The myristoylated alanine-rich C-kinase substrates (MARCKS): A membrane-anchored mediator of the cell function

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

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The Marcks brothers: A family of protein kinase C substrates

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Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5‐trisphosphate receptors in signal transduction through the B‐cell antigen receptor

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

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A role for MARCKS, the alpha isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages.

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Phosphorylation-regulated calmodulin binding to a prominent cellular substrate for protein kinase C

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The novel and specific Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4-methyl-5-isoquinoline)sulfonyl]-homopiperazine as a probing molecule for Rho-kinase-involved pathway

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Myristoylated Alanine-rich C Kinase Substrate (MARCKS) Produces Reversible Inhibition of Phospholipase C by Sequestering Phosphatidylinositol 4,5-Bisphosphate in Lateral Domains

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Adducin Is an In Vivo Substrate for Protein Kinase C: Phosphorylation in the MARCKS-related Domain Inhibits Activity in Promoting Spectrin–Actin Complexes and Occurs in Many Cells, Including Dendritic Spines of Neurons

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PIP3, PIP2, and Cell Movement—Similar Messages, Different Meanings?

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Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia.

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PIP2 signaling in lipid domains: a critical re‐evaluation

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The Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Binds Strongly to Phosphatidylinositol 4,5-Bisphosphate

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Identification of a phosphoinositide binding motif that mediates activation of mammalian and yeast phospholipase D isoenzymes

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Adducin Regulation

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Molecular Cloning and Characterization of a Novel Human Diacylglycerol Kinase ζ

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HMGB1, a pathogenic molecule that induces neurite degeneration via TLR4-MARCKS, is a potential therapeutic target for Alzheimer’s disease

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A 104-kDa diacylglycerol kinase containing ankyrin-like repeats localizes in the cell nucleus.

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Primary structure and domain organization of human alpha and beta adducin.

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Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C

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Phosphorylation-dependent binding of a synthetic MARCKS peptide to calmodulin.

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Transforming growth factor-β1 enhances the invasiveness of human MDA-MB-231 breast cancer cells by up-regulating urokinase activity

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Human GAP 43: Its deduced amino acid sequence and chromosomal localization in mouse and human

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Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain

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The role of protein kinase C and its neuronal substrates dephosphin, B-50, and MARCKS in neurotransmitter release

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A Computational Model for the Electrostatic Sequestration of PI(4,5)P2 by Membrane-Adsorbed Basic Peptides

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Tumor necrosis factor alpha modifies agonist-dependent responses in human neutrophils by inducing the synthesis and myristoylation of a specific protein kinase C substrate.

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Disruption of the MacMARCKS gene prevents cranial neural tube closure and results in anencephaly.

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Neural tube defects and abnormal brain development in F52-deficient mice.

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Myristoylated and Nonmyristoylated Forms of a Protein Are Phosphorylated by Protein Kinase C

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The Myristoylated Alanine‐Rich C‐Kinase Substrate (MARCKS) is Sequentially Phosphorylated by Conventional, Novel and Atypical Isotypes of Protein Kinase C

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The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes

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The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization

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Cloning and molecular characterization of the murine macrophage "68-kDa" protein kinase C substrate and its regulation by bacterial lipopolysaccharide.

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Involvement of Rho-kinase in inflammatory and neuropathic pain through phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS)

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Diacylglycerol Kinases as Emerging Potential Drug Targets for a Variety of Diseases

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The Myristoyl Moiety of Myristoylated Alanine-rich C Kinase Substrate (MARCKS) and MARCKS-related Protein Is Embedded in the Membrane

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Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation*

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Molecular cloning and characterization of the acidic 80-kDa protein kinase C substrate from rat brain. Identification as a glycoprotein.

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MARCKS modulates radial progenitor placement, proliferation and organization in the developing cerebral cortex

Weimer, J. M., Yokota, Y., Stanco, A., Stumpo, D. J., Blackshear, P. J., & Anton, E. S. (2009) · Development · doi:10.1242/dev.036616 · Cited by 74 · see citing works

X MARCKS the spot: myristoylated alanine-rich C kinase substrate in neuronal function and disease

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Novel Therapies to Inhibit Mucus Synthesis and Secretion in Airway Hypersecretory Diseases

Ha, E. V. S., & Rogers, D. F. (2015) · Pharmacology · doi:10.1159/000442794 · Cited by 73 · see citing works

Quantitative Tissue Proteomics Analysis Reveals Versican as Potential Biomarker for Early-Stage Hepatocellular Carcinoma

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Targeting Myristoylated Alanine-Rich C Kinase Substrate Phosphorylation Site Domain in Lung Cancer. Mechanisms and Therapeutic Implications

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Effect of reduced myristoylated alanine-rich C kinase substrate expression on hippocampal mossy fiber development and spatial learning in mutant mice: Transgenic rescue and interactions with gene background

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Myristoylated alanine‐rich C kinase substrate phosphorylation promotes cholangiocarcinoma cell migration and metastasis via the protein kinase C‐dependent pathway

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Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Protein Regulation of Human Neutrophil Migration

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SEQUENCES OF INTEREST: Molecular Cloning, Sequence, and Expression of a cDNA Encoding the Chicken Myristoylated Alanine-Rich C Kinase Substrate (MARCKS)

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Insulin activation of protein kinase C: a reassessment

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Comprehensive investigation of CASK mutations and other genetic etiologies in 41 patients with intellectual disability and microcephaly with pontine and cerebellar hypoplasia (MICPCH)

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Secretome protein signature of human pancreatic cancer stem-like cells

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MARCKS Regulates Growth and Radiation Sensitivity and Is a Novel Prognostic Factor for Glioma

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Protein kinase C activation potently down‐regulates the expression of its major substrate, 80K, in Swiss 3T3 cells.

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Reinduction of ErbB2 in astrocytes promotes radial glial progenitor identity in adult cerebral cortexPreprint

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Role of protein kinase C isoforms in bile formation and cholestasis

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Affinity purification and characterization of myristoylated alanine-rich protein kinase C substrate (MARCKS) from bovine brain. Comparison of the cytoplasmic and the membrane-bound forms.

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A Peptide Against the N-Terminus of Myristoylated Alanine-Rich C Kinase Substrate Inhibits Degranulation of Human Leukocytes In Vitro

Takashi, S., Park, J., Fang, S. J., Koyama, S., Parikh, I., & Adler, K. B. (2006) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0030rc · Cited by 59 · see citing works

Demyristoylation of the major substrate of protein kinase C (MARCKS) by the cytoplasmic fraction of brain synaptosomes.

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Involvement of PKCδ and PKD in pulmonary microvascular endothelial cell hyperpermeability

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The bi-directional translocation of MARCKS between membrane and cytosol regulates integrin-mediated muscle cell spreading

Disatnik, M., Boutet, S. C., Pacio, W., Chan, A. Y., Ross, L. B., Lee, C. H., & Rando, T. A. (2004) · Journal of Cell Science · doi:10.1242/jcs.01309 · Cited by 55 · see citing works

Elevated MARCKS phosphorylation contributes to unresponsiveness of breast cancer to paclitaxel treatment

Chen, C., Cheng, C.-T., Yuan, Y., Zhai, J., Arif, M., Fong, L. W. R., Wu, R., & Ann, D. K. (2015) · Oncotarget · doi:10.18632/oncotarget.3827 · Cited by 50 · see citing works

Deoxycholic acid activates protein kinase C and phospholipase C via increased Ca2+ entry at plasma membrane

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PhosphoMARCKS drives motility of mouse melanoma cells

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Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP)

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Directed migration of mouse macrophages in vitro involves myristoylated alanine-rich C-kinase substrate (MARCKS) protein

Green, T. D., Park, J., Yin, Q., Fang, S. J., Crews, A. L., Jones, S. L., & Adler, K. B. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.1211604 · Cited by 48 · see citing works

Myristoylated Alanine-Rich protein Kinase C Substrate (MARCKS) expression modulates the metastatic phenotype in human and murine colon carcinoma in vitro and in vivo

Rombouts, K., Carloni, V., Mello, T., Omenetti, S., Galastri, S., Madiai, S., Galli, A., & Pinzani, M. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.01.040 · Cited by 47 · see citing works

The expression of 80K/MARCKS, a major substrate of protein kinase C (PKC), is down-regulated through both PKC-dependent and -independent pathways. Effects of bombesin, platelet-derived growth factor, and cAMP.

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Upregulation of MARCKS in kidney cancer and its potential as a therapeutic target

Chen, C., Fong, L. W. R., Yu, E., Wu, R., Trott, J. F., & Weiss, R. H. (2017) · Oncogene · doi:10.1038/onc.2016.510 · Cited by 46 · see citing works

MicroRNA-21 Limits Uptake of Listeria monocytogenes by Macrophages to Reduce the Intracellular Niche and Control Infection

Johnston, D. G. W., Kearney, J., Zasłona, Z., Williams, M. A., O'Neill, L. A. J., & Corr, S. C. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00201 · Cited by 44 · see citing works

Interaction between Actin and the Effector Peptide of MARCKS-related Protein

Wohnsland, F., Schmitz, A. A. P., Steinmetz, M. O., Aebi, U., & Vergères, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910298199 · Cited by 44 · see citing works

MARCKS: a case of molecular exaptation?

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Developmental expression of MARCKS and protein kinase C in mice in relation to the exencephaly resulting from MARCKS deficiency

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MARCKS, a major protein kinase C substrate, assumes non‐helical conformations both in solution and in complex with Ca2+‐calmodulin

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MicroRNA-142-3p attenuates hepatic ischemia/reperfusion injury via targeting of myristoylated alanine-rich C-kinase substrate

Li, Y., Gao, M., Xu, L., Yin, L., Qi, Y., & Peng, J. (2020) · Pharmacological Research · doi:10.1016/j.phrs.2020.104783 · Cited by 40 · see citing works

Myristoylated alanine-rich C kinase substrate (MARCKS) regulates the expression of proinflammatory cytokines in macrophages through activation of p38/JNK MAPK and NF-κB

Lee, S., Suk, K., & Lee, W. (2015) · Cellular Immunology · doi:10.1016/j.cellimm.2015.04.004 · Cited by 39 · see citing works

Characterization of the Targeting, Binding, and Phosphorylation Site Domains of an A Kinase Anchor Protein and a Myristoylated Alanine-rich C Kinase Substrate-like Analog That Are Encoded by a Single Gene

Rossi, E. A., Li, Z., Feng, H., & Rubin, C. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.38.27201 · Cited by 39 · see citing works

Myristoylated Alanine‐Rich Protein Kinase Substrate (MARCKS) Regulates Small GTPase Rac1 and Cdc42 Activity and Is a Critical Mediator of Vascular Smooth Muscle Cell Migration in Intimal Hyperplasia Formation

Yu, D., Makkar, G., Strickland, D. K., Blanpied, T. A., Stumpo, D. J., Blackshear, P. J., Sarkar, R., & Monahan, T. S. (2015) · Journal of the American Heart Association · doi:10.1161/jaha.115.002255 · Cited by 39 · see citing works

Myristoylated Alanine-rich C Kinase Substrate-mediated Neurotensin Release via Protein Kinase C-δ Downstream of the Rho/ROK Pathway

Li, J., O’Connor, K. L., Greeley, G. H., Blackshear, P. J., Townsend, C. M., & Evers, B. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409431200 · Cited by 38 · see citing works

Characterization and purification of a protein kinase C substrate in human B cells. Identification as lymphocyte-specific protein 1 (LSP1)

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A Myristoylated Alanine-Rich C Kinase Substrate–Related Peptide Suppresses Cytokine mRNA and Protein Expression in LPS-Activated Canine Neutrophils

Li, J., D’Annibale, M. A., Adler, K. B., Fang, S. J., Yin, Q., Birkenheuer, A. J., Levy, M. G., Jones, S. L., Sung, E. J., Hawkins, E. C., et al. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0278oc · Cited by 37 · see citing works

Promoter Sequence, Expression, and Fine Chromosomal Mapping of the Human Gene (MLP) Encoding the MARCKS-like Protein: Identification of Neighboring and Linked Polymorphic Loci forMLPandMACSand Use in the Evaluation of Human Neural Tube Defects

Stumpo, D. J., Eddy, R. L., Haley, L. L., Sait, S. N. J., Shows, T. B., Lai, W. S., Young, W. S., Speer, M. C., Dehejia, A. M., Polymeropoulos, M. H., et al. (1998) · Genomics · doi:10.1006/geno.1998.5247 · Cited by 36 · see citing works

MicroRNA 429 Regulates Mucin Gene Expression and Secretion in Murine Model of Colitis

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Evidence for a non-myristoylated pool of the 80 kDa protein kinase C substrate of rat brain

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Myristoylated alanine-rich C-kinase substrate as a prognostic biomarker in human primary lung squamous cell carcinoma

Hanada, S., Kakehashi, A., Nishiyama, N., Wei, M., Yamano, S., Chung, K., Komatsu, H., Inoue, H., Suehiro, S., & Wanibuchi, H. (2013) · Cancer Biomarkers · doi:10.3233/cbm-130354 · Cited by 34 · see citing works

Overexpression of the myristoylated alanine-rich C kinase substrate in human choroidal melanoma cells affects cell proliferation.

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MARCKS protein overexpression in inflammatory breast cancer

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In Vitro Neutrophil Migration Requires Protein Kinase C-Delta (δ-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation

Sheats, M. K., Sung, E. J., Adler, K. B., & Jones, S. L. (2014) · Inflammation · doi:10.1007/s10753-014-0078-9 · Cited by 33 · see citing works

Altered prefrontal cortical MARCKS and PPP1R9A mRNA expression in schizophrenia and bipolar disorder

Konopaske, G. T., Subburaju, S., Coyle, J. T., & Benes, F. M. (2015) · Schizophrenia Research · doi:10.1016/j.schres.2015.02.005 · Cited by 33 · see citing works

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

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Diacylglycerol kinase ζ: At the crossroads of lipid signaling and protein complex organization

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Role of MARCKS in regulating endothelial cell proliferation

Zhao, Y., Neltner, B. S., & Davis, H. W. (2000) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.2000.279.5.c1611 · Cited by 32 · see citing works

Inhibition of myristoylated alanine-rich C kinase substrate (MARCKS) protein inhibits ozone-induced airway neutrophilia and inflammation

Damera, G., Jester, W. F., Jiang, M., Zhao, H., Fogle, H. W., Mittelman, M. A., Haczku, A., Murphy, E., Parikh, I., & Panettieri, R. A. (2010) · Experimental Lung Research · doi:10.3109/01902140903131200 · Cited by 32 · see citing works

Protein Kinase C-mediated Phosphorylation of the Myristoylated Alanine-rich C-kinase Substrate Protects It from Specific Proteolytic Cleavage

Spizz, G., & Blackshear, P. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.553 · Cited by 31 · see citing works

Phosphorylation of MARCKS (80‐KDA) protein, a major substrate for protein kinase C in oligodendroglial progenitors

Bhat, N. R. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490300222 · Cited by 30 · see citing works

Tob-Mediated Cross-Talk between MARCKS Phosphorylation and ErbB-2 Activation

Cho, S. J., La, M., Ahn, J. K., Meadows, G. G., & Joe, C. O. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.4773 · Cited by 29 · see citing works

The Effector Domain of MARCKS Is a Nuclear Localization Signal that Regulates Cellular PIP2 Levels and Nuclear PIP2 Localization

Rohrbach, T. D., Shah, N., Jackson, W. P., Feeney, E. V., Scanlon, S. A., Gish, R., Khodadadi, R. B., Hyde, S. O., Hicks, P. H., Anderson, J. C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140870 · Cited by 28 · see citing works

The cloning and developmental regulation of murine diacylglycerol kinase ζ

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A possible role of myristoylated alanine-rich C kinase substrate in endocytic pathway of Alzheimer’s disease

Su, R., Han, Z.-Y., Fan, J.-P., & Zhang, Y.-L. (2010) · Neuroscience Bulletin · doi:10.1007/s12264-010-0131-0 · Cited by 27 · see citing works

Involvement of inhibition of RhoA/Rho kinase signaling in simvastatin-induced amelioration of neuropathic pain

Ohsawa, M., Ishikura, K., Mutoh, J., & Hisa, H. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.07.029 · Cited by 26 · see citing works

MARCKS promotes invasion and is associated with biochemical recurrence in prostate cancer

Dorris, E., O’Neill, A., Hanrahan, K., Treacy, A. D., & Watson, R. W. G. (2017) · Oncotarget · doi:10.18632/oncotarget.18894 · Cited by 26 · see citing works

Transformed 3T3 cells have reduced levels and altered subcellular distribution of the major PKC substrate protein marcks

Reed, J. C., Rapp, U. R., & Cuddy, M. (1991) · Cellular Signalling · doi:10.1016/0898-6568(91)90033-q · Cited by 25 · see citing works

MARCKS as a Negative Regulator of Lipopolysaccharide Signaling

Manček‐Keber, M., Benčina, M., Japelj, B., Panter, G., Andrä, J., Brandenburg, K., Triantafilou, M., Triantafilou, K., & Jerala, R. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1003605 · Cited by 24 · see citing works

PKC phosphorylates MARCKS Ser159 not only directly but also through RhoA/ROCK

Tanabe, A., Kamisuki, Y., Hidaka, H., Suzuki, M., Negishi, M., & Takuwa, Y. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.04.082 · Cited by 23 · see citing works

Histone deacetylase 1 is increased in rheumatoid arthritis synovium and promotes synovial cell hyperplasia and synovial inflammation in the collagen-induced arthritis mouse model via the microRNA-124-dependent MARCKS-JAK/STAT axis

Meng, Q., Pan, B., & Sheng, P. (2021) · Clinical and Experimental Rheumatology · doi:10.55563/clinexprheumatol/1xsigp · Cited by 23 · see citing works

MARCKS regulates tonic and chronic active B cell receptor signaling

Xu, C., Fang, Y., Yang, Z., Jing, Y., Zhang, Y., Liu, C., & Liu, W. (2018) · Leukemia · doi:10.1038/s41375-018-0244-4 · Cited by 22 · see citing works

Chromosomal mapping of the human (MACS) and mouse (Macs) genes encoding the MARCKS protein

Blackshear, P. J., Tuttle, J. S., Oakey, R. J., Seldin, M. F., Chery, M., Philippe, C., & Stumpo, D. J. (1992) · Genomics · doi:10.1016/s0888-7543(05)80300-3 · Cited by 22 · see citing works

Suppression of the lipopolysaccharide-induced expression of MARCKS-related protein (MRP) affects transmigration in activated RAW264.7 cells

Chun, K., Bae, E. M., Kim, J., Suk, K., & Lee, W. (2009) · Cellular Immunology · doi:10.1016/j.cellimm.2009.01.011 · Cited by 20 · see citing works

A Novel Predictor of Cancer Malignancy: Up-regulation of Myristoylated Alanine-Rich C Kinase Substrate Phosphorylation in Lung Cancer

Chen, C., Chiu, C.-L., Adler, K. B., & Wu, R. (2014) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201401-0053le · Cited by 20 · see citing works

miR-34c-3p acts as a tumor suppressor gene in osteosarcoma by targeting MARCKS

Liu, H., Su, P., Zhi, L., & Zhao, K. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6108 · Cited by 19 · see citing works

Mapping the interface between calmodulin and MARCKS-related protein by fluorescence spectroscopy

Ulrich, A., Schmitz, A. A. P., Braun, T., Yuan, T., Vogel, H. J., & Vergères, G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.090500397 · Cited by 19 · see citing works

Peptides derived from MARCKS block coagulation complex assembly on phosphatidylserine

Kastelowitz, N., Tamura, R., Onasoga, A. A., Stalker, T. J., White, O. R., Brown, P. D. N., Brodsky, G. L., Brass, L. F., Branchford, B. R., Paola, J. D., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04494-y · Cited by 19 · see citing works

Targeting the phosphorylation site of myristoylated alanine‐rich C kinase substrate alleviates symptoms in a murine model of steroid‐resistant asthma

Wang, C., Lin, Y., Chang, B., Chen, C., Wu, R., & Lee, C. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14596 · Cited by 19 · see citing works

Functional Diversification of the Four MARCKS Family Members in Zebrafish Neural Development

Prieto, D., & Zolessi, F. R. (2016) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.22691 · Cited by 18 · see citing works

The Role of Myristoylated Protein Kinase C Substrates in Intracellular Signaling Pathways in Macrophages

Aderem, A. A. (1992) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-77377-8_7 · Cited by 18 · see citing works

MARCKS phosphorylation is modulated by a peptide mimetic of MARCKS effector domain leading to increased radiation sensitivity in lung cancer cell lines

Rohrbach, T. D., Jones, R. B., Hicks, P. H., Weaver, A. N., Cooper, T. S., Eustace, N. J., Yang, E. S.-H., Jarboe, J. S., Anderson, J. C., & Willey, C. D. (2016) · Oncology Letters · doi:10.3892/ol.2016.5550 · Cited by 16 · see citing works

Lymphocyte modulation by tofacitinib in patients with rheumatoid arthritis

Isailovic, N., Ceribelli, A., Cincinelli, G., Vecellio, M. L., Guidelli, G. M., Caprioli, M., Luciano, N., Motta, F., Selmi, C. F., & Santis, M. D. (2021) · Clinical & Experimental Immunology · doi:10.1111/cei.13609 · Cited by 13 · see citing works

Stromal Expression of MARCKS Protein in Ovarian Carcinomas Has Unfavorable Prognostic Value

Doghri, R., Manai, M., Finetti, P., Driss, M., Agavnian, E., Lopez, M., Elghardallou, M., Charafe‐Jauffret, E., Manaï, M., Chaffanet, M., et al. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms19010041 · Cited by 12 · see citing works

Myristoylated alanine-rich C-kinase substrate effector domain phosphorylation regulates the growth and radiation sensitization of glioblastoma

Eustace, N. J., Anderson, J. C., Langford, C. P., Trummell, H. Q., Hicks, P. H., Jarboe, J. S., Mobley, J. A., Hjelmeland, A. B., Hackney, J. R., Pedersen, R. T., et al. (2019) · International Journal of Oncology · doi:10.3892/ijo.2019.4766 · Cited by 10 · see citing works

Ser46-Phosphorylated MARCKS Is a Marker of Neurite Degeneration at the Pre-aggregation Stage in PD/DLB Pathology

Fujita, K., Homma, H., Kondo, K., Ikuno, M., Yamakado, H., Tagawa, K., Murayama, S., Takahashi, R., & Okazawa, H. (2018) · eNeuro · doi:10.1523/eneuro.0217-18.2018 · Cited by 7 · see citing works

Presence of Conserved Domains in the C-Terminus of MARCKS, a Major In Vivo Substrate of Protein Kinase C: Application of Ion Trap Mass Spectrometry to the Elucidation of Protein Structures

Yamauchi, E., Kiyonami, R., Kanai, M., & Taniguchit, H. (1998) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022002 · Cited by 7 · see citing works

Mechanism of inhibition of taurolithocholate‐induced retrieval of plasma membrane MRP 2 by cyclic AMP and tauroursodeoxycholate

Park, S. W., Webster, C. R. L., & Anwer, M. S. (2017) · Physiological Reports · doi:10.14814/phy2.13529 · Cited by 3 · see citing works

CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02019-6 · Cited by 48 · see citing works

Profiling Phosphoproteome Landscape in Circulating Extracellular Vesicles from Microliters of Biofluids through Functionally Tunable Paramagnetic Separation

Sun, J., Li, Q. X., Ding, Y., Wei, D., Hadisurya, M., Luo, Z., Gu, Z., Chen, B., & Tao, W. A. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202305668 · Cited by 30 · see citing works

The Role of MARCKS in Metastasis and Treatment Resistance of Solid Tumors

Chiu, C.-L., Zhao, H., Chen, C., Wu, R., & Brooks, J. D. (2022) · Cancers · doi:10.3390/cancers14194925 · Cited by 28 · see citing works

Myristoylated, alanine-rich C-kinase substrate (MARCKS) regulates toll-like receptor 4 signaling in macrophages

Issara-Amphorn, J., Sjoelund, V. H., Smelkinson, M. G., Montalvo, S., Yoon, S. H., Manes, N. P., & Nita‐Lazar, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-46266-x · Cited by 18 · see citing works

Investigating endogenous immune-mediated monocyte memory in rheumatoid arthritis

Marzeda, A. M., Schwenzer, A., Didov, B. S., Woolcock, K., Richard, J.-B., Jennings, L. K., Julé, A. M., Yang, N., Davidson, S., Sansom, S. C., et al. (2025) · Annals of the Rheumatic Diseases · doi:10.1016/j.ard.2025.03.016 · Cited by 15 · see citing works

Superior antitumor immune response achieved with proton over photon immunoradiotherapy is amplified by the nanoradioenhancer NBTXR3

Hu, Y. Y., Paris, S., Sahoo, N., Wang, Q., Wang, Q., Barsoumian, H. B., Huang, A., SILVA, J. D., Bienassis, C., Leyton, C. S. K., et al. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02855-0 · Cited by 14 · see citing works

Nuclear transport of phosphorylated LanCL2 promotes invadopodia formation and tumor progression of glioblastoma by activating STAT3/Cortactin signaling

Zhao, H., Liu, Y., Wang, J., Wu, C.-P., Zhou, X., Cai, L.-R., Liu, J., Liu, X., Xu, Y., Li, W.-P., et al. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.03.007 · Cited by 13 · see citing works

Unraveling sex differences in Alzheimer's disease and related endophenotypes with brain proteomes

Mei, Z., Liu, J., Bennett, D. A., Seyfried, N., Wingo, A. P., & Wingo, T. S. (2025) · Alzheimer's & Dementia · doi:10.1002/alz.70206 · Cited by 11 · see citing works

Advancements in the study of synaptic plasticity and mitochondrial autophagy relationship

Zhu, Y., Hui, Q., Zhang, Z., Fu, H., Qin, Y., Zhao, Q., Li, Q., Zhang, J., Guo, L., He, W., et al. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25309 · Cited by 11 · see citing works

MARCKS as a Potential Therapeutic Target in Inflammatory Breast Cancer

Manai, M., ELBini-Dhouib, I., Finetti, P., Bichiou, H., Reduzzi, C., Aissaoui, D., Hamida, N. B., Agavnian, E., Srairi‐Abid, N., Lopez, M., et al. (2022) · Cells · doi:10.3390/cells11182926 · Cited by 11 · see citing works

Allergen-induced activation of epithelial P2Y2 receptors promotes adenosine triphosphate exocytosis and type 2 immunity in airways

Srisomboon, Y., Tojima, I., Iijima, K., Kita, H., & O’Grady, S. M. (2025) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2025.01.019 · Cited by 10 · see citing works

Circulating extracellular vesicle-derived MARCKSL1 is a potential diagnostic non-invasive biomarker in metastatic colorectal cancer patients

Rong, W., Shao, S., Pu, Y., Ji, Q., & Zhu, H. (2023) · Scientific Reports · doi:10.1038/s41598-023-37008-0 · Cited by 9 · see citing works

D-Cysteine Activates Chaperone-Mediated Autophagy in Cerebellar Purkinje Cells via the Generation of Hydrogen Sulfide and Nrf2 Activation

Ueda, E., Ohta, T., Konno, A., Hirai, H., Kurauchi, Y., Katsuki, H., & Seki, T. (2022) · Cells · doi:10.3390/cells11071230 · Cited by 9 · see citing works

MARCKS Is an Essential Regulator of Reactive Oxygen Species Production in the Monocytic Cell Type

Huber, R., Diekmann, M., Hoffmeister, L., Kühl, F., Welz, B., & Brand, K. (2022) · Antioxidants · doi:10.3390/antiox11081600 · Cited by 9 · see citing works

Binding-induced lipid domains: Peptide-membrane interactions with PIP2 and PS

Al-Mualem, Z. A., Chen, X., Shafieenezhad, A., Senning, E. N., & Baiz, C. R. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.12.019 · Cited by 8 · see citing works

NAC couples protein synthesis with nascent polypeptide myristoylation on the ribosome

Zdancewicz, S., Maldosevic, E., Malezyna, K., & Jomaa, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00548-4 · Cited by 7 · see citing works

PIP2 Interacts Electrostatically with MARCKS-like Protein-1 and ENaC in Renal Epithelial Cells

Yue, Q., Al-Khalili, O. K., Moseley, A. S., Yoshigi, M., Wynne, B. M., Ma, H., & Eaton, D. C. (2022) · Biology · doi:10.3390/biology11121694 · Cited by 7 · see citing works

MARCKS and PI(4,5)P2 reciprocally regulate actin-based dendritic spine morphology

Calabrese, B., & Halpain, S. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-09-0370 · Cited by 7 · see citing works

Regulation of Adaptive Immunity by Lipid Post-translational Modifications

Mattingly, J. R., Wu, A. Y., & York, A. G. (2025) · Immune Network · doi:10.4110/in.2025.25.e11 · Cited by 5 · see citing works

Neurotrophic factor biomarkers for ischemic stroke diagnosis and mechanistic insights

Xu, L., Wang, P., Yang, L., Liu, Y., Li, X., Yin, Y., & Lan, C. (2025) · Scientific Reports · doi:10.1038/s41598-025-86935-7 · Cited by 5 · see citing works

Human nonunion tissues display differential gene expression in comparison to physiological fracture callus

Salichos, L., Thayavally, R., Kloen, P., & Hadjiargyrou, M. (2024) · Bone · doi:10.1016/j.bone.2024.117091 · Cited by 5 · see citing works

Stretch triggers microtubule stabilization and MARCKS-dependent membrane incorporation in the shaft of embryonic axons

Sousa, S., Aroso, M., Bessa, R., Veríssimo, E., da Silva, T. F., Lopes, C. D. F., Brites, P., Vieira, J., Vieira, C. P., Aguiar, P., et al. (2024) · Current Biology · doi:10.1016/j.cub.2024.08.018 · Cited by 5 · see citing works

Proteomic Mapping of Hippocampal Pathways Involved in Lead (Pb)–Induced Neurotoxicity

Matte, K., Pingle, S. D., Ramaiah, M. K., Tumane, R., & Sherekar, P. (2026) · Journal of Applied Toxicology · doi:10.1002/jat.70123 · Cited by 4 · see citing works

Profiling Phosphoproteome Landscape in Circulating Extracellular Vesicles from Microliters of Biofluids through Functionally Tunable Paramagnetic Separation

Sun, J., Li, Q. X., Ding, Y., Dong, W., Hadisurya, M., Luo, Z., Gu, Z., Chen, B., & Tao, W. A. (2023) · Angewandte Chemie · doi:10.1002/ange.202305668 · Cited by 4 · see citing works

MARCKS Effector Domain, a reversible lipid ligand, illuminates late stages of membrane fusion

Orr, A. S., & Wickner, W. T. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-06-0228 · Cited by 4 · see citing works

Marcks overexpression in retinal ganglion cells promotes optic nerve regeneration

Peng, X.-Q., Li, Y.-Z., Gu, C., He, X., Li, C.-P., Yong-quan, S., Du, H., Teng, Z., & Liu, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07281-6 · Cited by 5 · see citing works

Identification of Feature Genes of a Novel Neural Network Model for Bladder Cancer

Zhang, Y., Hua, S., Jiang, Q., Xie, Z., Wu, L., Wang, X., Shi, F., Dong, S., & Jiang, J. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.912171 · Cited by 4 · see citing works

Single-cell sequencing reveals cell heterogeneity and aberrantly activated pathways associated with microvascular invasion in hepatocellular carcinoma

Cui, J., Zeng, F., Tang, M., & Yin, S. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1449624 · Cited by 3 · see citing works

Nanotopography-Mediated Mechanotransduction Enhances hBMSCs Adhesion on TiO2 Nanotubes

Xiong, C., Feng, H., Lu, L., Jing, Z., Wang, Y., Yang, Y., Meng, D., Zhang, Y., Li, W., & Cai, H. (2026) · Journal of Functional Biomaterials · doi:10.3390/jfb17040200 · Cited by 3 · see citing works

Single-cell sequencing of the vermiform appendix during development identifies transcriptional relationships with appendicitis in preschool children

Meng, L., Yang, Y., He, S., Chen, H., Zhan, Y., Yang, R., Li, Z., Zhu, J., Zhou, J., Li, Y., et al. (2024) · BMC Medicine · doi:10.1186/s12916-024-03611-9 · Cited by 3 · see citing works

Detection of Immune Microenvironment Changes and Immune‐Related Regulators in Langerhans Cell Histiocytosis Bone Metastasis

Lin, J., Tang, H., Xu, Z., & Zeng, R. (2023) · BioMed Research International · doi:10.1155/2023/1447435 · Cited by 3 · see citing works

MARCKS is a New Prognostic Biomarker in Hepatocellular Carcinoma

Lu, H., Zhao, R., Qin, Q., Tang, L., Ma, G., He, B., Liang, J., Wei, L., Wang, X., Bie, Q., et al. (2023) · International Journal of General Medicine · doi:10.2147/ijgm.s408651 · Cited by 3 · see citing works

Role for the PIP2‐binding protein myristoylated alanine‐rich C‐kinase substrate in vascular tissue: A novel therapeutic target for cardiovascular disease

Albert, A. P., Jahan, K. S., Greenberg, H. Z. E., & Shamsaldeen, Y. A. (2024) · Journal of Cell Communication and Signaling · doi:10.1002/ccs3.12052 · Cited by 3 · see citing works

Activation of Marck-like Genes and Proteins During Initial Phases of Regeneration in the Amputated Tail and Limb of the Lizard Podarcis muralis

Alibardi, L. (2025) · Journal of Developmental Biology · doi:10.3390/jdb13020012 · Cited by 3 · see citing works

MARCKS N-terminal sequence-derived inhibitor peptides impair monocytic ROS production and migration via MARCKS-independent effects

Kühl, F., Kopper, J. L., Wriede, L. S., Welz, B., Lichtinghagen, R., Brand, K., & Huber, R. (2025) · Molecular Biology Reports · doi:10.1007/s11033-025-11027-8 · Cited by 3 · see citing works

Chemical Biology Drives Membrane-Curvature-Sensing Peptide Probes for Extracellular Vesicle Capture and Applications

Sun, G., & Yin, H. H. (2026) · Biochemistry · doi:10.1021/acs.biochem.5c00700 · Cited by 2 · see citing works

Anabolic steroids induced changes at the level of protein expression: Effects of prolonged administration of testosterone and nandrolone to pigs

Gebauer, J., Hodkovicová, N., Tošnerová, K., Skoupá, K., Bátik, A., Bartejsova, I., Charvatova, M., Levá, L., Jarošová, R., Sládek, Z., et al. (2024) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2024.104422 · Cited by 2 · see citing works

Investigation of Genetic Changes in Three Families with Bipolar Disease

Geniş, E. Ç., Erdoğan, M. Ö., Çam, F. S., Aydemır, Ö., Akin, F., Çelebi, H. B. G., & Solak, M. (2024) · Molecular Syndromology · doi:10.1159/000539115 · Cited by 2 · see citing works

A peptide against the N-terminus of myristoylated alanine-rich C kinase substrate promotes neuronal differentiation in SH-SY5Y human neuroblastoma cells

Ferdous, J., Naitou, K., & Shiraishi, M. (2024) · Journal of Veterinary Medical Science · doi:10.1292/jvms.24-0276 · Cited by 2 · see citing works

The delayed effect of the neuroprotector fabomotizole on the brain proteome in rats with the rotenone model of parkinsonism

Бунеева, О. А., Капица, И. Г., Zavialova, M. G., Kaloshina, S. A., Zgoda, V. G., & Medvedev, A. E. (2025) · Biomeditsinskaya Khimiya · doi:10.18097/pbmcr1586 · Cited by 1 · see citing works

Edited HSPCs rescue frataxin deficiency and inflammation-driven multisystemic pathology in Friedreich’s ataxia mice

Sivakumar, A., Corl, A. N., Muñoz, K. J., Arumugam, S., Gunes, B. B., Solis, A. B., Murthy, R., El-Hachem, L. R., Pizzo, D. P., Blair, I. A., et al. (2026) · Journal of Clinical Investigation · doi:10.1172/jci209546 · Cited by 1 · see citing works

Combining proteomics and Phosphoproteomics to investigate radiation-induced rectal fibrosis in rats and the effects of pSTAT3 inhibitor S3I-201 on human intestinal fibroblasts

Pan, H., Zhao, Z., Zhu, Y., Gao, Y., Ruan, H., Huang, Y., Chi, P., & Huang, S. (2024) · Journal of Proteomics · doi:10.1016/j.jprot.2024.105287 · Cited by 1 · see citing works

Immunolocalization of MARCKS-like protein during early stages of tail fin regeneration in the goldfish supports a role in triggering regeneration

Alibardi, L. (2025) · Zoomorphology · doi:10.1007/s00435-025-00742-2 · Cited by 1 · see citing works

Proteomic profiling of macrophages: effects of inflammatory activation and anti-inflammatory treatment with IBD therapeutics

Lichtner, S., Schunck, K., Frey, J., Osti, J., Dannheimer, S., Schnur, S., Lehr, C., Schneider, M., & Hittinger, M. (2025) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2025.114869 · Cited by 1 · see citing works

Myristoylated alanine rich C kinase substrate/Activated Cdc42-associated kinase 1 regulates cortactin to promote neutrophil elastase-induced mucin secretion in airway epithelial cellsPreprint

Zhong, Y., He, M., Perelman, J. M., Кolosov, V. P., Li, Q., & Zhou, X. (2022) · Research Square · doi:10.21203/rs.3.rs-2091761/v1

A multi-network approach to Alzheimer’s Disease gene prioritization complements cis -regulatory prioritization with molecular quantitative trait lociPreprint

Brabec, J. L., Lara, M. K., Tyler, A. L., & Mahoney, J. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.03.539189

CRISPR activation screen uncovers MARCKSL1 as a gauge for extracellular vesicle secretion

Zhong, Y., George, A. E., Koning, R. I., Liv, N., de Heus, C., Tjokrodirijo, R. T. N., Messchendorp, M., Akkermans, J. J. L. L., Cabukusta, B., Janssen, G. M. C., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.117744

HER2 Interactome Profiling Reveals MARCKS as a Candidate Marker Associated with Aggressive Breast Cancer

Yokoyama, A., Sawatsubashi, S., Ebata, A., Miki, Y., Otsubo, Y., & Suzuki, T. (2025) · Cancers · doi:10.3390/cancers17172882

A MARCKS Effector Domain‐Derived Cytotoxic Peptide Induces Acute Tumor Cell Death

Wang, Y., Qiu, Y., Liu, D., Zhang, H., & Xu, C. (2025) · Cell Biochemistry and Function · doi:10.1002/cbf.70139

MARCKS‐Like Protein Immunolocalization in Healing Appendages of Amphibians Suggests Its Involvement in Regeneration

Alibardi, L. (2025) · Journal of Experimental Zoology Part B Molecular and Developmental Evolution · doi:10.1002/jez.b.70006

Additional file 1 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25844356

Additional file 7 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26721480

Additional file 2 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.25844516

Additional file 6 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26721477

Additional file 3 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26721468

Additional file 8 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26721483

Additional file 5 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26721474

Additional file 4 of CircTRIM1 encodes TRIM1-269aa to promote chemoresistance and metastasis of TNBC via enhancing CaM-dependent MARCKS translocation and PI3K/AKT/mTOR activation

Li, Y., Wang, Z. H., Yang, J., Sun, Y., He, Y., Wang, Y., Chen, X., Liang, Y., Zhang, N., Wang, X., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26721471

Bioinformatics characterization and tissue-specific expression of MARCKS and MLP genes in the regenerating salamander Cynops orientalis

Shui, L., Feng, Y., & Liu, W.-H. (2026) · Molecular Genetics and Genomics · doi:10.1007/s00438-026-02361-y

The transmembrane IL-15 isoform expressed on human melanoma cells triggers modulatory effects on tumor progression upon stimulation with the soluble IL-15Rα chain

Forcelloni, S., Giron‐Michel, J., Boccio, P. D., Cufaro, M. C., Sebastiano, A. D., Mariotti, F. R., Ciancaglini, C., Chouaı̈b, S., Padelli, M., Vespa, S., et al. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1798481

Identification of MARCKSL1 as an independent prognostic biomarker and analysis of its potential regulatory network in hepatocellular carcinoma

Li, H., Zhang, W., Zhao, J., Ke, T., Shen, P., Lin, T., Zhan, N., Zhan, Y., & Yang, X. (2026) · Discover Oncology · doi:10.1007/s12672-026-05217-4

Protein kinase Cη–MARCKS axis associations with epithelial barrier disturbance and inflammatory readouts in ulcerative colitis

Liu, Z., Shang, Y., Zhang, X., Han, X., Gao, F., & Chen, X. (2026) · Scientific Reports · doi:10.1038/s41598-026-61345-5

Multiomics combined with machine learning identifies cytoskeleton-related molecular signatures in peripheral immune cells of rheumatoid arthritis

Hu, B., Zhang, Q., Dai, Y., Tang, D., Zhu, T., Zheng, Z., Zhang, W., & Lu, Y. (2026) · European journal of medical research · doi:10.1186/s40001-026-04911-x

Actin Cytoskeleton Dysregulation Links Testicular and Sperm Dysfunction in Type 1 Diabetes

Ambruosi, M. R., Biasi, A., Boccella, S., Romdhani, I., Falvo, S., Guida, F., Maione, S., Minucci, S., & Venditti, M. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27167423

IL-9R/Arg1 pathway promotes polyamine metabolism in human airway macrophages

Zhang, W., Cheon, I. S., Pajulas, A., Sinn, A. L., Krishnan, M. S., Zhang, J., Abdelaal, A. M., Liu, X., Jackson, K. G., Zhang, J., et al. (2026) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2026.08.016

The influence of neuroprotector isatin on haloperidolinduced catalepsy and proteomic profile of mice brain

Бунеева, О. А., Капица, И. Г., Zavialova, M. G., Kaloshina, S. A., Zgoda, V. G., & Ae, M. (2026) · Biomeditsinskaya Khimiya · doi:10.18097/pbmcr1718

PM175 Matrix Metalloproteinase-9 Gene Promotor -1562 C/T Polymorphism and Ischemic Stroke in Tunisian Patients

Soualmia, H., Akrem, J., Midani, F., Mannai, R., Hentati, F., & Kharrat, M. (2016) · Global Heart · doi:10.1016/j.gheart.2016.03.345

Membrane Association of the Myristoylated Alanine-rich C Kinase Substrate (MARCKS) Protein.

Swierczynski, S. L., & Blackshear, P. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13436 · Cited by 100 · see citing works

Estrazione e rappresentazione della conoscenza nella bioinformatica

Baldacci, L. <. (2007) · PubMed · doi:10.6092/unibo/amsdottorato/139

Cross-talk unfolded: MARCKS proteins

Arbuzova, A., Schmitz, A. A. P., & Vergères, G. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3620001 · Cited by 323 · see citing works

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.

George, D. J., & Blackshear, P. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35845-9 · Cited by 62 · see citing works