Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation - Wikidata - thesis-toulmin - TriplyDB

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

http://www.wikidata.org/entity/Q24302539

about

A transcriptome analysis identifies molecular effectors of unconjugated bilirubin in human neuroblastoma SH-SY5Y cells Defining human ERAD networks through an integrative mapping strategy SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3 Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD A novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein response RNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Inhibition of p97-dependent protein degradation by Eeyarestatin I Murine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infection Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3 Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids Glycoprotein Quality Control and Endoplasmic Reticulum Stress Mechanisms and models of endoplasmic reticulum stress in chondrodysplasia Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins.The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.Varicella-Zoster Virus Infectious Cycle: ER Stress, Autophagic Flux, and Amphisome-Mediated Trafficking A DERL3-associated defect in the degradation of SLC2A1 mediates the Warburg effect The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis ER chaperones in mammalian development and human diseases Identification of new protein interactions between dengue fever virus and its hosts, human and mosquito ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER Derlin-2-deficient mice reveal an essential role for protein dislocation in chondrocytes Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice Soy glyceollins regulate transcript abundance in the female mouse brain Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2 A molecular analysis of desiccation tolerance mechanisms in the anhydrobiotic nematode Panagrolaimus superbus using expressed sequenced tags.Surviving endoplasmic reticulum stress is coupled to altered chondrocyte differentiation and function ER stress affects processing of MHC class I-associated peptides.The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation.The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.Comparative sequence analysis reveals regulation of genes in developing schistosomula of Schistosoma mansoni exposed to host portal serum Selenoproteins: molecular pathways and physiological roles.The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.Efficient detection of proteins retro-translocated from the ER to the cytosol by in vivo biotinylation.BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum.

P2860

18056a85c2a70226a0afd13ff06ff74e690bf965 324cdbc32819196319b071a27f91595534b1c5bd 361852f1440e3d47e6bf081bb95c3818d8dbd618 7fefbf66058d5f118a3778ba000346a546fd243c 949e9ec9af4564019314bd983f291cbd6e8213cd 9f6bad71d1def72aeba1ea1863780cdb2ebdfd3e a5b292c8cd5d7b1aa363982d053490d0bc0c4df1 a80dd15b1195af053ccc78be5d93b4884464c6b1 f594920fe421c0fd02cc605e1749cc4fd450ae2c

P248

Q21283747-58F05A21-30F2-4E83-A5EB-9579022A6C5D Q24298439-52B5A5E9-6875-40E7-A2E9-42261A143984 Q24298501-55F79F50-F3FA-47CC-8184-C53E2F650114 Q24300776-E520D248-E456-466C-A73C-8C5F12043433 Q24301000-0EF1B0B5-EFF7-4786-868B-651A60077E49 Q24304415-79097E83-4CAB-433B-BA04-03E212183CEB Q24306408-1E05A527-5407-450F-85BC-9807195C5A8C Q24312778-1E803899-9DEC-4DA1-A4F3-43D1792B5658 Q24317491-058DA83F-A05E-4F32-95F1-F9551FBEDD11 Q24323658-D9FBDAB5-90A1-43C0-B53E-13F55DC8F6EC Q24648805-DDE761FC-094D-4830-A98D-7A5E40FC735C Q24674111-B326C924-DBDE-4C2E-A959-AFE451AE286D Q24683139-39D4485C-F57E-4C94-888C-0B40820D657F Q26781978-2099A8E0-2282-4EAE-A31A-D4007D3D56A1 Q26801535-EFB403AD-CF69-4416-B26E-B88B5770A26E Q26995280-FFB98BF6-BE29-4D23-8495-1DA2ECB48A6E Q27863410-89D68A3A-1503-4CDC-91EC-82B74C36EF43 Q27934285-1E9425A9-8391-42D3-9F50-079EEC4C329E Q27938831-566167B9-20AA-4EAC-BC58-7FB4D79540CD Q28076761-7F98FF2B-4D94-466F-A436-C4E0D39E3464 Q28237387-1E4ED6CA-0B88-4A79-968F-55CAC76CE67F Q28264480-4B2F40F7-996C-4BAC-AA3D-8775F122EF29 Q28269674-C6EA802B-ACAA-42C2-9AF9-57E3E53C77B6 Q28300625-C6ABE8AC-6128-4C3A-8E21-678FD4E288BA Q28485040-64416DCE-71D9-44E6-A619-99B6C314C118 Q28512215-7F361FA6-D8B8-4E69-B795-911048C764C5 Q28593497-CE5CFC33-E0E8-4B57-A5F6-7FD34F5FB178 Q28730861-D95845C9-BBDE-4593-9209-2A014203B03F Q30356806-6065CBB5-F7A0-4D5B-BCBC-88122FF2A0C7 Q30478432-EB9264C1-F49D-44D6-A6D9-796D47EF778C Q30506753-E4C03905-8C66-42F6-85EE-5037813E4FA2 Q33273633-C6BE3610-F782-4DD9-9E96-8D481547067E Q33409763-B5BA6E59-B834-4EB9-93F6-3CA25F93562C Q33571592-B5FEA0BB-C33A-497C-A46A-772F5DDC5BFC Q33721156-8BBD60D0-5E18-4017-A733-D327613D7295 Q33807012-D96AA335-ACB4-473E-B982-601E9F7F20B7 Q33913069-4FAE7E80-5360-450E-9E74-0D360CDD0627 Q33967026-8EA57FA7-75C5-4282-B123-1A238CE4AF04 Q34009537-F6261E12-7FC1-4B24-A52D-CF15E674D1A0 Q34103187-B56D4A81-9141-49B9-8CF5-35A9F8ACC245

P2860

Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation

http://www.wikidata.org/entity/Q24302539

description

2006 nî lūn-bûn

@nan

2006 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年学术文章

@wuu

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

name

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@ast

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en-gb

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@nl

type

label

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@ast

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en-gb

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@nl

prefLabel

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@ast

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en-gb

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@nl

P1433

Q24302539-B2CFBFD0-A9A6-4656-81B0-3CE24B8952A1

P1476

Q24302539-4C295EFE-D22E-4845-8376-5D109DE63317

P2093

Q24302539-1F62BE8E-EBC4-4389-8F7F-63981E13038C

Q24302539-320B9674-6429-41E2-815F-CC83B2A86A19

Q24302539-337EF66D-E925-487B-AEC5-827B93263D4C

Q24302539-6EBEE8B1-3D7D-479B-8A87-4CC08F361DE5

Q24302539-D81AFE61-6E66-42F1-8A2E-6E5C3E183F9D

P2860

Q24302539-170059E6-5687-47CB-91AB-5038A94FEFE7

Q24302539-18BF2887-79F9-4D20-90E4-8CD6683350B1

Q24302539-1AEDF694-4996-478A-9E65-ACC3DA4F897E

Q24302539-1EF0B509-5721-49FE-B35C-68370EE047D9

Q24302539-24FBE106-FC03-4518-899B-9C3D9BC76E24

Q24302539-2B9431AB-B10E-4D00-A459-AA4D9B90C61B

Q24302539-31444452-24D8-4DFC-84E4-25047B15353E

Q24302539-33C0D552-82E8-4698-8947-41F7C8336557

Q24302539-363FC5B3-B002-426C-807C-D4BDFF61CC68

Q24302539-36EB19CC-6538-4A7F-80C2-38FB9270BA0A

P304

Q24302539-9B7FAE4D-C268-4FC9-B534-5B0A0141CBCF

P31

Q24302539-030C675A-B30B-4067-8B98-2CB1473DB8FA

P3181

Q24302539-60F2AA35-2F02-429F-9D8D-A80C70B0199B

P356

Q24302539-9452F672-30EF-4EE7-B393-531BABC495C0

P407

Q24302539-E7F1C4BD-DBFF-4FD9-A7DF-4BE0D808C351

P433

Q24302539-826DD09D-5481-4055-B0A3-554DEA18FA5D

P478

Q24302539-97CE7F79-2FA2-4C33-82EF-C0C7E0202490

P50

Q24302539-D458A227-A57A-4719-BDE6-361D4084FE29

P577

Q24302539-FEB108FF-70B8-4FF7-86D4-611A6C76A0EB

P5875

Q24302539-BB74E549-58E0-433F-95F8-C52247EF2E6F

P698

Q24302539-08BFB666-ECF7-4022-A7CB-B9478E7C2F41

P921

Q24302539-08A97BB4-311F-4612-B4C7-FF78C1214C4B

Q24302539-2130328D-7540-4572-9B67-04C2A0FCFC36

Q24302539-4242F206-B6E2-4203-B49F-90DB0F4BF597

Q24302539-BFE11035-4F92-44A4-A1B7-7B7D9A20B88E

Q24302539-E14E5D80-1970-4227-863D-DDB8C29AE004

P932

Q24302539-B815DE17-913D-47DD-994F-56C154175CCD

P3181

P356

P1433

Journal of Cell Biology

P1476

Derlin-2 and Derlin-3 are regu ...... for ER-associated degradation

@en

P2093

Kazuhiro Nagata

http://www.w3.org/2001/XMLSchema#string

Kazutoshi Mori

http://www.w3.org/2001/XMLSchema#string

Randal J Kaufman

http://www.w3.org/2001/XMLSchema#string

Tetsuya Okada

http://www.w3.org/2001/XMLSchema#string

Yukako Oda

http://www.w3.org/2001/XMLSchema#string

P2860

Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle

A membrane protein required for dislocation of misfolded proteins from the ER

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins

Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation

Evolutionary conservation of components of the protein translocation complex

Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane

P304

383-393

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

2910493

http://www.w3.org/2001/XMLSchema#string

P356

10.1083/JCB.200507057

http://www.w3.org/2001/XMLSchema#string

P407

P433

3

http://www.w3.org/2001/XMLSchema#string

P478

172

http://www.w3.org/2001/XMLSchema#string

P50

P577

2006-01-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

7325163

http://www.w3.org/2001/XMLSchema#string

P698

16449189

http://www.w3.org/2001/XMLSchema#string

P921

retrograde protein transport, ER to cytosol

P932

2063648

http://www.w3.org/2001/XMLSchema#string