about
Quality control of inner nuclear membrane proteins by the Asi complex.Analysis of familial hemophagocytic lymphohistiocytosis type 4 (FHL-4) mutant proteins reveals that S-acylation is required for the function of syntaxin 11 in natural killer cellsSterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4Intermediate organelles of the plant secretory pathway: identity and function.Quality control: ER-associated degradation: protein quality control and beyondA phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.Protein domains involved in assembly in the endoplasmic reticulum promote vacuolar delivery when fused to secretory GFP, indicating a protein quality control pathway for degradation in the plant vacuole.Tomato spotted wilt virus glycoproteins induce the formation of endoplasmic reticulum- and Golgi-derived pleomorphic membrane structures in plant cells.Golgi-dependent transport of vacuolar sorting receptors is regulated by COPII, AP1, and AP4 protein complexes in tobacco.Receptor salvage from the prevacuolar compartment is essential for efficient vacuolar protein targeting.Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo.The syntaxins SYP31 and SYP81 control ER-Golgi trafficking in the plant secretory pathway.Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail.TANGO1 builds a machine for collagen export by recruiting and spatially organizing COPII, tethers and membranes.A recycling-defective vacuolar sorting receptor reveals an intermediate compartment situated between prevacuoles and vacuoles in tobacco.Predominant Golgi Residency of the Plant K/HDEL Receptor Is Essential for Its Function in Mediating ER RetentionVacuolar transport in tobacco leaf epidermis cells involves a single route for soluble cargo and multiple routes for membrane cargoBiallelic TANGO1 mutations cause a novel syndromal disease due to hampered cellular collagen secretion
P50
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P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Ombretta Foresti
@ast
Ombretta Foresti
@en
Ombretta Foresti
@es
Ombretta Foresti
@nl
Ombretta Foresti
@sl
type
label
Ombretta Foresti
@ast
Ombretta Foresti
@en
Ombretta Foresti
@es
Ombretta Foresti
@nl
Ombretta Foresti
@sl
prefLabel
Ombretta Foresti
@ast
Ombretta Foresti
@en
Ombretta Foresti
@es
Ombretta Foresti
@nl
Ombretta Foresti
@sl
P1053
J-8165-2015
P106
P1153
9336367900
P21
P31
P3829
P496
0000-0002-6878-0395