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The MARCKS family of cellular protein kinase C substrates.

作者信息

Blackshear P J

机构信息

Howard Hughes Medical Institute Laboratories, Duke University Medical Center, Durham, North Carolina 27710.

出版信息

J Biol Chem. 1993 Jan 25;268(3):1501-4.

PMID:8420923
Abstract
摘要

相似文献

1
The MARCKS family of cellular protein kinase C substrates.细胞蛋白激酶C底物的MARCKS家族
J Biol Chem. 1993 Jan 25;268(3):1501-4.
2
The MARCKS family of protein kinase-C substrates.蛋白激酶C底物的MARCKS家族。
Biochem Soc Trans. 1995 Aug;23(3):587-91. doi: 10.1042/bst0230587.
3
Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species.主要蛋白激酶C底物酸性80 kDa蛋白激酶C底物(80K)与肉豆蔻酰化富含丙氨酸的蛋白激酶C底物(MARCKS)之间的关系。不同物种中一个基因家族的成员或等效基因。
Eur J Biochem. 1992 Oct 1;209(1):7-14. doi: 10.1111/j.1432-1033.1992.tb17255.x.
4
The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane.豆蔻酰化富含丙氨酸的蛋白激酶C底物(MARCKS)和MARCKS相关蛋白的豆蔻酰部分嵌入膜中。
J Biol Chem. 1995 Aug 25;270(34):19879-87. doi: 10.1074/jbc.270.34.19879.
5
Protein kinase C-mediated phosphorylation of the myristoylated alanine-rich C-kinase substrate protects it from specific proteolytic cleavage.蛋白激酶C介导的富含肉豆蔻酰化丙氨酸的C激酶底物的磷酸化可保护其免受特定的蛋白水解切割。
J Biol Chem. 1996 Jan 5;271(1):553-62. doi: 10.1074/jbc.271.1.553.
6
Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP).钙调蛋白与源自豆蔻酰化富含丙氨酸的蛋白激酶C底物(MARCKS)和MARCKS相关蛋白(MRP)的肽复合后的钙结合及构象特性。
Eur Biophys J. 1997;25(4):239-47. doi: 10.1007/s002490050036.
7
Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein.蛋白激酶C介导的重组肉豆蔻酰化富含丙氨酸的C激酶底物(MARCKS)和MARCKS相关蛋白的磷酸化及钙调蛋白结合
J Biol Chem. 1994 Mar 25;269(12):9361-7.
8
Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein appears to involve myristate-dependent binding in the absence of a myristoyl protein receptor.富含豆蔻酰化丙氨酸的蛋白激酶C底物(MARCKS)蛋白与膜的结合似乎在没有豆蔻酰化蛋白受体的情况下涉及豆蔻酸盐依赖性结合。
J Biol Chem. 1992 Dec 5;267(34):24879-85.
9
Differential expression of MARCKS and other calmodulin-binding protein kinase C substrates in cultured neuroblastoma and glioma cells.培养的神经母细胞瘤和胶质瘤细胞中MARCKS及其他钙调蛋白结合蛋白激酶C底物的差异表达
J Neurochem. 1994 Dec;63(6):2314-23. doi: 10.1046/j.1471-4159.1994.63062314.x.
10
A mouse brain cDNA encodes a novel protein with the protein kinase C phosphorylation site domain common to MARCKS.一种小鼠脑cDNA编码一种具有与MARCKS共有的蛋白激酶C磷酸化位点结构域的新型蛋白质。
FEBS Lett. 1991 Jul 29;286(1-2):147-51. doi: 10.1016/0014-5793(91)80961-2.

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Sensitive fluorescent biosensor reveals differential subcellular regulation of PKC.灵敏的荧光生物传感器揭示了蛋白激酶C的亚细胞差异调节。
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Calmodulin: a highly conserved and ubiquitous Ca sensor.
钙调蛋白:一种高度保守且普遍存在的 Ca 传感器。
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Sensitive Fluorescent Biosensor Reveals Differential Subcellular Regulation of PKC.灵敏的荧光生物传感器揭示蛋白激酶C的亚细胞差异调控
bioRxiv. 2024 Mar 30:2024.03.29.587373. doi: 10.1101/2024.03.29.587373.
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Antitumor effects of chemically modified miR-143 lipoplexes in a mouse model of pelvic colorectal cancer via myristoylated alanine-rich C kinase substrate downregulation.化学修饰的miR-143脂质复合物通过下调富含肉豆蔻酰化丙氨酸的C激酶底物对盆腔结直肠癌小鼠模型的抗肿瘤作用
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LINC01268 promotes epithelial-mesenchymal transition, invasion and metastasis of gastric cancer the PI3K/Akt signaling pathway and targeting MARCKS.LINC01268通过PI3K/Akt信号通路并靶向MARCKS促进胃癌的上皮-间质转化、侵袭和转移。
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A myristoylated alanine-rich C-kinase substrate (MARCKS) inhibitor peptide attenuates neutrophil outside-in β-integrin activation and signaling.一个豆蔻酰化的丙氨酸丰富的 C 激酶底物(MARCKS)抑制剂肽可减弱中性粒细胞外向β整合素激活和信号转导。
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