La proteína quinasa de serina/treonina 2 asociada a los microtúbulos es una enzima que en los humanos está codificada por el gen MAST2.​ La proteína codificada por este gen controla la actividad de y NF-kappaB.​

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dbo:abstract
  • La proteína quinasa de serina/treonina 2 asociada a los microtúbulos es una enzima que en los humanos está codificada por el gen MAST2.​ La proteína codificada por este gen controla la actividad de y NF-kappaB.​ (es)
  • La proteína quinasa de serina/treonina 2 asociada a los microtúbulos es una enzima que en los humanos está codificada por el gen MAST2.​ La proteína codificada por este gen controla la actividad de y NF-kappaB.​ (es)
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prop-es:authors
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (es)
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (es)
  • Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (es)
  • Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP, Rodríguez-Crespo I (es)
  • Bonaldo MF, Lennon G, Soares MB (es)
  • Lumeng C, Phelps S, Crawford GE, Walden PD, Barald K, Chamberlain JS (es)
  • Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL (es)
  • Nakayama M, Kikuno R, Ohara O (es)
  • Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (es)
  • Walden PD, Cowan NJ (es)
  • Walden PD, Millette CF (es)
  • Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (es)
  • Gisler SM, Stagljar I, Traebert M, Bacic D, Biber J, Murer H (es)
  • Zhou H, Xiong H, Li H, Plevy SE, Walden PD, Sassaroli M, Prestwich GD, Unkeless JC (es)
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (es)
  • Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (es)
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (es)
  • Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (es)
  • Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP, Rodríguez-Crespo I (es)
  • Bonaldo MF, Lennon G, Soares MB (es)
  • Lumeng C, Phelps S, Crawford GE, Walden PD, Barald K, Chamberlain JS (es)
  • Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL (es)
  • Nakayama M, Kikuno R, Ohara O (es)
  • Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (es)
  • Walden PD, Cowan NJ (es)
  • Walden PD, Millette CF (es)
  • Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (es)
  • Gisler SM, Stagljar I, Traebert M, Bacic D, Biber J, Murer H (es)
  • Zhou H, Xiong H, Li H, Plevy SE, Walden PD, Sassaroli M, Prestwich GD, Unkeless JC (es)
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (es)
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  • J. Biol. Chem. (es)
  • Carcinogenesis (es)
  • Cell (es)
  • Cancer Res. (es)
  • DNA Res. (es)
  • Genome Res. (es)
  • J. Immunol. (es)
  • Biol. Reprod. (es)
  • Mol. Cell. Biol. (es)
  • Mol. Syst. Biol. (es)
  • Nat. Biotechnol. (es)
  • Nat. Neurosci. (es)
  • Proteomics (es)
  • J. Biol. Chem. (es)
  • Carcinogenesis (es)
  • Cell (es)
  • Cancer Res. (es)
  • DNA Res. (es)
  • Genome Res. (es)
  • J. Immunol. (es)
  • Biol. Reprod. (es)
  • Mol. Cell. Biol. (es)
  • Mol. Syst. Biol. (es)
  • Nat. Biotechnol. (es)
  • Nat. Neurosci. (es)
  • Proteomics (es)
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prop-es:title
  • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks (es)
  • Interaction of the type IIa Na/Pi cotransporter with PDZ proteins (es)
  • Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability (es)
  • A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette (es)
  • Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation (es)
  • Proteomic identification of brain proteins that interact with dynein light chain LC8 (es)
  • Large-scale mapping of human protein-protein interactions by mass spectrometry (es)
  • Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro (es)
  • Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma receptor control IL-12 p40 synthesis and NF-kappa B activation (es)
  • Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding (es)
  • Normalization and subtraction: two approaches to facilitate gene discovery (es)
  • Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis (es)
  • Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation (es)
  • Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases (es)
  • Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs (es)
  • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks (es)
  • Interaction of the type IIa Na/Pi cotransporter with PDZ proteins (es)
  • Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability (es)
  • A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette (es)
  • Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation (es)
  • Proteomic identification of brain proteins that interact with dynein light chain LC8 (es)
  • Large-scale mapping of human protein-protein interactions by mass spectrometry (es)
  • Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro (es)
  • Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma receptor control IL-12 p40 synthesis and NF-kappa B activation (es)
  • Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding (es)
  • Normalization and subtraction: two approaches to facilitate gene discovery (es)
  • Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis (es)
  • Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation (es)
  • Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases (es)
  • Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs (es)
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dct:subject
rdfs:comment
  • La proteína quinasa de serina/treonina 2 asociada a los microtúbulos es una enzima que en los humanos está codificada por el gen MAST2.​ La proteína codificada por este gen controla la actividad de y NF-kappaB.​ (es)
  • La proteína quinasa de serina/treonina 2 asociada a los microtúbulos es una enzima que en los humanos está codificada por el gen MAST2.​ La proteína codificada por este gen controla la actividad de y NF-kappaB.​ (es)
rdfs:label
  • MAST2 (es)
  • MAST2 (es)
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is foaf:primaryTopic of