Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes. - Wikidata - wikimedia - TriplyDB

Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.

Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.

http://www.wikidata.org/entity/Q41833801

about

The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components MARCKS is a natively unfolded protein with an inaccessible actin-binding site: evidence for long-range intramolecular interactions Cross-talk unfolded: MARCKS proteins.Phosphoinositide 3-kinase-dependent membrane recruitment of p62(dok) is essential for its negative effect on mitogen-activated protein (MAP) kinase activation.Functional role of the interaction between polysialic acid and myristoylated alanine-rich C kinase substrate at the plasma membrane Quantitative proteomics analysis of human endothelial cell membrane rafts: evidence of MARCKS and MRP regulation in the sphingosine 1-phosphate-induced barrier enhancement.Macrophage-enriched myristoylated alanine-rich C kinase substrate and its phosphorylation is required for the phorbol ester-stimulated diffusion of beta 2 integrin molecules.MacMARCKS is not essential for phagocytosis in macrophages.A myristoyl/phosphoserine switch controls cAMP-dependent protein kinase association to membranes.Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization.RGS4 binds to membranes through an amphipathic alpha -helix.Interaction between actin and the effector peptide of MARCKS-related protein. Identification of functional amino acid segments.

P2860

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P2860

Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.

http://www.wikidata.org/entity/Q41833801

description

1998 nî lūn-bûn

@nan

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

1998年论文

@zh

1998年论文

@zh-cn

name

Binding of MARCKS (myristoylat ...... icular phospholipid membranes.

@en

type

label

Binding of MARCKS (myristoylat ...... icular phospholipid membranes.

@en

prefLabel

Binding of MARCKS (myristoylat ...... icular phospholipid membranes.

@en

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P1433

Biochemical Journal

P1476

Binding of MARCKS (myristoylat ...... icular phospholipid membranes.

@en

P2093

Ramsden JJ

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

Vergères G

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

P2860

MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin

Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein

The MARCKS family of cellular protein kinase C substrates

Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids

The myristoyl-electrostatic switch: a modulator of reversible protein-membrane interactions.

Membrane structure of protein kinase C and calmodulin binding domain of myristoylated alanine rich C kinase substrate determined by site-directed spin labeling.

Phosphorylation and associated translocation of the 87-kDa protein, a major protein kinase C substrate, in isolated nerve terminals

Phosphorylation reverses the membrane association of peptides that correspond to the basic domains of MARCKS and neuromodulin.

Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains.

MARCKS deficiency in mice leads to abnormal brain development and perinatal death.

P304

5-11

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P31

scholarly article

P356

10.1042/BJ3300005

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P407

P478

330 ( Pt 1)

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P577

1998-02-01T00:00:00Z

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P5875

13768345

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P698

9461483

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P932

1219100

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