Direct binding of neutral endopeptidase 24.11 to ezrin/radixin/moesin (ERM) proteins competes with the interaction of CD44 with ERM proteins. - Wikidata - awgldk - TriplyDB

Direct binding of neutral endopeptidase 24.11 to ezrin/radixin/moesin (ERM) proteins competes with the interaction of CD44 with ERM proteins.

Direct binding of neutral endopeptidase 24.11 to ezrin/radixin/moesin (ERM) proteins competes with the interaction of CD44 with ERM proteins.

http://www.wikidata.org/entity/Q38346327

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Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex Ezrin-radixin-moesin (ERM)-binding phosphoprotein 50 organizes ERM proteins at the apical membrane of polarized epithelia Characterization of a novel interaction between ELMO1 and ERM proteins.Casein kinase 2 dependent phosphorylation of neprilysin regulates receptor tyrosine kinase signaling to Akt Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation.Amyloid beta-degrading cryptidases: insulin degrading enzyme, presequence peptidase, and neprilysin.Role of neprilysin in airway inflammation induced by diesel exhaust emissions.Possible involvement of CD10 in the development of endometriosis due to its inhibitory effects on CD44-dependent cell adhesion.Merlin and the ERM proteins--regulators of receptor distribution and signaling at the cell cortex.Concise review: neutral endopeptidase (CD10): a multifaceted environment actor in stem cells, physiological mechanisms, and cancer.Adenoviral neutral endopeptidase gene delivery in combination with paclitaxel for the treatment of prostate cancer.Ezrin/radixin/moesin are required for the purinergic P2X7 receptor (P2X7R)-dependent processing of the amyloid precursor protein.Neprilysin inhibits angiogenesis via proteolysis of fibroblast growth factor-2.Neuropeptide-stimulated cell migration in prostate cancer cells is mediated by RhoA kinase signaling and inhibited by neutral endopeptidase.Prostate cancer invasion is influenced more by expression of a CD44 isoform including variant 9 than by Muc18.Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tails of adhesion molecules CD43 and PSGL-1 Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP)Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of adhesion molecule CD44.Rational redesign of neutral endopeptidase binding to merlin and moesin proteins.Negative regulation of NEP expression by hypoxia.Hyaluronan synthesis inhibitor supplements the inhibitory effects of zoledronic acid on bone metastasis of lung cancer.

P2860

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P2860

Direct binding of neutral endopeptidase 24.11 to ezrin/radixin/moesin (ERM) proteins competes with the interaction of CD44 with ERM proteins.

http://www.wikidata.org/entity/Q38346327

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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name

Direct binding of neutral endo ...... ion of CD44 with ERM proteins.

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Direct binding of neutral endo ...... ion of CD44 with ERM proteins.

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P1433

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P1433

Journal of Biological Chemistry

P1476

Direct binding of neutral endo ...... ion of CD44 with ERM proteins.

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P2093

Akira Iwase

http://www.w3.org/2001/XMLSchema#string

Daniel Navarro

http://www.w3.org/2001/XMLSchema#string

David M Nanus

http://www.w3.org/2001/XMLSchema#string

Ruoqian Shen

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular cloning of the common acute lymphoblastic leukemia antigen (CALLA) identifies a type II integral membrane protein

NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin

Ezrin is a cyclic AMP-dependent protein kinase anchoring protein

CD44 cell adhesion molecules

Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway

Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2

Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain

Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation

Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4, 5-bisphosphate

P304

11898-11905

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scholarly article

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10.1074/JBC.M212737200

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12

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P478

279

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P577

2004-01-02T00:00:00Z

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P698

14704146

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