MCM3-binding GANP DNA-primase is associated with a novel phosphatase component G5PR

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Genes to cells edited by Jun-ichi Tomizawa, Blackwell Science Ltd. Institutional: £218.00 (Europe), £242.00 (Rest of World), US$382.00 (USA and Canada). Individual: £65.00 (Europe), £72.00 (Rest of World), US$114.00 (USA and Canada) ISSN 1356 9597

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Turn up the HEAT

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A novel nuclear phosphoprotein, GANP, is up-regulated in centrocytes of the germinal center and associated with MCM3, a protein essential for DNA replication

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A new member of the α4‐related molecule (α4‐b) that binds to the protein phosphatase 2A is expressed selectively in the brain and testis

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The hybridoma revolution: an offshoot of basic research

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PP2A holoenzyme assembly: In cauda venenum (the sting is in the tail)

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Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases

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Physiologic functions of PP2A: Lessons from genetically modified mice

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Identification and functional analysis of two Ca2+-binding EF-hand motifs in the B″/PR72 subunit of protein phosphatase 2A

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Protein phosphatase subunit G5PR is needed for inhibition of B cell receptor-induced apoptosis

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Diversity in genomic organisation, developmental regulation and distribution of the murine PR72/B″ subunits of protein phosphatase 2A

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Protein phosphatase subunit G5PR that regulates the JNK-mediated apoptosis signal is essential for the survival of CD4 and CD8 double-positive thymocytes

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Transgenic overexpression of G5PR that is normally augmented in centrocytes impairs the enrichment of high-affinity antigen-specific B cells, increases peritoneal B-1a cells, and induces autoimmunity in aged female mice

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BCR-crosslinking induces a transcription of protein phosphatase component G5PR that is required for mature B-cell survival

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α4 Is an Essential Regulator of PP2A Phosphatase Activity

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Eya3 partners with PP2A to induce c-Myc stabilization and tumor progression

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Regulation of Protein Phosphatase 2A Catalytic Activity by alpha4 Protein and Its Yeast Homolog Tap42

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Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation

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Structure-Activity Relationship Studies of Fostriecin, Cytostatin, and Key Analogs, with PP1, PP2A, PP5, and (β12–β13)-Chimeras (PP1/PP2A and PP5/PP2A), Provide Further Insight into the Inhibitory Actions of Fostriecin Family Inhibitors

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