Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2
about
Domain Swapping and Different Oligomeric States for the Complex Between Calmodulin and the Calmodulin-Binding Domain of Calcineurin AInsights into the oligomerization of CRMPs: crystal structure of human collapsin response mediator protein 5Collapsin response mediator protein 2: high-resolution crystal structure sheds light on small-molecule binding, post-translational modifications, and conformational flexibility.Collapsin response mediator proteins regulate neuronal development and plasticity by switching their phosphorylation status.Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins.Collapsin response mediator protein-2 is a calmodulin-binding proteinCollapsin response mediator protein-2 phosphorylation promotes the reversible retraction of oligodendrocyte processes in response to non-lethal oxidative stress.Opening Pandora's jar: a primer on the putative roles of CRMP2 in a panoply of neurodegenerative, sensory and motor neuron, and central disorders.Collapsin Response Mediator Protein-2 (CRMP2) is a Plausible Etiological Factor and Potential Therapeutic Target in Alzheimer's Disease: Comparison and Contrast with Microtubule-Associated Protein TauPhosphorylation and mRNA splicing of collapsin response mediator protein-2 determine inhibition of rho-associated protein kinase (ROCK) II function in carcinoma cell migration and invasion.Challenging the catechism of therapeutics for chronic neuropathic pain: Targeting CaV2.2 interactions with CRMP2 peptides.Collapsin response mediator protein-2: an emerging pathologic feature and therapeutic target for neurodisease indications.MICAL, the flavoenzyme participating in cytoskeleton dynamicsMolecular dynamics simulations and in vitro analysis of the CRMP2 thiol switch.Structure of human collapsin response mediator protein 1: a possible role of its C-terminal tail.Emerging roles of collapsin response mediator proteins (CRMPs) as regulators of voltage-gated calcium channels and synaptic transmission.Structural basis for CRMP2-induced axonal microtubule formation.A single structurally conserved SUMOylation site in CRMP2 controls NaV1.7 function.(S)-Lacosamide Binding to Collapsin Response Mediator Protein 2 (CRMP2) Regulates CaV2.2 Activity by Subverting Its Phosphorylation by Cdk5.Clozapine influences cytoskeleton structure and calcium homeostasis in rat cerebral cortex and has a different proteomic profile than risperidone.Chemical shift perturbation mapping of the Ubc9-CRMP2 interface identifies a pocket in CRMP2 amenable for allosteric modulation of Nav1.7 channelsCRMP2 and voltage-gated ion channels: potential roles in neuropathic pain
P2860
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P2860
Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2
description
2008 nî lūn-bûn
@nan
2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Crystal and solution structure ...... in response mediator protein 2
@ast
Crystal and solution structure ...... in response mediator protein 2
@en
Crystal and solution structure ...... in response mediator protein 2
@nl
type
label
Crystal and solution structure ...... in response mediator protein 2
@ast
Crystal and solution structure ...... in response mediator protein 2
@en
Crystal and solution structure ...... in response mediator protein 2
@nl
prefLabel
Crystal and solution structure ...... in response mediator protein 2
@ast
Crystal and solution structure ...... in response mediator protein 2
@en
Crystal and solution structure ...... in response mediator protein 2
@nl
P2093
P2860
P3181
P1433
P1476
Crystal and solution structure ...... in response mediator protein 2
@en
P2093
Noora Löytynoja
Petri Kursula
Viivi Majava
P2860
P304
P3181
P356
10.1111/J.1742-4658.2008.06601.X
P407
P577
2008-08-11T00:00:00Z