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Cited by in CrossRef
For: Shiryaev A, Kostenko S, Dumitriu G, Moens U. Septin 8 is an interaction partner and in vitro substrate of MK5. World J Biol Chem 2012; 3(5): 98-109 [PMID: 22649572 DOI: 10.4331/wjbc.v3.i5.98]
URL: https://www.wjgnet.com/1949-8454/full/v3/i5/98.htm
Number Citing Articles
1
Joaquim Javary, Eugénie Goupil, Mathilde Soulez, Evgeny Kanshin, Antoine Bouchard, Ole‐Morten Seternes, Pierre Thibault, Jean‐Claude Labbé, Sylvain Meloche. Phosphoproteomic analysis identifies supervillin as an ERK3 substrate regulating cytokinesis and cell ploidyJournal of Cellular Physiology 2024; 239(3) doi: 10.1002/jcp.30938
2
Pramod Sahadevan, Bruce G. Allen. MK5: A novel regulator of cardiac fibroblast function?IUBMB Life 2017; 69(10): 785 doi: 10.1002/iub.1677
3
Bailey Werner, Smita Yadav. Phosphoregulation of the septin cytoskeleton in neuronal development and diseaseCytoskeleton 2023; 80(7-8): 275 doi: 10.1002/cm.21728
4
Chun‐Hsiang Lin, Yi‐Ru Shen, Han‐Yu Wang, Chi‐Wu Chiang, Chia‐Yih Wang, Pao‐Lin Kuo. Regulation of septin phosphorylation: SEPT12 phosphorylation in sperm septin assemblyCytoskeleton 2019; 76(1): 137 doi: 10.1002/cm.21491
5
Md Imtiaz Khalil, Vibha Singh, Judy King, Arrigo De Benedetti. TLK1‐mediated MK5‐S354 phosphorylation drives prostate cancer cell motility and may signify distinct pathologiesMolecular Oncology 2022; 16(13): 2537 doi: 10.1002/1878-0261.13183
6
Khushboo Sharma, Manoj B. Menon. Decoding post‐translational modifications of mammalian septinsCytoskeleton 2023; 80(7-8): 169 doi: 10.1002/cm.21747
7
Katarina Akhmetova, Maxim Balasov, Anton Svitin, Elena Chesnokova, Matthew Renfrow, Igor Chesnokov. Phosphorylation of Pnut in the Early Stages ofDrosophilaEmbryo Development Affects Association of the Septin Complex with the Membrane and Is Important for ViabilityG3 Genes|Genomes|Genetics 2018; 8(1): 27 doi: 10.1534/g3.117.300186
8
Manoj B. Menon. Encyclopedia of Signaling Molecules2018; : 4875 doi: 10.1007/978-3-319-67199-4_101986
9
Ugo Moens, Sergiy Kostenko, Baldur Sveinbjørnsson. The Role of Mitogen-Activated Protein Kinase-Activated Protein Kinases (MAPKAPKs) in InflammationGenes 2013; 4(2): 101 doi: 10.3390/genes4020101
10
Gregory R. Keele, Jeremy W. Prokop, Hong He, Katie Holl, John Littrell, Aaron W. Deal, Yunjung Kim, Patrick B. Kyle, Esinam Attipoe, Ashley C. Johnson, Katie L. Uhl, Olivia L. Sirpilla, Seyedehameneh Jahanbakhsh, Melanie Robinson, Shawn Levy, William Valdar, Michael R. Garrett, Leah C. Solberg Woods. Sept8/SEPTIN8 involvement in cellular structure and kidney damage is identified by genetic mapping and a novel human tubule hypoxic modelScientific Reports 2021; 11(1) doi: 10.1038/s41598-021-81550-8
11
Sergiy Kostenko, Karin Lægreid Jensen, Ugo Moens. Phosphorylation of heat shock protein 40 (Hsp40/DnaJB1) by mitogen-activated protein kinase-activated protein kinase 5 (MK5/PRAK)The International Journal of Biochemistry & Cell Biology 2014; 47: 29 doi: 10.1016/j.biocel.2013.11.004
12
Manoj B. Menon, Alexey Kotlyarov. Encyclopedia of Signaling Molecules2016; : 1 doi: 10.1007/978-1-4614-6438-9_321-1
13
Manoj B. Menon, Alexey Kotlyarov. Encyclopedia of Signaling Molecules2018; : 2934 doi: 10.1007/978-3-319-67199-4_321
14
Manoj B. Menon. Encyclopedia of Signaling Molecules2017; : 1 doi: 10.1007/978-1-4614-6438-9_101986-1
15
Liyue Liu, Qin Li, Li Lin, Min Wang, Yuanan Lu, Weimin Wang, Junfa Yuan, Lijuan Li, Xueqin Liu. Proteomic analysis of epithelioma papulosum cyprini cells infected with spring viremia of carp virusFish & Shellfish Immunology 2013; 35(1): 26 doi: 10.1016/j.fsi.2013.03.367
16
Yoonhee Kim, Chaeyoung Kim, Sung Min Son, Hyundong Song, Hyun Seok Hong, Sun-ho Han, Inhee Mook-Jung. The novel RAGE interactor PRAK is associated with autophagy signaling in Alzheimer’s disease pathogenesisMolecular Neurodegeneration 2016; 11(1) doi: 10.1186/s13024-016-0068-5
17
Nicole E. James, Evelyn Cantillo, Naohiro Yano, Clinton O. Chichester, Paul A. DiSilvestro, Virginia Hovanesian, R. Shyama Prasad Rao, Kyukwang K. Kim, Richard G. Moore, Nagib Ahsan, Jennifer R. Ribeiro. Septin-2 is overexpressed in epithelial ovarian cancer and mediates proliferation via regulation of cellular metabolic proteinsOncotarget 2019; 10(31): 2959 doi: 10.18632/oncotarget.26836
18
Lee Dolat, Qicong Hu, Elias T. Spiliotis. Septin functions in organ system physiology and pathologyBiological Chemistry 2014; 395(2): 123 doi: 10.1515/hsz-2013-0233
19
Hosni A. M. Hussein, Shaw M. Akula. Profiling of cellular microRNA responses during the early stages of KSHV infectionArchives of Virology 2017; 162(11): 3293 doi: 10.1007/s00705-017-3478-y
20
Huicong Liu, Rong Tan, Jia Tong, Shuo Wen, Can Wu, Muding Rao, Jiangli Zhu, Shiqian Qi, Eryan Kong. Palmitoylation is required for Sept8‐204 and Sept5 to form vesicle‐like structure and colocalize with synaptophysinJournal of Cellular Biochemistry 2024; 125(3) doi: 10.1002/jcb.30529