STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein (Q24323287)

Derlin 3

1 reference

Ubiquitin conjugating enzyme E2 J1

1 reference

Valosin containing protein

1 reference

Synoviolin 1

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Ubiquitin conjugating enzyme E2 G2

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ubiquitin-dependent ERAD pathway

1 reference

1 reference

Takashi Sato

1

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Yasuhiro Sako

2

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Misato Sho

3

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Mamiko Momohara

4

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Mary Ann Suico

5

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Tsuyoshi Shuto

6

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Hideki Nishitoh

7

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Tsukasa Okiyoneda

8

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Koichi Kokame

9

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Masayuki Kaneko

10

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Manabu Taura

11

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Masanori Miyata

12

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Keisuke Chosa

13

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Tomoaki Koga

14

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Saori Morino-Koga

15

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Ikuo Wada

16

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Hirofumi Kai

Transthyretin: a review from a structural perspective.

17

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language of work or name

English

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publication date

13 July 2012

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published in

Molecular Cell

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volume

47

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issue

1

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page(s)

99-110

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cites work

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Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals

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ER stress differentially regulates the stabilities of ERAD ubiquitin ligases and their substrates

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Quality and quantity control at the endoplasmic reticulum

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The biological and chemical basis for tissue-selective amyloid disease

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Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator

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Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms

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Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp

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Neurodegeneration in familial amyloid polyneuropathy: from pathology to molecular signaling

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Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation

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D18G transthyretin is monomeric, aggregation prone, and not detectable in plasma and cerebrospinal fluid: a prescription for central nervous system amyloidosis?

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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 required for dislocation of misfolded proteins from the ER

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

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OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

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Quality control in the endoplasmic reticulum

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One step at a time: endoplasmic reticulum-associated degradation

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Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell

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The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

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Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control.

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Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome

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Glucosidase and mannosidase inhibitors mediate increased secretion of mutant alpha1 antitrypsin Z.

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Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)

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Calnexin phosphorylation attenuates the release of partially misfolded alpha1-antitrypsin to the secretory pathway.

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Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum

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Myeloid Elf-1-like factor, an ETS transcription factor, up-regulates lysozyme transcription in epithelial cells through interaction with promyelocytic leukemia protein

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Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast

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EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming

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The Endoplasmic Reticulum-associated Degradation of Transthyretin Variants Is Negatively Regulated by BiP in Mammalian Cells

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Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

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Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates

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7 January 2021

Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding.

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7 January 2021

Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII.

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7 January 2021

Chaperone-like functions of high-mannose type and complex-type N-glycans and their molecular basis

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7 January 2021

Ubiquitin-mediated control of oncogene and tumor suppressor gene products

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7 January 2021

The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum

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EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

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7 January 2021

Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle

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7 January 2021

Adapting proteostasis for disease intervention

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Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns

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Roles of N-linked glycans in the endoplasmic reticulum

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7 January 2021