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MARCKSL1 gene
Known as:
MLP1
, F52
, MARCKS-like 1
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National Institutes of Health
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Related topics
Related topics
1 relation
Broader (1)
Genes
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2000
Highly Cited
2000
Selective transcriptional regulations in the human liver cell by hepatitis B viral X protein.
Jae-Seok Han
,
Hae Yong Yoo
,
Byung Hyune Choi
,
Hyune Mo Rho
Biochemical and Biophysical Research…
2000
Corpus ID: 6346564
The hepatitis B viral X protein (HBx) is known as a transcription factor and potential oncogene. To gain a better view of the…
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1998
1998
MacMARCKS Is Not Essential for Phagocytosis in Macrophages*
D. Underhill
,
Jianmin Chen
,
L. Allen
,
A. Aderem
Journal of Biological Chemistry
1998
Corpus ID: 21241051
MacMARCKS (also known as myristoylated alanine-rich protein kinase C substrate (MARCKS)-related protein) is a member of the…
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1998
1998
Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes.
Guy Vergères
,
Jeremy J. Ramsden
Biochemical Journal
1998
Corpus ID: 37647202
The myristoylated alanine-rich C kinase substrate (MARCKS) protein family has two known members, MARCKS itself and MARCKS-related…
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Highly Cited
1996
Highly Cited
1996
Neural tube defects and abnormal brain development in F52-deficient mice.
Min Wu
,
Dong Feng Chen
,
Toshikuni Sasaoka
,
Susumu Tonegawa
Proceedings of the National Academy of Sciences…
1996
Corpus ID: 43716120
F52 is a myristoylated, alanine-rich substrate for protein kinase C. We have generated F52-deficient mice by the gene targeting…
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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*
Sharon L. Swierczynski
,
P. Blackshear
Journal of Biological Chemistry
1996
Corpus ID: 45065282
The myristoylated alanine-rich protein kinase C substrate (MARCKS) is a widely expressed, prominent substrate for protein kinase…
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Highly Cited
1996
Highly Cited
1996
Role of MacMARCKS in Integrin-dependent Macrophage Spreading and Tyrosine Phosphorylation of Paxillin*
Jianxun Li
,
Zixin Zhu
,
Zhihua Bao
Journal of Biological Chemistry
1996
Corpus ID: 7152660
The cellular function of the MARCKS family of protein kinase C substrates is unknown. In this report, we present evidence that…
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Highly Cited
1995
Highly Cited
1995
MacMARCKS Mutation Blocks Macrophage Phagocytosis of Zymosan (*)
Zixin Zhu
,
Zhihua Bao
,
Jianxun Li
Journal of Biological Chemistry
1995
Corpus ID: 20993893
A major protein kinase C substrate, MacMARCKS (F52, MPR), was examined for its role in phagocytosis. In macrophage-phagocytosing…
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1993
1993
Nucleotide sequence, expression, and chromosomal mapping of Mrp and mapping of five related sequences.
D. Lobach
,
J. Rochelle
,
M. Watson
,
M. Seldin
,
P. Blackshear
Genomics
1993
Corpus ID: 19666022
We isolated and characterized a genomic clone for the mouse MARCKS-related protein, or MRP, also known as F52 and MacMARCKS. A…
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1993
1993
Regulation of peptide-calmodulin complexes by protein kinase C in vivo.
R. Hinrichsen
,
P. Blackshear
Proceedings of the National Academy of Sciences…
1993
Corpus ID: 27922253
We used the freshwater protozoan Paramecium tetraurelia to investigate the potential regulation by protein kinase C of calmodulin…
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Highly Cited
1992
Highly Cited
1992
MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates
Jianxun Li
,
A. Aderem
Cell
1992
Corpus ID: 2848152
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