Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins. - Wikidata - wikimedia - TriplyDB

Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins.

Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins.

http://www.wikidata.org/entity/Q34719366

about

ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C Disease-associated mutations affect intracellular traffic and paracellular Mg2+ transport function of Claudin-16 Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation Human oligodendrocytes express Cx31.3: function and interactions with Cx32 mutants Loss-of-function GJA12/Connexin47 mutations cause Pelizaeus-Merzbacher-like disease The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Systemic inflammation disrupts oligodendrocyte gap junctions and induces ER stress in a model of CNS manifestations of X-linked Charcot-Marie-Tooth disease.Divergent effects of two sequence variants of GJB3 (G12D and R32W) on the function of connexin 31 in vitro Defining a minimal motif required to prevent connexin oligomerization in the endoplasmic reticulum Inefficient maturation of the rat luteinizing hormone receptor. A putative way to regulate receptor numbers at the cell surface Autophagy modulates dynamics of connexins at the plasma membrane in a ubiquitin-dependent manner Identification of a dimerization domain in the TMEM16A calcium-activated chloride channel (CaCC)Connexin32 mutations cause loss of function in Schwann cells and oligodendrocytes leading to PNS and CNS myelination defects Rab2A is a pivotal switch protein that promotes either secretion or ER-associated degradation of (pro)insulin in insulin-secreting cells.Phenotypes and cellular effects of GJB1 mutations causing CMT1X in a cohort of 226 Chinese CMT families.Identification of rab20 as a potential regulator of connexin 43 trafficking.Modularity of the Hrd1 ERAD complex underlies its diverse client range.CamKII inhibitors reduce mitotic instability, connexon anomalies and progression of the in vivo behavioral phenotype in transgenic animals expressing a mutated Gjb1 gene.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control Low pH enhances connexin32 degradation in the pancreatic acinar cell.Sequential actions of the AAA-ATPase valosin-containing protein (VCP)/p97 and the proteasome 19 S regulatory particle in sterol-accelerated, endoplasmic reticulum (ER)-associated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase.Regulation of lens gap junctions by Transforming Growth Factor beta.Mechanisms of gap junction traffic in health and disease Voltage opens unopposed gap junction hemichannels formed by a connexin 32 mutant associated with X-linked Charcot-Marie-Tooth disease Degradation of a connexin40 mutant linked to atrial fibrillation is accelerated.Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase Membrane traffic in myelinating oligodendrocytes.Syndromic and non-syndromic disease-linked Cx43 mutations.Autophagy: a pathway that contributes to connexin degradation.Human connexin disorders of the skin.Sharing signals: connecting lung epithelial cells with gap junction channels.The connexin46 mutant, Cx46T19M, causes loss of gap junction function and alters hemi-channel gating Cardio-metabolic effectsof HIV protease inhibitors (lopinavir/ritonavir)Connexin gene pathology.Androgen-regulated formation and degradation of gap junctions in androgen-responsive human prostate cancer cells Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD).Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin.Vitamin D3 regulates the formation and degradation of gap junctions in androgen-responsive human prostate cancer cells Missense mutations in GJB2 encoding connexin-26 cause the ectodermal dysplasia keratitis-ichthyosis-deafness syndrome.Functional alterations in gap junction channels formed by mutant forms of connexin 32: evidence for loss of function as a pathogenic mechanism in the X-linked form of Charcot-Marie-Tooth disease.

P2860

Q24318838-82D5F223-1D9E-453B-BD69-15356183DEC4 Q24544268-0264FE59-E3C2-4FEF-99EF-796A8E39DD9D Q24653719-93B97B5A-BA89-4F56-8E45-82FB85EC5629 Q24655300-8FEF8E67-ECBF-4077-9307-40B13F04A6AA Q24682835-9C298CD3-F323-414F-8995-0AD041067BA2 Q27015793-8BF0E2FC-E56C-42F2-AF11-B220045AECC8 Q27316720-AC83B39E-8399-422E-B8A2-861BDB3EAE4F Q28191724-44B80B50-A231-46A6-B623-0892EAC2965E Q28564736-AF1871F6-D380-42D1-8AAE-1CBC500F2F25 Q28577566-7618A1E5-9892-4ABF-A7C5-2E9B8CD9C41D Q28590933-1322E019-045B-4F2D-A214-F5E630785673 Q28592114-1E53A6FB-74C3-4A30-83EE-8A4A5A2DA71B Q30485962-90418EDB-7775-4530-A984-4BBA1C26CDF4 Q30844266-47F8A79C-E8BE-4E20-B86B-10FA916881A7 Q32186771-EA361808-86DF-4B50-B208-80AEEB1B904A Q33354230-1EB4B264-6752-44C2-A628-94FD85ED972E Q33717057-A5C5DC3C-B6F2-444C-8D74-EC24191C335A Q33750892-86BA49A2-81DF-41D5-8C87-A58A598A5CC2 Q33761462-D0B67652-9E0E-4509-BC14-2587FD7E273E Q33840000-FBE0D82C-4B4D-4130-B666-209E93D96BDA Q33846508-3D034500-CFF5-4BB7-9552-E304CE7584BF Q33848751-5AF5B574-7111-41AE-9BFB-C306B55E094D Q34017761-7E3BC342-0BB0-4645-804A-207FA246BE12 Q34021416-6EF804B5-0DA9-4648-BE75-AC094154A8E0 Q34055972-435D5F6E-9410-4859-9E2F-E6263E2E7BE5 Q34119006-5361EE5F-3ABB-4A5D-863A-AEA68D729E87 Q34199609-444D51FE-6222-4DFB-9EAF-1544DAC2F166 Q34398416-66B84186-7354-453A-9819-72E3A8492888 Q34625117-B2A56959-6211-4DCB-B8E1-6FB126587D14 Q34685630-044A3632-9635-4595-993C-062C7024E3DB Q34958828-92EB4175-77F4-4C67-8A5A-BBD2DFE691E9 Q34990414-DF509444-E851-4E12-BC1B-B971270225F7 Q35009815-A6DAE44E-B0FD-4763-BF97-B6A573C7BAAC Q35161187-0D03EF99-2E17-4BA4-958E-BE295120BCD6 Q35191051-B74EFAEB-6A4F-4E65-A39C-F5A3ECA28E99 Q35206022-C4256295-3E0B-408B-A412-A6A02E76F268 Q35227496-2916DC5B-7CC9-44EB-9F3F-2823EA705EBD Q35238349-3A06CF7A-DFAD-4D48-8681-82D0D1C3CC92 Q35764888-2989848A-966A-4A2D-8822-B3D29AB1B3C0 Q35895439-49A8AFFE-8BAB-4C45-82EB-922C5BA92AEA

P2860

Intracellular transport, assembly, and degradation of wild-type and disease-linked mutant gap junction proteins.

http://www.wikidata.org/entity/Q34719366

description

2000 nî lūn-bûn

@nan

2000 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Intracellular transport, assem ...... mutant gap junction proteins.

@ast

Intracellular transport, assem ...... mutant gap junction proteins.

@en

Intracellular transport, assem ...... mutant gap junction proteins.

@nl

type

label

Intracellular transport, assem ...... mutant gap junction proteins.

@ast

Intracellular transport, assem ...... mutant gap junction proteins.

@en

Intracellular transport, assem ...... mutant gap junction proteins.

@nl

prefLabel

Intracellular transport, assem ...... mutant gap junction proteins.

@ast

Intracellular transport, assem ...... mutant gap junction proteins.

@en

Intracellular transport, assem ...... mutant gap junction proteins.

@nl

P1433

Q34719366-0F03680C-24F5-4DA9-9F32-A15729EE26FA

P1476

Q34719366-021E3359-3E2E-40BE-9BFE-3FC5B4FF480E

P2093

Q34719366-67125F9A-3BC3-4A33-8104-11CB85FD5F92

Q34719366-6CCF80E8-064B-4DC9-A9A9-E7C0B92A64AA

Q34719366-96C7A93B-D8E3-4574-8003-6F84C9E7E2D1

P2860

Q34719366-0025B352-9548-46DB-B761-F0D983A42CDB

Q34719366-021293D8-7414-4AA7-A65E-24B4CB524EF6

Q34719366-04C36219-E90F-4F1B-9BFC-8BE435B81CB0

Q34719366-0E2B15ED-8D22-46DA-B7EC-4C418EF146DC

Q34719366-0E7CDDEB-CEE2-49F1-9F24-731B45581978

Q34719366-10C98206-F5EC-440E-9019-CF81C0FFD8F3

Q34719366-203CDD43-6C4D-464F-9837-1AE17BBFE92E

Q34719366-23351D47-0D98-417F-AC15-9ACA4D694322

Q34719366-293AABC3-6F19-4D20-BF7C-CA69B42BDF5F

Q34719366-2AAAB873-7A90-48D0-A27F-84A8BE4F8867

P304

Q34719366-4CAB7B11-46B6-4F61-815B-1223F8D94855

P31

Q34719366-0C776FA7-A618-4CA6-907F-BCFE0CB53BD0

P356

Q34719366-49138A05-6B80-40CB-A127-47207881524E

P433

Q34719366-0CAEB4AE-606C-4B42-9871-B71CA6162A33

P478

Q34719366-550DD537-1079-4C6A-B6C5-6BC63F7E0EDF

P577

Q34719366-A0651461-DA33-43D7-B902-6BB1E96EDD61

P698

Q34719366-BE6FC38D-0EF1-4429-986B-FBC2E59C7A68

P932

Q34719366-F450D2AA-533B-4523-B128-0355E44C9004

P356

P1433

Molecular Biology of the Cell

P1476

Intracellular transport, assem ...... mutant gap junction proteins.

@en

P2093

J K VanSlyke

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

L S Musil

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

S M Deschenes

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

P2860

Mutations in the human connexin gene GJB3 cause erythrokeratodermia variabilis

Connexin46 mutations in autosomal dominant congenital cataract.

A missense mutation in the human connexin50 gene (GJA8) underlies autosomal dominant "zonular pulverulent" cataract, on chromosome 1q

Structure, function and regulation of the vacuolar (H+)-ATPase

Connexin mutations in X-linked Charcot-Marie-Tooth disease

An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex

Brefeldin A: insights into the control of membrane traffic and organelle structure

Connexin 26 mutations in hereditary non-syndromic sensorineural deafness

Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

Connexin32 and X-linked Charcot-Marie-Tooth disease

P304

1933-1946

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

P31

scholarly article

P356

10.1091/MBC.11.6.1933

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

P433

6

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

P478

11

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

P577

2000-06-01T00:00:00Z

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

P698

10848620

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

P932

14894

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