Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin (Q28242760)

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scientific article (publication date: April 2004)

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Language	Label	Description	Also known as
English	Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin	scientific article (publication date: April 2004)

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instance of

scholarly article

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title

Dissection of the dislocation pathway for type I membrane proteins with a new small molecule inhibitor, eeyarestatin (English)

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main subject

cell biology

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membrane protein

1 reference

based on heuristic

inferred from title

author

Domenico Tortorella

series ordinal

6

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Jatin M. Vyas

object named as

Jatin M Vyas

series ordinal

3

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Hidde Ploegh

series ordinal

5

object named as

Hidde L Ploegh

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author name string

Edda Fiebiger

series ordinal

1

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Christian Hirsch

series ordinal

2

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Eva Gordon

series ordinal

4

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language of work or name

English

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publication date

April 2004

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published in

Molecular Biology of the Cell

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volume

15

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issue

4

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page(s)

1635-46

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cites work

Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.

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

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HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins

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Antigen presentation subverted: Structure of the human cytomegalovirus protein US2 bound to the class I molecule HLA-A2

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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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Pathways for protein disulphide bond formation

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Der3p/Hrd1p Is Required for Endoplasmic Reticulum-associated Degradation of Misfolded Lumenal and Integral Membrane Proteins

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Role of Cue1p in Ubiquitination and Degradation at the ER Surface

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

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ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway

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Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast

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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 role for N-glycanase in the cytosolic turnover of glycoproteins

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Traffic jams II: an update of diseases of intracellular transport

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Analysis of protease activity in live antigen-presenting cells shows regulation of the phagosomal proteolytic contents during dendritic cell activation

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Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays.

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Visualization of the ER-to-cytosol dislocation reaction of a type I membrane protein

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Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol

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Proteasome inhibitors: from research tools to drug candidates

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Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast

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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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Signal peptide cleavage of a type I membrane protein, HCMV US11, is dependent on its membrane anchor

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Intracellular targeting of the proteasome

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Rapid degradation of a large fraction of newly synthesized proteins by proteasomes.

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Why certain antibodies cross-react with HLA-A and HLA-G: epitope mapping of two common MHC class I reagents.

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29 September 2017

Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential

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In Vitro Translation and Assembly of a Complete T Cell Receptor–CD3 Complex

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Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein

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29 September 2017

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Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum

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29 September 2017

Use of a monoclonal antibody (W6/32) in structural studies of HLA-A,B,C, antigens

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Cytokines regulate proteolysis in major histocompatibility complex class II-dependent antigen presentation by dendritic cells

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Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation

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Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits

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Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera

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Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells

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Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products

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Ubiquitin and the control of protein fate in the secretory and endocytic pathways

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Identifiers

DOI

10.1091/MBC.E03-07-0506

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PMC publication ID

379262

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PubMed publication ID

14767067

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