| 释义 |
- References
- Further reading
{{Infobox_gene}}Serine/threonine-protein kinase MARK1 is an enzyme that in humans is encoded by the MARK1 gene.[1][2]References1. ^{{cite journal |vauthors=Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E | title = MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption | journal = Cell | volume = 89 | issue = 2 | pages = 297–308 |date=May 1997 | pmid = 9108484 | pmc = | doi =10.1016/S0092-8674(00)80208-1 }}
2. ^{{cite web | title = Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4139| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Drewes G, Trinczek B, Illenberger S, etal |title=Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7679–88 |year= 1995 |pmid= 7706316 |doi= 10.1074/jbc.270.13.7679}}
- {{cite journal |vauthors=Yang SD, Yu JS, Shiah SG, Huang JJ |title=Protein kinase FA/glycogen synthase kinase-3 alpha after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain. |journal=J. Neurochem. |volume=63 |issue= 4 |pages= 1416–25 |year= 1994 |pmid= 7931292 |doi=10.1046/j.1471-4159.1994.63041416.x }}
- {{cite journal |vauthors=Illenberger S, Drewes G, Trinczek B, etal |title=Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. |journal=J. Biol. Chem. |volume=271 |issue= 18 |pages= 10834–43 |year= 1996 |pmid= 8631898 |doi= 10.1074/jbc.271.18.10834}}
- {{cite journal | author=Paudel HK |title=The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1777–85 |year= 1997 |pmid= 8999860 |doi=10.1074/jbc.272.3.1777 }}
- {{cite journal |vauthors=Sengupta A, Kabat J, Novak M, etal |title=Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. |journal=Arch. Biochem. Biophys. |volume=357 |issue= 2 |pages= 299–309 |year= 1998 |pmid= 9735171 |doi= 10.1006/abbi.1998.0813 }}
- {{cite journal |vauthors=Wang JZ, Wu Q, Smith A, etal |title=Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. |journal=FEBS Lett. |volume=436 |issue= 1 |pages= 28–34 |year= 1998 |pmid= 9771888 |doi=10.1016/S0014-5793(98)01090-4 }}
- {{cite journal |vauthors=Hanger DP, Betts JC, Loviny TL, etal |title=New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. |journal=J. Neurochem. |volume=71 |issue= 6 |pages= 2465–76 |year= 1998 |pmid= 9832145 |doi=10.1046/j.1471-4159.1998.71062465.x }}
- {{cite journal |vauthors=Schneider A, Biernat J, von Bergen M, etal |title=Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. |journal=Biochemistry |volume=38 |issue= 12 |pages= 3549–58 |year= 1999 |pmid= 10090741 |doi= 10.1021/bi981874p }}
- {{cite journal |vauthors=Reynolds CH, Betts JC, Blackstock WP, etal |title=Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. |journal=J. Neurochem. |volume=74 |issue= 4 |pages= 1587–95 |year= 2000 |pmid= 10737616 |doi=10.1046/j.1471-4159.2000.0741587.x }}
- {{cite journal |vauthors=Nagase T, Kikuno R, Ishikawa K, etal |title=Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 2 |pages= 143–50 |year= 2000 |pmid= 10819331 |doi=10.1093/dnares/7.2.143 }}
- {{cite journal |vauthors=Liu F, Iqbal K, Grundke-Iqbal I, Gong CX |title=Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. |journal=FEBS Lett. |volume=530 |issue= 1–3 |pages= 209–14 |year= 2002 |pmid= 12387894 |doi=10.1016/S0014-5793(02)03487-7 }}
- {{cite journal |vauthors=Liu F, Zaidi T, Iqbal K, etal |title=Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5 |journal=Neuroscience |volume=115 |issue= 3 |pages= 829–37 |year= 2003 |pmid= 12435421 |doi=10.1016/S0306-4522(02)00510-9 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
- {{cite journal |vauthors=Timm T, Li XY, Biernat J, etal |title=MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1 |journal=EMBO J. |volume=22 |issue= 19 |pages= 5090–101 |year= 2003 |pmid= 14517247 |doi= 10.1093/emboj/cdg447 | pmc=204455 }}
- {{cite journal |vauthors=Trinczek B, Brajenovic M, Ebneth A, Drewes G |title=MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5915–23 |year= 2004 |pmid= 14594945 |doi= 10.1074/jbc.M304528200 }}
- {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
- {{cite journal |vauthors=Lizcano JM, Göransson O, Toth R, etal |title=LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1 |journal=EMBO J. |volume=23 |issue= 4 |pages= 833–43 |year= 2005 |pmid= 14976552 |doi= 10.1038/sj.emboj.7600110 | pmc=381014 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
- {{cite journal |vauthors=Benzinger A, Muster N, Koch HB, etal |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer |journal=Mol. Cell. Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200 }}
{{refend}}{{PDB Gallery|geneid=4139}}{{Serine/threonine-specific protein kinases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{gene-1-stub}} 1 : EC 2.7.11 |