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We began analyzing https://link.springer.com/article/10.1007/s11427-008-0068-y, but it redirected us to https://link.springer.com/article/10.1007/s11427-008-0068-y. The analysis below is for the second page.

Title[redir]:
Recent progress on the structure of Ser/Thr protein phosphatases | Science China Life Sciences
Description:
PP1, PP2A and PP2B, belonging to the PPP family of Ser/Thr protein phosphatases, participate in regulating many important physiological processes, such as cell cycle control, regulation of cell growth and division regulation, etc. The sequence homology between them is relatively high, and tertiary structure is conserved. Because of the complexity of the structure of PP2A and the diversity of its regulatory subunits, its structure is less well known than those of PP1 and PP2B. The PP2A holoenzyme consists of a heterodimeric core enzyme, comprising a scaffolding subunit and a catalytic subunit, as well as a variable regulatory subunit. In this study, the subunit compositions, similarities and differences between the Ser/Thr protein phsphatases structures are summarized.

Matching Content Categories {πŸ“š}

  • Education
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Keywords {πŸ”}

article, google, scholar, cas, protein, structure, phosphatase, subunit, cell, calcineurin, crystal, phosphatases, biol, nature, china, catalytic, access, privacy, cookies, content, serthr, wang, wei, ppa, regulation, chem, human, res, information, publish, research, search, science, mol, bound, complex, brain, data, log, journal, life, recent, progress, baijing, zhang, qun, regulatory, holoenzyme, enzyme, structures,

Topics {βœ’οΈ}

immunophilin-immunosuppressant fkbp12-fk506 complex month download article/chapter human fkbp12-fk506-calcineurin complex ser/thr protein phosphatases related subjects calcineurincyclophilin-cyclosporin shows common protein serine/threonine phosphatase-1 serine/threonine phosphatases implicated calmodulin-stimulated protein phosphatase full article pdf pp2a holoenzyme consists protein phosphatase-1 bound protein phosphatase-1 mrnas serine/threonine phosphatases sci china ser privacy choices/manage cookies molecular biology protein phosphatase-1 alpha life sciences aims double-faced phosphatase phosphatase inhibitor-1 mrna protein phosphatase2a holoenzyme phosphatase activity article science messenger phosphoprotein res heterodimeric core enzyme tumor-inducing toxins article wang adult rat brain european economic area surface hydrophobic pocket Ξ²12–β13 loop immunophilin-drug complexes hippocampal synaptic plasticity darpp-32-expressing neurons conditions privacy policy article log mol biochem parasitology key regulatory element highly regulated family recognizing cellular regulators calcineurin-nfat complex nat rev neurosci protein phosphatase-1 protein phosphatase 1 variable regulatory subunit beijing normal university beijing key laboratory x-ray structure check access

Schema {πŸ—ΊοΈ}

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         headline:Recent progress on the structure of Ser/Thr protein phosphatases
         description:PP1, PP2A and PP2B, belonging to the PPP family of Ser/Thr protein phosphatases, participate in regulating many important physiological processes, such as cell cycle control, regulation of cell growth and division regulation, etc. The sequence homology between them is relatively high, and tertiary structure is conserved. Because of the complexity of the structure of PP2A and the diversity of its regulatory subunits, its structure is less well known than those of PP1 and PP2B. The PP2A holoenzyme consists of a heterodimeric core enzyme, comprising a scaffolding subunit and a catalytic subunit, as well as a variable regulatory subunit. In this study, the subunit compositions, similarities and differences between the Ser/Thr protein phsphatases structures are summarized.
         datePublished:2008-05-17T00:00:00Z
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      headline:Recent progress on the structure of Ser/Thr protein phosphatases
      description:PP1, PP2A and PP2B, belonging to the PPP family of Ser/Thr protein phosphatases, participate in regulating many important physiological processes, such as cell cycle control, regulation of cell growth and division regulation, etc. The sequence homology between them is relatively high, and tertiary structure is conserved. Because of the complexity of the structure of PP2A and the diversity of its regulatory subunits, its structure is less well known than those of PP1 and PP2B. The PP2A holoenzyme consists of a heterodimeric core enzyme, comprising a scaffolding subunit and a catalytic subunit, as well as a variable regulatory subunit. In this study, the subunit compositions, similarities and differences between the Ser/Thr protein phsphatases structures are summarized.
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External Links {πŸ”—}(132)

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