The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)
about
The degradation of apolipoprotein B100: multiple opportunities to regulate VLDL triglyceride production by different proteolytic pathwaysHow Polyomaviruses Exploit the ERAD Machinery to Cause InfectionThe yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.Overexpression, Purification and Characterisation of the Plasmodium falciparum Hsp70-z (PfHsp70-z) ProteinA Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum MembraneThe biogenesis of chylomicronsHsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone systemUbiquitylation in ERAD: reversing to go forward?Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta.Hsp70- and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila.Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesRkr1/Ltn1 Ubiquitin Ligase-mediated Degradation of Translationally Stalled Endoplasmic Reticulum Proteins.Intracellular trafficking and secretion of VLDL.Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels.Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.The endoplasmic reticulum-associated degradation pathways of budding yeast.The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelHsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseThe activities and function of molecular chaperones in the endoplasmic reticulum.The many intersecting pathways underlying apolipoprotein B secretion and degradationSuppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110ERAD and how viruses exploit it.Structural mechanisms of chaperone mediated protein disaggregation.Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon.Endoplasmic reticulum-associated degradation of the renal potassium channel, ROMK, leads to type II Bartter syndrome.Membrane Protein Quantity Control at the Endoplasmic Reticulum.Co-evolutionary analysis implies auxiliary functions of HSP110 in Plasmodium falciparum.Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activityThe use of in vitro assays to measure endoplasmic reticulum-associated degradation.The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins.Can modulators of apolipoproteinB biogenesis serve as an alternate target for cholesterol-lowering drugs?
P2860
Q26824858-61A368EE-97E2-4D77-9C2E-B67150EEE563Q27468807-699E7C1F-BB33-489B-95F9-36FF73C38023Q27932962-40F35A1E-584F-4966-9054-EF2625F04508Q27937556-45843AF4-834A-4A1C-9F68-8D4ACC80885EQ27973911-C3783D21-519D-41F9-9B28-259E3687ABD2Q28547004-D4540A9D-03E3-4BD2-A1D6-CFB5E492A06AQ28833221-A5321D9A-F371-42FF-A83D-E71DF23B434DQ33818438-00317910-9FD8-4EA4-B23E-F016922A5ECFQ33863568-8730E68A-CA9A-4AA9-8538-36F876400F83Q33963759-33A2E303-B124-4D53-BAF0-ABE7C2F9FE93Q34177990-A2B47990-4F2B-4FA9-8E4E-2E335C68D370Q34204041-F3E3F130-1EB9-49A4-B8FC-E881F7BDC72EQ34765885-C6CD102D-1613-4620-BA8C-B271BDCD6957Q35756661-5452FE71-352F-4EC7-B25B-FD0AD8C2D4C2Q35883810-36355E48-5A4D-4E19-9DED-EBFA9B6DE534Q35906628-CD2FEF57-CD33-471E-AA52-04043C2CA820Q36003713-99486C2C-3F1F-4990-821B-4E2013732AB3Q36027390-35F929C2-85F0-4C53-B381-6F5221DDE26CQ36418006-2995F66E-8D6A-4061-9C04-CD0B8E2B3C9BQ36947831-7CA7A827-B925-4E2F-8FEA-5C5015F68C9BQ36947877-78A0A009-8E7C-456B-BE3C-9A8C14480FCAQ36982944-6FB9BAC7-19B6-409E-A9C6-82566A068545Q37240302-1A605E41-9AFB-48A9-AA14-93E9B6A3F8F0Q37299616-89E3F152-7F07-44F8-986A-E44F59F7B910Q38234935-67B578D7-625C-4154-8C68-0037010E2451Q38490755-A8E68AA0-6D44-4363-91A2-5F2338E7AC15Q38604728-F1A2F779-573C-4F4B-A467-4B6D29839419Q38669157-B0ABA6B5-E3F5-4CD0-BAB6-8204CE769B02Q38981333-D821E269-7788-4F11-AA00-08E36B188DE1Q40860270-540C72CA-8BED-485F-9663-1ABA194A3C11Q41480929-7FC85B23-64A5-411F-855E-FB3735279A86Q42234007-7D81E6F1-AC50-4492-9D6C-59EDD7A4A943Q42949802-69607581-5AD2-42B9-8439-BDD710225810Q52600967-CA8814B0-A0AF-4D1F-BC50-3E1A9D2A9984
P2860
The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 06 September 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The Hsp110 molecular chaperone ...... -associated degradation (ERAD)
@en
The Hsp110 molecular chaperone ...... ticulum-associated degradation
@nl
type
label
The Hsp110 molecular chaperone ...... -associated degradation (ERAD)
@en
The Hsp110 molecular chaperone ...... ticulum-associated degradation
@nl
prefLabel
The Hsp110 molecular chaperone ...... -associated degradation (ERAD)
@en
The Hsp110 molecular chaperone ...... ticulum-associated degradation
@nl
P2093
P2860
P356
P1476
The Hsp110 molecular chaperone ...... -associated degradation (ERAD)
@en
P2093
David M Habiel
Jeffrey L Brodsky
Stacy L Hrizo
Viktoria Gusarova
P2860
P304
32665-32675
P356
10.1074/JBC.M705216200
P407
P577
2007-09-06T00:00:00Z