Signal peptide peptidase is required for dislocation from the endoplasmic reticulum (Q28243253)

5

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Joana Loureiro

object named as

Joana Loureiro

1

0 references

Hidde Ploegh

6

object named as

Hidde L Ploegh

0 references

Eric Spooner

3

object named as

Eric Spooner

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author name string

Brendan N Lilley

2

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Vanessa Noriega

Viral subversion of the immune system

4

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language of work or name

English

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publication date

15 June 2006

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published in

Nature

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volume

441

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issue

7095

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page(s)

894-7

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cites work

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Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

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The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol

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A membrane protein required for dislocation of misfolded proteins from the ER

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Quality control in the endoplasmic reticulum

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ERAD: the long road to destruction

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Human cytomegalovirus US2 endoplasmic reticulum-lumenal domain dictates association with major histocompatibility complex class I in a locus-specific manner

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Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane

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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

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US2, a Human Cytomegalovirus-encoded Type I Membrane Protein, Contains a Non-cleavable Amino-terminal Signal Peptide

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Membrane-specific, host-derived factors are required for US2- and US11-mediated degradation of major histocompatibility complex class I molecules

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Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins

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Identification of signal peptide peptidase, a presenilin-type aspartic protease

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Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs

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Intramembrane proteolysis of signal peptides: an essential step in the generation of HLA-E epitopes

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Intramembrane proteolysis promotes trafficking of hepatitis C virus core protein to lipid droplets

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Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin

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A misassembled transmembrane domain of a polytopic protein associates with signal peptide peptidase

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Signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor

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A system for stable expression of short interfering RNAs in mammalian cells

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Intramembrane proteolysis and post-targeting functions of signal peptides

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Complete differentiation between enkephalinase and angiotensin-converting enzyme inhibition by retro-thiorphan

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On the mechanism of SPP-catalysed intramembrane proteolysis; conformational control of peptide bond hydrolysis in the plane of the membrane

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A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised

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Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover.

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XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation

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