Presenilin-1 maintains a nine-transmembrane topology throughout the secretory pathway (Q28252623)

1

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Alexandra Tolia

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Katleen Dillen

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Veerle Baert

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Stefan Vrijens

6

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Wim Annaert

Journal of Biological Chemistry

7

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language of work or name

English

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publication date

8 September 2006

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published in

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volume

281

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issue

36

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page(s)

26569-77

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cites work

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Aph-1, Pen-2, and Nicastrin with Presenilin generate an active gamma-Secretase complex

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Presenilin couples the paired phosphorylation of beta-catenin independent of axin: implications for beta-catenin activation in tumorigenesis

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Topology of the C-terminal fragment of human presenilin 1.

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Presenilins mutated at Asp-257 or Asp-385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin

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Presenilin 1 mediates the turnover of telencephalin in hippocampal neurons via an autophagic degradative pathway

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Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum

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Structure of the Golgi and distribution of reporter molecules at 20 degrees C reveals the complexity of the exit compartments

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Quality control in the endoplasmic reticulum

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Trafficking of potassium channels

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Bi-directional protein transport between the ER and Golgi

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X11 alpha and x11 beta interact with presenilin-1 via their PDZ domains

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Identification of a novel PSD-95/Dlg/ZO-1 (PDZ)-like protein interacting with the C terminus of presenilin-1

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Disulfide connectivity prediction using recursive neural networks and evolutionary information.

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