MSN

(redirected from Moesin)
Also found in: Medical.
AcronymDefinition
MSNMicrosoft Network
MSNMaster's of Science in Nursing
MSNMission
MSNMobile Suit (Newtype; Gundam gaming)
MSNMedical Surgical Nursing
MSNMessi-Suárez-Neymar (nickname for Barcelona soccer stars)
MSNMake Some Noise
MSNMobile Social Network
MSNMobile Ad-Hoc and Sensor Networks (International Conference)
MSNMedicare Summary Notice
MSNMultiple Subscriber Number (ISDN)
MSNMichigan School of Nursing
MSNMiddle School North (various locations)
MSNModem Serial Number
MSNMultilayer Switched Network
MSNMulticast Service Node
MSNManufacturing Sequence Number
MSNMultiple Serial Number
MSNMultiple Subscriber Number
MSNMobile Service Node
MSNMulti System Network
MSNManagement Services Network (various locations)
MSNMahou Sensei Negima (anime)
MSNMessage Sequence Number
MSNMandatory Spay/Neuter
MSNMuseum Security Network (mailing list)
MSNMartian Successor Nadesico (anime series)
MSNMicrosoft Service Network
MSNMaquila Solidarity Network (Canada)
MSNManufacturer Serial Number
MSNMilitary Service Number
MSNMoesin (gene)
MSNMexico Solidarity Network
MSNMerchant Services Network
MSNMulti-Service Network
MSNMultiple Special Needs
MSNMedium Spiny Neurons
MSNMath/Science Network (Oakland, CA)
MSNMadison, WI, USA - Dane County Regional Airport (Airport Code)
MSNMonitoring Cell Sequence Number
MSNMost Significant Nibble
MSNMulti-Service Node
MSNMaine Support Network (Readfield, ME)
MSNMuslim Student Network
MSNMechanical Serial Number
MSNMesoporous Silica Nanoparticle
MSNMarine Safety Network
MSNModern Satellite Network
MSNMemorial Service Network (National Cemetery Administration; US VA)
MSNMethodist Student Network (University of South Carolina)
MSNMass Spectrometry to the N-th Power
MSNMigration Storage Node
References in periodicals archive ?
N-terminal (JH 7) of Jak molecule has a receptor binding site while C-terminal (JH 1) is responsible for catalytic activity.1,3 These regions have four functional domains, which includes a FERM (band 4.1, ezrin, radixin, moesin), an SH2 (Src homology 2) like domain, a tyrosine kinase and kinase-like pseudokinase domain.4,6-8
Merlin is a member of the band 4.1-superfamily of proteins and has some sequence homology with the Ezrin, radixin, and moesin (ERM) family.
Merlin protein is part of 4.1 protein family, with homologies with other proteins, such as ezrin, radixin, and moesin [8].
Huang, "Role of moesin, Src, and ROS in advanced glycation end productinduced vascular endothelial dysfunction," Microcirculation, vol.
In TCR stimulation process, LCK can activate VAV GTPase to control the status of ezrin and moesin cytoskeletal protein phosphorylation, which regulates a series of protein translocation events [31, 32].
Furthermore, according to our previous work [17, 34], we detected in PD samples with respect to CTR a significantly lower level of the protein ezrin, a member of the ERM (ezrin, radixin, and moesin) protein family, involved in the connection of major cytoskeletal structures to the plasma membrane [44].
FAK contains three distinct domains: a four-point-one, ezrin, radixin, moesin (FERM) domain; a kinase domain; and a focal adhesion targeting (FAT) domain [21].
Interaction of the ICL of TM4SF5 with the F1 lobe in the four-pointone, ezrin, radixin, moesin (FERM) domain of FAK releases the inhibitory intramolecular interaction between the FERM domain (F2 lobe) and the kinase domain (C lobe centered on Phe562) leading to transautophosphorylation of the Tyr 397, which is buried by the intramolecular interaction in FAK [12].
PP1-mediated moesin dephosphorylation couples polar relaxation to mitotic exit.
(177) There is also a significant group of miRNAs whose targets are associated with cell protrusions and the cytoskeleton, including transgelin 2 (TAGLN2), targeted by miR-1, (178) moesin (MSN), and actin-related protein 2/3 complex, subunit 5 (ARPC5), targeted by miR-133a, (179,180) and podoplanin (PDPN) targeted by miR-363.
Role for moesin in lipopolysaccharide-stimulated signal transduction.
The microvilli are associated to the intermediate filament cytoskeleton, being very rich in ezrin and moesin, two members of the ERM (ezrin/radixin/moesin) family, and their respective transmembrane-binding proteins, such as CD44 with actin polymerization, all colocalized within these membrane protrusions [17].