Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps - Test2 - elhamkhani - TriplyDB

Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps

Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps

http://www.wikidata.org/entity/Q24306408

about

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor The role of EDEM2 compared with EDEM1 in ricin transport from the endoplasmic reticulum to the cytosol Unfolded Protein Response and Macroautophagy in Alzheimer's, Parkinson's and Prion Diseases Recent technical developments in the study of ER-associated degradation The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology The Pathogen-Occupied Vacuoles of Anaplasma phagocytophilum and Anaplasma marginale Interact with the Endoplasmic Reticulum Tcf19 is a novel islet factor necessary for proliferation and survival in the INS-1 β-cell line A Golgi-localized mannosidase (MAN1B1) plays a non-enzymatic gatekeeper role in protein biosynthetic quality control.Mammalian ER mannosidase I resides in quality control vesicles, where it encounters its glycoprotein substrates.Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation.Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Hydrophobicity of protein determinants influences the recognition of substrates by EDEM1 and EDEM2 in human cells.Glycoprotein folding and quality-control mechanisms in protein-folding diseases Cell biology of the endoplasmic reticulum and the Golgi apparatus through proteomics Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant.Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1.The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.Herp coordinates compartmentalization and recruitment of HRD1 and misfolded proteins for ERAD.Novel function of the endoplasmic reticulum degradation-enhancing α-mannosidase-like proteins in the human hepatitis B virus life cycle, mediated by the middle envelope protein.Endoplasmic reticulum degradation-enhancing α-mannosidase-like protein 1 targets misfolded HLA-B27 dimers for endoplasmic reticulum-associated degradation.Liver-specific loss of glucose-regulated protein 78 perturbs the unfolded protein response and exacerbates a spectrum of liver diseases in mice.A shared endoplasmic reticulum-associated degradation pathway involving the EDEM1 protein for glycosylated and nonglycosylated proteins.Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Demonstration that endoplasmic reticulum-associated degradation of glycoproteins can occur downstream of processing by endomannosidase.Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates

P2860

1d2f7013540f52629cf33521031e49181cacf688 33895f9596f7a1aeaf98c4e0220e993ca867cb37 3d00bd84524cea8ebfd69450c245655e1f510ef8 481d1b88438783931a7830c2c07b48ec4c5788a6 49b1dc54bddc77a65ba3b0904033589c324a6f3e 95355475e337a4e4cff41a6fb28ba036c2e80d47 9dc48b9d2947f4734b7155e5bd4c211a8bc2b517 a371182ec5183ad34d9cc746f56412339be2bd49 ce72be904621edf3a1c4e511dc5eb901a747d42a ce99d5e45b04869e259cd72384e4a4c7c4ed4206 e01447813ca8683c70921697ce542621e21afa2f ee82f3decdcd62e51afc2c383576bef343ad12cd

P248

Q24295045-7F83D8B2-330D-4F78-9C31-27955BA92EFB Q24339440-902717A1-9F1A-4810-A126-73C9786D617D Q26773443-044A0B82-EDC0-4F78-8ECA-67555CBEE2C6 Q26823514-D4333F79-CCE7-4DAC-9D57-C4F3D85120A3 Q27015793-2D874995-DBC5-42F4-84E0-A137DDA8BD58 Q27330263-59DE2C7D-FE55-451B-85CF-727C32FEF726 Q28510633-5EBFDC42-1BD9-4B7B-851C-C92728C3C95B Q30360183-74CFAC7C-DD16-4F07-A1F1-D6D196162451 Q34960623-48A34160-1142-405B-B3EF-A54BDBC2E2CE Q35027539-A5D3FD14-0756-4B5C-8C8F-AA42100554E7 Q35160159-9C3EE9E3-9906-4356-9902-05B94A66D6FD Q35555897-7889204E-786B-42F9-8D82-8ECBD16D5E16 Q37621073-6B4A45A9-1A47-48D5-B472-16A055CFE703 Q38071282-E5EC0616-D51B-475E-A1AC-55981BBC728E Q38318154-FA8E86E1-A5EA-4290-BE43-63A4A5061434 Q38331877-7B1BBF70-4314-4DF9-AC8D-454131774D06 Q38507330-13505C66-2FEB-4038-B217-3F26B24E67C4 Q38542175-45BC787E-0AD7-45DA-979F-0E2691C9FFD3 Q38753899-044ADC31-85BF-48C3-8FFC-8A3A390624D3 Q39703354-0D1BDEBB-7A68-43D1-B069-0E0C744C5E02 Q41825121-18C23739-D683-480C-8A66-B7852A69BA66 Q42827982-1358BBDA-75D6-4F10-ABC1-B6CF9F01F662 Q48316566-60E13343-08E1-43D3-B058-C83E7D002C46 Q51767890-950AEEFB-F276-45B0-8D10-92E1C4405B74 Q58121237-4B50F40F-BDE3-45C3-A7C6-10B04949DCB1

P2860

Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps

http://www.wikidata.org/entity/Q24306408

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Mannose trimming is required f ...... m-associated degradation steps

@ast

Mannose trimming is required f ...... m-associated degradation steps

@en

Mannose trimming is required f ...... m-associated degradation steps

@en-gb

Mannose trimming is required f ...... m-associated degradation steps

@nl

type

label

Mannose trimming is required f ...... m-associated degradation steps

@ast

Mannose trimming is required f ...... m-associated degradation steps

@en

Mannose trimming is required f ...... m-associated degradation steps

@en-gb

Mannose trimming is required f ...... m-associated degradation steps

@nl

prefLabel

Mannose trimming is required f ...... m-associated degradation steps

@ast

Mannose trimming is required f ...... m-associated degradation steps

@en

Mannose trimming is required f ...... m-associated degradation steps

@en-gb

Mannose trimming is required f ...... m-associated degradation steps

@nl

P1433

Q24306408-79548CF1-9AAD-476E-92BF-A468B9EFC9EE

P1476

Q24306408-04CB1873-BCF2-4A2A-ACC1-723A535713B9

P2093

Q24306408-559443F0-205C-40D7-BD9B-FDACEE7F715F

Q24306408-6FDC5873-9D52-473B-8DD1-B7F348A148E4

Q24306408-C92C53C3-C40C-4F28-8241-69E73EC436DA

Q24306408-EFA7DD16-4A31-40DC-A176-DABB48643E5B

P2860

Q24306408-01A2E74C-8403-4E1D-ADBC-6A7D6A16F8B7

Q24306408-0AA326B8-69F7-430F-8E38-447DCC6AA264

Q24306408-0F1A7C27-3955-4745-B4A5-C7A74EC6DE46

Q24306408-1494A220-F02D-4A10-8391-6746367E0FE7

Q24306408-1567AD51-36C1-471C-B208-E79494DE6D53

Q24306408-17D82717-D00A-42FC-8F0A-968EA7DF6179

Q24306408-1A43264A-CCC5-4E2A-B1A6-D3DAE67D7888

Q24306408-1E05A527-5407-450F-85BC-9807195C5A8C

Q24306408-299D658C-6140-4B95-A42C-75BF664CD4A8

Q24306408-2C69B8E1-F25F-4D29-959B-03537DBC60FF

P304

Q24306408-848905A1-3584-43F0-88DC-CED49BB38E84

P31

Q24306408-7AB62A73-8C01-4AB3-A9D7-F7FA57E67A75

P356

Q24306408-B4D5F534-410E-43D6-B68D-8064CCBE5343

P407

Q24306408-1CAA7D60-6E56-4B33-BFDA-13462019EAB6

P433

Q24306408-7C514912-5714-4926-BECB-6A02F8CEE03C

P478

Q24306408-F7C70948-163E-49C9-9905-E672AEC8823F

P577

Q24306408-CE737916-F2EE-4C97-8A72-953B6ED710B0

P698

Q24306408-58F79258-FD3A-4F73-838B-19AC25B0F25A

P921

Q24306408-0FEE185B-05C7-4C71-8C72-D58502CFF9C4

Q24306408-6B7A6D5B-535E-4C34-8456-1B7053904397

Q24306408-755F5136-531F-4569-BC2C-8DA794267D85

Q24306408-80269E17-790A-43F7-843A-6BB090E0B3F1

Q24306408-C0D006D5-EB51-44CC-9F55-745FA39F5E13

Q24306408-CB10E037-DF73-4BFD-A0E7-7FCDF95A9D6A

Q24306408-D9301A7F-B2E1-43EE-B9DB-58C8DF59FC1C

Q24306408-DFABD648-25BD-4DC6-AA21-CAFB0FDD5B93

P932

Q24306408-079E5504-1888-4DC3-9CA5-1146649F4039

P356

JBC.M110.154849

P1433

Journal of Biological Chemistry

P1476

Mannose trimming is required f ...... m-associated degradation steps

@en

P2093

Bella Groisman

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

Efrat Ron

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

Gerardo Z Lederkremer

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

Marina Shenkman

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

P2860

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 HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum

Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator

Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation

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

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD

Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans

Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP

BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complex

P304

1292-300

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

P31

scholarly article

P356

10.1074/JBC.M110.154849

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

P407

P433

2

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

P478

286

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

P577

2011-01-14T00:00:00Z

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

P698

21062743

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

P921

mannose trimming involved in glycoprotein ERAD pathway

ER degradation enhancing alpha-mannosidase like protein 1

protein alpha-1,2-demannosylation

Mannosidase alpha class 1B member 1

Endoplasmic reticulum lectin 1

endoplasmic reticulum

P932

3020737

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