyword(s):  
Unmanned Ground Vehicles ◽  
Ground Vehicles ◽  
Selective Stabilization

scholarly journals Atomic model of microtubule-bound tau

2018 ◽  
Author(s):  
Elizabeth H. Kellogg ◽  
Nisreen M.A. Hejab ◽  
Simon Poepsel ◽  
Kenneth H. Downing ◽  
Frank DiMaio ◽  
...  
Keyword(s):  
High Resolution ◽  
Physiological Role ◽  
Biochemical Data ◽  
Disease Pathogenesis ◽  
Developmentally Regulated ◽  
Computational Approaches ◽  
Selective Stabilization ◽  
Tubulin Binding ◽  
Future Treatments ◽  
Β Tubulin

AbstractTau is a developmentally regulated protein found in axons, whose physiological role is to stabilize and bundle microtubules (MTs). Hyper-phosphorylation of tau is thought to cause its detachment from MTs and subsequent aggregation into pathological fibrils that have been implicated in Alzheimer’s disease pathogenesis. Despite its known MT binding role, there is no consensus regarding which tau residues are crucial for tau-MT interactions, where on the MT tau binds, and how binding results in MT stabilization. We have used cryo-EM to visualize the interaction of different tau constructs with MTs at high resolution (3.2-4.8 Å) and used computational approaches to generate atomic models of tau-tubulin interactions. Our work shows that the highly conserved tubulin-binding repeats within tau adopt very similar structures in their interactions with the MT. Each tau repeat binds the MT exterior and adopts an extended structure along the crest of the protofilament (PF), interacting with both α- and β-tubulin, thus stabilizing the interface between tubulin dimers. Our structures agree with and explain previous biochemical data concerning the effect of phosphorylation on MT affinity and lead to a model in which tau repeats bind in tandem along a PF, tethering together tubulin dimers and stabilizing longitudinal polymerization interfaces. These structural findings could establish a basis of future treatments aiming at the selective stabilization of tau-MT interactions.

scholarly journals The Dynamic Modulation of GABAA Receptor Trafficking and Its Role in Regulating the Plasticity of Inhibitory Synapses

2011 ◽  
Vol 91 (3) ◽  
pp. 1009-1022 ◽  
Author(s):  
Mansi Vithlani ◽  
Miho Terunuma ◽  
Stephen J. Moss
Keyword(s):  
Neuronal Excitability ◽  
Tonic Inhibition ◽  
Inhibitory Synapses ◽  
General Anesthetics ◽  
Selective Stabilization ◽  
Neuronal Plasma Membrane ◽  
Sites Of Action ◽  
And Behavior ◽  
The Impact ◽  
The Brain

Inhibition in the adult mammalian central nervous system (CNS) is mediated by γ-aminobutyric acid (GABA). The fast inhibitory actions of GABA are mediated by GABA type A receptors (GABAARs); they mediate both phasic and tonic inhibition in the brain and are the principle sites of action for anticonvulsant, anxiolytic, and sedative-hypnotic agents that include benzodiazepines, barbiturates, neurosteroids, and some general anesthetics. GABAARs are heteropentameric ligand-gated ion channels that are found concentrated at inhibitory postsynaptic sites where they mediate phasic inhibition and at extrasynaptic sites where they mediate tonic inhibition. The efficacy of inhibition and thus neuronal excitability is critically dependent on the accumulation of specific GABAAR subtypes at inhibitory synapses. Here we evaluate how neurons control the number of GABAARs on the neuronal plasma membrane together with their selective stabilization at synaptic sites. We then go on to examine the impact that these processes have on the strength of synaptic inhibition and behavior.

Sign in / Sign up

Export Citation Format

Share Document