Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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P1476

Induced oligomerization targets Golgi proteins for degradation in lysosomes.

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P2093

Adam D Linstedt

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Collin Bachert

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Ritika Tewari

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P2860

Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains

Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein

Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease

Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130

MAL, an integral element of the apical sorting machinery, is an itinerant protein that cycles between the trans-Golgi network and the plasma membrane

Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins

Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition

A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies.

Targeting of the yeast plasma membrane [H+]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole.

Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.

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4427-4437

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scholarly article

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10.1091/MBC.E15-04-0207

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P478

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2015-10-07T00:00:00Z

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26446839

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4666137

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