Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation - Wikidata - awgldk - TriplyDB

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

http://www.wikidata.org/entity/Q39730551

about

Rho GTPase and cAMP/protein kinase A signaling mediates myocilin-induced alterations in cultured human trabecular meshwork cells A luminal flavoprotein in endoplasmic reticulum-associated degradation Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation A deubiquitinase negatively regulates retro-translocation of nonubiquitinated substrates The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease ER chaperones in mammalian development and human diseases Stabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxication Proteomic analysis of MG132-treated germinating pollen reveals expression signatures associated with proteasome inhibition A large and intact viral particle penetrates the endoplasmic reticulum membrane to reach the cytosol Attachment and entry of Chlamydia have distinct requirements for host protein disulfide isomerase.Acute ablation of PERK results in ER dysfunctions followed by reduced insulin secretion and cell proliferation.The E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation.Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum Endoplasmic reticulum calcium regulates the retrotranslocation of Trypanosoma cruzi calreticulin to the cytosol.Role of intramembrane charged residues in the quality control of unassembled T-cell receptor alpha-chains at the endoplasmic reticulum The final moments of misfolded proteins en route to the proteasome.PERK (EIF2AK3) regulates proinsulin trafficking and quality control in the secretory pathway.Neuroligin trafficking deficiencies arising from mutations in the alpha/beta-hydrolase fold protein family Hsp90 is required for transfer of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol.Toxin instability and its role in toxin translocation from the endoplasmic reticulum to the cytosol.Substrate recognition by the protein disulfide isomerases.Mechanisms of neuroprotection by protein disulphide isomerase in amyotrophic lateral sclerosis.Establishment of an in vitro transport assay that reveals mechanistic differences in cytosolic events controlling cholera toxin and T-cell receptor α retro-translocation Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit Characterization of a mutant Escherichia coli heat-labile toxin, LT(R192G/L211A), as a safe and effective oral adjuvant.Action of protein disulfide isomerase on proinsulin exit from endoplasmic reticulum of pancreatic β-cells.Structural and functional interactions between the cholera toxin A1 subunit and ERdj3/HEDJ, a chaperone of the endoplasmic reticulum.The nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation.Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells Division of labor among oxidoreductases: TMX1 preferentially acts on transmembrane polypeptides.PDI reductase acts on Akita mutant proinsulin to initiate retrotranslocation along the Hrd1/Sel1L-p97 axis.Protein quality control in the early secretory pathway Derlin-1 facilitates the retro-translocation of cholera toxin.The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.Cellular response to unfolded proteins in the endoplasmic reticulum of plants.Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.

P2860

Q24299747-E74A71AB-48DA-4B27-9F39-9416F0D94364 Q24309147-C5D60CE2-C4DA-4FAB-9377-B0EC55B2C775 Q24322026-E4F4FC71-E853-4F43-A930-9CA7B03D514E Q24337261-2BE95F8B-E4A1-407B-AD59-30475EFB3283 Q27015793-488DED7E-1EBE-40B2-8252-65582C207CFA Q28087358-D1500A5A-F74B-4BFA-8600-8D3F8D81B9FA Q28300625-0B239D0F-20C4-4428-9304-25CDF10F32B4 Q28485727-74FC94BD-C305-4C6F-B022-9EEB6D6DA41C Q28543385-2C2A88D7-FC26-42BA-87A8-CA8FC6E7C219 Q31010336-93C58914-B0F7-4758-B00F-0480C24DDE18 Q33426342-B94AE063-185B-43CD-98CC-E247EDA5BCD3 Q33500340-3D4C3901-C098-41F1-A4FD-8162A5368E77 Q33571592-C377C89D-EF1B-4566-8B95-38F3B6534E08 Q33676397-0705390F-0B71-4EAA-92E5-230C864097A2 Q33722074-9944982E-471B-4BAC-B8EF-88DABD133AE7 Q33748594-6253D237-161C-46E8-B18F-B5A16472E5A3 Q33980716-7DE38683-937C-4620-B4C0-A378EA685549 Q34024253-4F0AC7A5-DE7C-4759-96CC-DAA3E3C3CC4A Q34121266-FDB50F67-DCB4-4E14-BF7B-D1117D4B6D37 Q34181280-BE5ED6E2-0A0B-4473-BF71-572BCD384885 Q34426721-6BA30396-0DA5-4F5F-A7AC-14EF862F7A59 Q34692501-C0A08BDA-317F-42D3-BAC3-8D33B535B388 Q34986548-58E6BA5C-38AD-4052-AB2A-96FC732D7564 Q35022480-6B8A721B-4DF5-438B-8494-7D9EE8405B2B Q35063023-588054A1-8AC0-44C9-8FEF-856EC83D2713 Q35066293-48B01BDD-230A-49E5-BF1A-4654FDE8AC0D Q35643714-ADA97529-6C9E-4DB3-A5B2-D51756DE080A Q35671627-3F612C1D-D2D4-4740-A6C1-4A003847DEAC Q35717779-BD3A1B57-5150-453C-9826-9B3844D63901 Q35723571-AFAB80CF-B205-4CA7-A509-5ECBB30A3D6B Q35756661-88AE7F9D-9C2B-4472-95CD-E20E1063CAEF Q35942438-15D8C968-046B-486D-9CD6-1DAD80905290 Q36115364-2C205316-2DEE-4577-8A11-7A0A91DD68BF Q36115375-779C4E95-D944-465D-A90A-D74B5479A6F3 Q36446833-C9854AB3-E78E-4B1A-99D8-2B352B4C7E83 Q36488986-7FA912C1-6B57-4CEC-8256-978E29967C2D Q36680557-2102C4C1-7F6E-45AB-A00A-2CA88709CBC3 Q36704502-DD9A0331-B74F-48BF-9DD8-9253137C2DAE Q36719733-4B580BB5-AC66-4EA1-8C58-CD951EB2D682 Q36890014-BC25F819-6C75-4DBC-BECC-9BBF5B0147AF

P2860

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

http://www.wikidata.org/entity/Q39730551

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

2006年论文

@zh

2006年论文

@zh-cn

name

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

@en

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation.

@nl

type

label

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

@en

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation.

@nl

prefLabel

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

@en

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation.

@nl

P1433

Q39730551-2ECFE16E-8D53-43F1-A813-084A14CF8224

P1476

Q39730551-6EB8EE13-960F-4209-BD61-94E61F36E594

P2093

Q39730551-0156D4BB-81B7-4343-BC36-8D195E26B5FB

Q39730551-307062D4-44E2-41F4-B197-2385CC67C7CB

Q39730551-359F5DDE-628F-4423-898D-6E2280695A77

Q39730551-8AF31E55-D9A8-4717-879B-A5F54E7E7C23

Q39730551-A1B5B7BE-95A7-49E8-8012-B005396E2F73

P2860

Q39730551-293AC4EA-05BC-42C6-8245-06F0B9376B2C

Q39730551-52FB791A-B1BE-4CE9-8173-D08DE8689C78

Q39730551-59D12853-7330-4E78-A7F8-7D44E360D778

Q39730551-5D79D1CA-F4B9-4A46-B690-D16E46CD015E

Q39730551-65527AE3-137B-4DB2-889F-94A832FE8F0D

Q39730551-6D19AE2D-C6F3-4BF4-A0C5-F2B1CB064CBC

Q39730551-764C84CF-F8B2-4A44-A928-8B43A0AB7E53

Q39730551-7841B4B6-B4BC-42EE-A823-08B130424297

Q39730551-7AFA090F-4AAE-4C18-95B8-004640546893

Q39730551-7E67CA50-9FDD-4AEB-8F94-B13656E1016B

P304

Q39730551-2BFF59C9-0D71-49B1-B4F7-15F6224042FE

P31

Q39730551-1CBB31BA-9DC4-4D42-BDD0-E4174FB9E724

P356

Q39730551-FEF4DD72-8F88-4AEA-964A-F33ECEBE1139

P407

Q39730551-C953D8B0-A52C-4FB2-B3AD-734BEC5EFC0B

P433

Q39730551-537428F6-8F7A-4419-9A4C-BB85AE318445

P478

Q39730551-046C98E9-2A0C-420F-8ED3-7B79442740DF

P50

Q39730551-F204A4EE-BB94-4086-BBEC-448D09D245E5

P577

Q39730551-8215AB98-2917-4795-BE1C-5F04685DA48F

P5875

Q39730551-64A2A433-449E-4F7C-90B1-5E3367006E11

P698

Q39730551-7097D2F7-455A-4399-B728-0F768C50C95A

P932

Q39730551-A55CBA7E-7792-4F46-898D-4144AD390FA9

P356

P1433

Journal of Cell Biology

P1476

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation

@en

P2093

Billy Tsai

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

Kelsey Sivick

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

Michele L Forster

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

Peter Arvan

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

Young-Nam Park

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

P2860

Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3

Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity

Protein disulfide isomerase

Differential cooperative enzymatic activities of protein disulfide isomerase family in protein folding.

Quality control in the endoplasmic reticulum

Enteric bacterial toxins: mechanisms of action and linkage to intestinal secretion.

ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding.

Retro-translocation of proteins from the endoplasmic reticulum into the cytosol.

The endoplasmic reticulum membrane is permeable to small molecules.

Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.

P304

853-859

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

P31

scholarly article

P356

10.1083/JCB.200602046

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

P407

P433

6

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

P478

173

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

P50

Wayne I. Lencer

P577

2006-06-01T00:00:00Z

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

P5875

6999262

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

P698

16785320

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

P932

2063911

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