Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
about
Shiga Toxins as Multi-Functional Proteins: Induction of Host Cellular Stress Responses, Role in Pathogenesis and Therapeutic ApplicationsActivation of cell stress response pathways by Shiga toxinsA bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause diseaseEeyarestatin 1 interferes with both retrograde and anterograde intracellular trafficking pathwaysCytosolic entry of Shiga-like toxin a chain from the yeast endoplasmic reticulum requires catalytically active Hrd1pInduction of apoptosis by Shiga toxins.BiP negatively affects ricin transport.The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effectShiga toxins: intracellular trafficking to the ER leading to activation of host cell stress responses.Shiga toxins induce autophagy leading to differential signalling pathways in toxin-sensitive and toxin-resistant human cells.The nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation.The Translocation Domain of Botulinum Neurotoxin A Moderates the Propensity of the Catalytic Domain to Interact with Membranes at Acidic pHRetrograde trafficking of AB₅ toxins: mechanisms to therapeuticsBcl-2 regulates the onset of shiga toxin 1-induced apoptosis in THP-1 cellsInsights on the trafficking and retro-translocation of glycosphingolipid-binding bacterial toxins.Retromer guides STxB and CD8-M6PR from early to recycling endosomes, EHD1 guides STxB from recycling endosome to Golgi.Shiga toxin is transported into the nucleoli of intestinal epithelial cells via a carrier-dependent process.Passage through the Golgi is necessary for Shiga toxin B subunit to reach the endoplasmic reticulum.Cholera toxin up-regulates endoplasmic reticulum proteins that correlate with sensitivity to the toxin.Shiga Toxin Therapeutics: Beyond Neutralization.
P2860
Q26752966-5079840D-B9A7-45C5-AC18-A813377F5CDDQ27027623-3ACDDB7A-A860-4377-86F9-4D72338B2681Q28087358-B259A3B7-D708-49D2-9A40-46691BFC45CEQ28479267-DB24E137-AD7F-4F4F-949D-96147826BD38Q28481415-F4DB1270-8049-4856-B82F-DFF157FF90ACQ33793688-51D47A9D-ACDE-481C-BD0F-48B0D1F4CC0BQ34344213-5F9E1875-A622-4DA9-96AD-2915AB5D693BQ34407346-1D5A4476-1065-425D-ACD3-ED8BD2153D62Q35155837-7769B224-E1B6-40E2-BA1C-491FE22CFF2CQ35214193-488B671C-9C8F-454F-BDA4-234457691476Q35717779-AE2F7025-43DB-40BC-89D3-8B25B868576CQ35987067-F428C965-A4DB-48AE-A4C2-BB0545A7332BQ37171510-18B90BA5-830D-4E71-8EA2-6562C287565FQ37451195-1C594517-0A8A-4D62-B3A2-71FDC20F269BQ38037553-B6D80930-C8D6-4F7A-B17A-02FAA1A522A9Q39357458-1594F8E5-3C60-41BF-8265-7DF04D98F6E2Q39699154-0E434A3A-0C8F-46ED-8A0F-CD6360E450A8Q39883425-FFE16C65-08EA-4F1C-9230-512BC0FA585EQ40020256-F7706049-8BE7-42B7-946A-CD7AC64D6E6DQ41669177-A912EBB1-16ED-4130-8F62-F4D9EB62F1CE
P2860
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
@en
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
@nl
type
label
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
@en
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
@nl
prefLabel
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
@en
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23.
@nl
P2860
P356
P1433
P1476
Shiga toxin B-subunit binds to the chaperone BiP and the nucleolar protein B23
@en
P2093
Thomas Falguières
P2860
P304
P356
10.1042/BC20050001
P577
2006-02-01T00:00:00Z