Moesin, the major ERM protein of lymphocytes and platelets, differs from ezrin in its insensitivity to calpain.
about
Cytoskeletal protein radixin activates integrin alpha(M)beta(2) by binding to its cytoplasmic tailCD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathwayMolecular Mechanisms for cAMP-Mediated Immunoregulation in T cells - Role of Anchored Protein Kinase A Signaling UnitsA glimpse of the ERM proteinsMoesin controls clathrin-mediated S1PR1 internalization in T cellsSphingolipid regulation of ezrin, radixin, and moesin proteins family: implications for cell dynamics.The biology of extracellular vesicles with focus on platelet microparticles and their role in cancer development and progressionOrganizing the cell cortex: the role of ERM proteinsSpatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activationMegakaryocyte-derived microparticles: direct visualization and distinction from platelet-derived microparticlesMoesin regulates stable microtubule formation and limits retroviral infection in cultured cells.The cytoskeletal linker protein moesin: decreased levels in Wiskott-Aldrich syndrome platelets and identification of a cleavage pathway in normal platelets.Platelets mediate increased endothelium permeability in dengue through NLRP3-inflammasome activation.Ezrin is highly expressed in early thymocytes, but dispensable for T cell development in mice.Binding of moesin and ezrin to membranes containing phosphatidylinositol (4,5) bisphosphate: a comparative study of the affinity constants and conformational changes.Alveolar echinococcosis: characterization of diagnostic antigen Em18 and serological evaluation of recombinant Em18.Nodes of Ranvier form in association with ezrin-radixin-moesin (ERM)-positive Schwann cell processesImaging of T-cell interactions with antigen presenting cells in culture and in intact lymphoid tissue.The distal pole complex: a novel membrane domain distal to the immunological synapse.Proteomics analysis of the ezrin interactome in B cells reveals a novel association with Myo18aα.Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytes.Ezrin regulates focal adhesion and invadopodia dynamics by altering calpain activity to promote breast cancer cell invasion.Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin.Ezrin and moesin function together to promote T cell activation.Local phosphocycling mediated by LOK/SLK restricts ezrin function to the apical aspect of epithelial cellsCoordinate control of cytoskeletal remodeling and calcium mobilization during T-cell activationInhibition of calpain blocks platelet secretion, aggregation, and spreadingMembrane-organizing protein moesin controls Treg differentiation and antitumor immunity via TGF-β signalingCalpain-1 inhibitors for selective treatment of rheumatoid arthritis: what is the future?Calpain Genetic Disruption and HSP90 Inhibition Combine To Attenuate Mammary Tumorigenesis.Ezrin is a negative regulator of death receptor-induced apoptosis.Involvement of ezrin/moesin in de novo actin assembly on phagosomal membranes.Src phosphorylates ezrin at tyrosine 477 and induces a phosphospecific association between ezrin and a kelch-repeat protein family member.The ERM Protein Moesin Regulates CD8(+) Regulatory T Cell Homeostasis and Self-Tolerance.Radixin stimulates Rac1 and Ca2+/calmodulin-dependent kinase, CaMKII: cross-talk with Galpha13 signaling.The amino-terminal domains of the ezrin, radixin, and moesin (ERM) proteins bind advanced glycation end products, an interaction that may play a role in the development of diabetic complications.First Case of X-Linked Moesin Deficiency Identified After Newborn Screening for SCID.Endothelial cell calpain activity facilitates lymphocyte diapedesis.Moesin-deficient mice reveal a non-redundant role for moesin in lymphocyte homeostasis.Aberrant T Cell Signaling and Subsets in Systemic Lupus Erythematosus.
P2860
Q24298322-84433567-644D-481D-82AB-82D5D4DE0A91Q24598098-754A8E7A-4C85-4B3C-912A-EBED01D4B420Q26744973-C824ADB4-4C4C-42C8-9B8F-0845E3845326Q26765004-C27462DB-2114-4298-8099-C4A980C4664DQ27342788-5E37B708-3925-40C7-BBBA-1B5F212AEB6CQ27691440-D9ECD6EC-7DBB-40F4-9B9D-C609D5CA9891Q28066054-586A904F-449A-4DB1-81D4-9DD5B0C0D260Q28277373-12270BE8-6483-4ADA-8CED-47F766FD8853Q30478059-85800F25-83E6-4F66-8C23-164231F06C4EQ30485800-C59DDC27-F109-4336-B127-6F5608F6D1E9Q33266674-DC1CB346-032E-4524-9436-7E540BED0A89Q33329717-2FED0C45-6CD7-4537-B22C-7EC628E9C127Q33410191-47FDDC25-D434-47A8-B712-D88741E7C3D0Q33678939-DCC801B7-DAB4-4E28-A4E7-7904451D5FF3Q33952374-56DBEEA5-9A07-4034-A789-F97123A63737Q33964812-E05CC5DD-CE42-475A-B67E-83D9D065AF51Q34657208-5AE7E188-D2F9-4E3D-8E46-E48E89891D6AQ35005860-CC3E8B42-A9DD-4029-A436-27C45426A2F5Q35005877-92B85AAE-9CBC-40EA-ABBA-EB0BCD973F36Q35236062-BBB440A4-852C-4084-A00C-8180BA1F1393Q35775396-7AD9352E-3552-42DC-A66A-EED72D8F9766Q36115398-0D96A631-06CC-491B-AEAA-0E44BE44D466Q36149269-5D38896C-C1F1-4C0A-BCE1-61E88AAB3669Q36379032-2656DB4F-1444-4500-9090-1A516E4E3428Q36455890-EAF6B0DC-C94D-45A0-B8E9-7EE3BDD8B5BFQ37298815-1C98076A-8823-4DEC-8097-7C437AFC28D1Q37307187-0D4F4152-D44F-44F9-BF6D-45F0853CF5F5Q37730632-EC8C653D-9743-4359-9DB5-3BD6D4DFA2BFQ38161548-1A60362D-1069-439E-99C1-4A1E255D0EEBQ38769105-735A21C4-80D6-4737-BC23-68678A4A800FQ39771188-E0FEA651-591B-4479-9EA1-740ECE2694D8Q40386859-3C639275-E1A8-423D-A385-78CE3D00765AQ40476423-1142BCB7-9E57-4D2F-9303-8E3DE4F6BDC1Q42516322-91FF11F7-DFCD-4480-8610-DAFFC93149DCQ42809836-F5D49368-C0DA-4049-9954-A79C70561698Q44432075-F46D99AD-70BA-40C6-83DD-1716D58079B3Q45279328-1AC3ACA0-CCDA-4225-8758-9AF134AB9B00Q46741849-C50E1C85-9A05-4333-8103-866832476FBEQ54297674-326A0FFE-BDB3-4DF6-8FED-259B15A489CDQ55163735-8419ADEB-E1FE-438A-83FB-402E3C6DF32D
P2860
Moesin, the major ERM protein of lymphocytes and platelets, differs from ezrin in its insensitivity to calpain.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Moesin, the major ERM protein ...... its insensitivity to calpain.
@en
Moesin, the major ERM protein ...... its insensitivity to calpain.
@nl
type
label
Moesin, the major ERM protein ...... its insensitivity to calpain.
@en
Moesin, the major ERM protein ...... its insensitivity to calpain.
@nl
prefLabel
Moesin, the major ERM protein ...... its insensitivity to calpain.
@en
Moesin, the major ERM protein ...... its insensitivity to calpain.
@nl
P2093
P2860
P1433
P1476
Moesin, the major ERM protein ...... its insensitivity to calpain.
@en
P2093
A Bretscher
A Shcherbina
D M Kenney
E Remold-O'Donnell
P2860
P356
10.1016/S0014-5793(98)01674-3
P407
P577
1999-01-01T00:00:00Z