CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
about
IQGAP1 interacts with components of the slit diaphragm complex in podocytes and is involved in podocyte migration and permeability in vitroCortactin signalling and dynamic actin networksPodocin, a raft-associated component of the glomerular slit diaphragm, interacts with CD2AP and nephrinNephrin forms a complex with adherens junction proteins and CASK in podocytes and in Madin-Darby canine kidney cells expressing nephrinRole of Neuropilin-1 in Diabetic NephropathyRoles of adaptor proteins in podocyte biologyThe Rac1 hypervariable region in targeting and signaling: a tail of many storiesThe genetics and neuropathology of Alzheimer's diseaseCapping protein regulators fine-tune actin assembly dynamicsFyn binds to and phosphorylates the kidney slit diaphragm component NephrinA Cortactin-CD2-associated protein (CD2AP) complex provides a novel link between epidermal growth factor receptor endocytosis and the actin cytoskeletonLinking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85CD2AP/CMS regulates endosome morphology and traffic to the degradative pathway through its interaction with Rab4 and c-CblThe carboxyl terminus of Neph family members binds to the PDZ domain protein zonula occludens-1Ptf1a directly controls expression of immunoglobulin superfamily molecules Nephrin and Neph3 in the developing central nervous systemCD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survivalSlit diaphragms contain tight junction proteinsNephrin and CD2AP associate with phosphoinositide 3-OH kinase and stimulate AKT-dependent signalingStructure of the kidney slit diaphragm adapter protein CD2-associated protein as determined with electron microscopy.Inhibition of CIN85-mediated invasion by a novel SH3 domain binding motif in the lysyl oxidase propeptide.Rac1 recruits the adapter protein CMS/CD2AP to cell-cell contacts.CD2AP mutations are associated with sporadic nephrotic syndrome and focal segmental glomerulosclerosis (FSGS).CIN85/CMS family of adaptor molecules.Activation of adenosine 2A receptors preserves structure and function of podocytesCD2AP links cortactin and capping protein at the cell periphery to facilitate formation of lamellipodia.A novel TRPC6 mutation that causes childhood FSGS.Molecular genetic analysis of podocyte genes in focal segmental glomerulosclerosis--a review.Chromosome 2q31.1 associates with ESRD in women with type 1 diabetes.Transcriptional activation of the human CD2AP promoter by E2F1.Anion exchanger 1 interacts with nephrin in podocytes.Focusing on the glomerular slit diaphragm: podocin enters the pictureGenetic models: clues for understanding the pathogenesis of idiopathic nephrotic syndrome.Characterization of the interactions of the nephrin intracellular domain.Genetic causes of proteinuria and nephrotic syndrome: impact on podocyte pathobiology.Transcriptional induction of slit diaphragm genes by Lmx1b is required in podocyte differentiation.The LIM-homeodomain transcription factor Lmx1b plays a crucial role in podocytes.Advances in the biology and genetics of the podocytopathies: implications for diagnosis and therapyRelevance of VEGF and nephrin expression in glomerular diseases.Vascular endothelial growth factor receptor 2 direct interaction with nephrin links VEGF-A signals to actin in kidney podocytesPathogenic pathways are activated in each major cell type of the glomerulus in the Cd2ap mutant mouse model of focal segmental glomerulosclerosis
P2860
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P2860
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@ast
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@en
type
label
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@ast
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@en
prefLabel
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@ast
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@en
P2093
P2860
P1476
CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.
@en
P2093
P2860
P304
P356
10.1016/S0002-9440(10)63080-5
P407
P577
2001-12-01T00:00:00Z