Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells.
about
Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulumThe pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasomeRicin A chain insertion into endoplasmic reticulum membranes is triggered by a temperature increase to 37 {degrees}CEndoplasmic reticulum-mediated protein quality control in ArabidopsisRibosome-inactivating proteins: from plant defense to tumor attackThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe isolation and characterization of temperature-dependent ricin A chain molecules in Saccharomyces cerevisiaePokeweed antiviral protein: its cytotoxicity mechanism and applications in plant disease resistanceIdentification and Characterization of Endoplasmic Reticulum-Associated Degradation Proteins Differentially Affected by Endoplasmic Reticulum StressExpression, intracellular targeting and purification of HIV Nef variants in tobacco cells.Transfer of the cholera toxin A1 polypeptide from the endoplasmic reticulum to the cytosol is a rapid process facilitated by the endoplasmic reticulum-associated degradation pathwayInhibition of endoplasmic reticulum-associated degradation in CHO cells resistant to cholera toxin, Pseudomonas aeruginosa exotoxin A, and ricin.Relevant elements of a maize gamma-zein domain involved in protein body biogenesis.Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol.Dislocation of ricin toxin A chains in human cells utilizes selective cellular factorsWild type RTA and less toxic variants have distinct requirements for Png1 for their depurination activity and toxicity in Saccharomyces cerevisiaeRicinus communis intoxications in human and veterinary medicine-a summary of real cases.Cellular response to unfolded proteins in the endoplasmic reticulum of plants.The human immunodeficiency virus antigen Nef forms protein bodies in leaves of transgenic tobacco when fused to zeolin.Endoplasmic reticulum (ER) stress response and its physiological roles in plants.Ricin B chain targeted to the endoplasmic reticulum of tobacco protoplasts is degraded by a CDC48- and vacuole-independent mechanism.Generation of pokeweed antiviral protein mutations in Saccharomyces cerevisiae: evidence that ribosome depurination is not sufficient for cytotoxicity.Vesicular transport is not required for the cytoplasmic pool of cholera toxin to interact with the stimulatory alpha subunit of the heterotrimeric g protein.Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants.Secretory pathway research: the more experimental systems the better.Endoplasmic reticulum-associated degradation of glycoproteins in plantsThe secreted plant N-glycoproteome and associated secretory pathwaysClass I alpha-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana.The role of CDC48 in the retro-translocation of non-ubiquitinated toxin substrates in plant cells.Conformational instability of the cholera toxin A1 polypeptidePlant Ribosome-Inactivating Proteins: Progesses, Challenges and Biotechnological Applications (and a Few Digressions).An Arabidopsis reticulon and the atlastin homologue RHD3-like2 act together in shaping the tubular endoplasmic reticulum.Multiple mechanism-mediated retention of a defective brassinosteroid receptor in the endoplasmic reticulum of Arabidopsis.Genomic analysis of the unfolded protein response in Arabidopsis shows its connection to important cellular processes.Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features.Control of Tobacco mosaic virus movement protein fate by CELL-DIVISION-CYCLE protein48.Signal peptide-regulated toxicity of a plant ribosome-inactivating protein during cell stress.The potato virus X TGBp2 movement protein associates with endoplasmic reticulum-derived vesicles during virus infection.ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants.Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway.
P2860
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P2860
Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells.
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Ricin A chain without its part ...... to the cytosol in plant cells.
@ast
Ricin A chain without its part ...... to the cytosol in plant cells.
@en
type
label
Ricin A chain without its part ...... to the cytosol in plant cells.
@ast
Ricin A chain without its part ...... to the cytosol in plant cells.
@en
prefLabel
Ricin A chain without its part ...... to the cytosol in plant cells.
@ast
Ricin A chain without its part ...... to the cytosol in plant cells.
@en
P2093
P2860
P356
P1476
Ricin A chain without its part ...... to the cytosol in plant cells
@en
P2093
P2860
P304
14726-14731
P356
10.1073/PNAS.251386098
P407
P577
2001-12-01T00:00:00Z