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MARCKSL1 gene

Known as: MLP1, F52, MARCKS-like 1 
National Institutes of Health

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1 relation

Broader (1)

Genes

Papers overview

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Highly Cited
2003
Highly Cited
2003
Free energy landscape of protein folding in water: Explicit vs. implicit solvent
The Generalized Born (GB) continuum solvent model is arguably the most widely used implicit solvent model in protein folding and… 
Highly Cited
2003
Highly Cited
2003
TGFβ directs gene expression of activated microglia to an anti‐inflammatory phenotype strongly focusing on chemokine genes and cell migratory genes
In experimental autoimmune encephalomyelitis, the acute phase of the disease is produced by T‐helper lymphocyte type 1 (TH1… 
Highly Cited
2002
Highly Cited
2002
Lateral Sequestration of Phosphatidylinositol 4,5-Bisphosphate by the Basic Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Is Due to Nonspecific Electrostatic Interactions*
A peptide corresponding to the basic (+13), unstructured effector domain of myristoylated alanine-rich C kinase substrate (MARCKS… 
Highly Cited
2000
Highly Cited
2000
Selective transcriptional regulations in the human liver cell by hepatitis B viral X protein.
The hepatitis B viral X protein (HBx) is known as a transcription factor and potential oncogene. To gain a better view of the… 
Highly Cited
1996
Highly Cited
1996
Neural tube defects and abnormal brain development in F52-deficient mice.
F52 is a myristoylated, alanine-rich substrate for protein kinase C. We have generated F52-deficient mice by the gene targeting… 
Highly Cited
1996
Highly Cited
1996
Disruption of the MacMARCKS gene prevents cranial neural tube closure and results in anencephaly.
MacMARCKS is a member of the MARCKS family of protein kinase C (PKC) substrates. Biochemical evidence demonstrates that these… 
Highly Cited
1996
Highly Cited
1996
Myristoylation-dependent and Electrostatic Interactions Exert Independent Effects on the Membrane Association of the Myristoylated Alanine-rich Protein Kinase C Substrate Protein in Intact Cells*
The myristoylated alanine-rich protein kinase C substrate (MARCKS) is a widely expressed, prominent substrate for protein kinase… 
Highly Cited
1995
Highly Cited
1995
MacMARCKS Mutation Blocks Macrophage Phagocytosis of Zymosan (*)
A major protein kinase C substrate, MacMARCKS (F52, MPR), was examined for its role in phagocytosis. In macrophage-phagocytosing… 
Review
1995
Review
1995
The MARCKS family of protein kinase-C substrates.
37 Hallak, H., Muszbek, L., Laposata, M., Belmonte, E., 39 Neupert, T. A., Johnson, R. S., Hurley, J. B. and Brass, L. F. and… 
Highly Cited
1992
Highly Cited
1992
MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates
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