Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection. - Wikidata - awgldk - TriplyDB

Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection.

Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection.

http://www.wikidata.org/entity/Q37207734

about

Protein folding and quality control in the ER Sorting out the trash: the spatial nature of eukaryotic protein quality control Autophagy in cardiovascular biology The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology Autophagy in plasma cell pathophysiology On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein Tetrahydrohyperforin Inhibits the Proteolytic Processing of Amyloid Precursor Protein and Enhances Its Degradation by Atg5-Dependent Autophagy Collagen XXVII organises the pericellular matrix in the growth plate E3 ubiquitin ligase synoviolin is involved in liver fibrogenesis Enhanced lysosomal activity is involved in Bax inhibitor-1-induced regulation of the endoplasmic reticulum (ER) stress response and cell death against ER stress: involvement of vacuolar H+-ATPase (V-ATPase).Chemical chaperone treatment reduces intracellular accumulation of mutant collagen IV and ameliorates the cellular phenotype of a COL4A2 mutation that causes haemorrhagic stroke Megalencephalic leukoencephalopathy with subcortical cysts protein-1 modulates endosomal pH and protein trafficking in astrocytes: relevance to MLC disease pathogenesis Targeted induction of endoplasmic reticulum stress induces cartilage pathology.Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.Smoke exposure causes endoplasmic reticulum stress and lipid accumulation in retinal pigment epithelium through oxidative stress and complement activation.Interplay of substrate retention and export signals in endoplasmic reticulum quality control.Cellular strategies of protein quality control.Ultrastructural analysis in preclinical safety evaluation.Pulse-chase analysis of procollagen biosynthesis by azidohomoalanine labeling.Chaperoning osteogenesis: new protein-folding disease paradigms.Differential effects of rapamycin on rods and cones during light-induced stress in albino mice.Eucommia ulmoides Oliver extract, aucubin, and geniposide enhance lysosomal activity to regulate ER stress and hepatic lipid accumulation Chaperone Hsp47 Drives Malignant Growth and Invasion by Modulating an ECM Gene Network Endoplasmic reticulum stress or mutation of an EF-hand Ca(2+)-binding domain directs the FKBP65 rotamase to an ERAD-based proteolysis Ursolic acid attenuates diabetic mesangial cell injury through the up-regulation of autophagy via miRNA-21/PTEN/Akt/mTOR suppression The utility of mouse models to provide information regarding the pathomolecular mechanisms in human genetic skeletal diseases: The emerging role of endoplasmic reticulum stress (Review).Unbreak my heart: targeting mitochondrial autophagy in diabetic cardiomyopathy Endoplasmic Reticulum Stress in Heat- and Shake-Induced Injury in the Rat Small Intestine Autophagy promotes intracellular degradation of type I collagen induced by transforming growth factor (TGF)-β1.Reticulon Protein-1C: A New Hope in the Treatment of Different Neuronal Diseases.Impaired osteoblastogenesis in a murine model of dominant osteogenesis imperfecta: a new target for osteogenesis imperfecta pharmacological therapy.zVAD-fmk prevents cisplatin-induced cleavage of autophagy proteins but impairs autophagic flux and worsens renal function.Translational infidelity-induced protein stress results from a deficiency in Trm9-catalyzed tRNA modifications.The endoplasmic reticulum-associated degradation pathways of budding yeast.Hypertonic stress promotes autophagy and microtubule-dependent autophagosomal clusters Makings of a brittle bone: Unexpected lessons from a low protein diet study of a mouse OI model.The unfolded protein response and its relevance to connective tissue diseases.Evidence that autophagy, but not the unfolded protein response, regulates the expression of IL-23 in the gut of patients with ankylosing spondylitis and subclinical gut inflammation Lysosomal dysfunction and autophagy blockade contribute to IMB-6G-induced apoptosis in pancreatic cancer cells.

P2860

Q26823157-D1F2C81F-A321-416A-884A-B1819EC3777F Q26849685-4D2DC6EB-B2B0-4689-B61B-66B2F0216770 Q26866165-0A604605-994A-491F-9256-4AD1D23520DF Q27015793-F1289B48-BA29-4458-8C41-4BCE82A9447D Q27015920-7A638856-D591-4DB8-AFF9-26119E04A93A Q27022467-B4E65BCC-E16F-4D4F-AAAE-0C3EAC41EAAC Q28534369-13F5E5BA-0A43-48F7-9BD2-3855C6DCFE46 Q28547501-2DC22B61-E002-4921-BD1F-955352A93588 Q28594846-03AA22F4-1841-4454-8552-98806B7813BE Q28748731-5534C4E7-3CB9-46E9-A9E3-33B89447CF2D Q30502486-8B24EE02-41C6-4E5C-AD00-796DAB3848E7 Q30560237-D8B589B0-E561-4C6D-8626-DF33FAAB9D31 Q30577254-55F2D245-2121-4576-B3BD-83B43B83E9BB Q33510918-C7477E43-606B-4648-AC42-E39F914EB734 Q33597188-3B8A3422-B9CF-4ECD-844D-3C99884DAEB1 Q33652041-76D8642F-E6FA-45E2-B030-FDA950F7F2F0 Q33769005-B7BB2034-653A-4C19-886D-F8F444102B69 Q34199521-67F25CB8-E27F-4D47-A281-B185867CA8F7 Q34244280-93BD974B-46F0-450F-A01A-ACFFD893ADCC Q34626008-0B6223F6-6B34-426E-8398-EDAD9ADF6432 Q34672644-33F31349-0EE4-4188-B0CA-2A5AD52CE749 Q35027473-C23F0BCA-A7A8-4A3B-8AE2-4E2492EF90DF Q35069547-5C6B7554-3179-4B52-AD2C-81128AE38E43 Q35463568-FEE877F1-1318-4900-91DD-69AFF571CF4C Q35562258-55462B69-F8BE-45D4-A443-6484BC0B2A96 Q35562829-C712D36D-8F72-4F8F-BCCE-7270BF71CF17 Q35609918-C20B8D4D-7F5A-4ECE-B6A6-E2B7FC11D06B Q35667361-5F1466DE-82D5-4123-9092-7E7FA0AF5313 Q35860998-D49DC181-08EF-4FEF-A59B-30A4F3D5CAE0 Q35874334-342F7051-2D3A-4926-B5D7-1A19207883E9 Q36010989-06087AAC-BD65-476C-8664-0B0E48707E7D Q36282399-8D9F6DFC-8556-4F04-81A0-396F1EA33B48 Q36312626-1BB11891-058B-4773-B6A8-2F7FB639CD23 Q36391935-C4007BD4-20D0-4F48-B3FA-F7BCC929D1DE Q36418006-843540FA-8FDF-4681-9C93-4122A58196F5 Q36769706-1E3BD441-771B-4C82-80DD-9F38732FB204 Q37334366-E1782239-82CB-4219-BDA0-CDB91800F227 Q37444924-B8B465A3-D904-4A60-BCA1-B0FEA3D502B8 Q37445690-E69C8434-2C97-4A4A-A596-76C254ADA822 Q37615344-4D5D9FE9-6847-4C14-9EAB-5208C16A00F0

P2860

Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection.

http://www.wikidata.org/entity/Q37207734

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 08 April 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Autophagic elimination of misf ...... as a means of cell protection.

@en

Autophagic elimination of misf ...... as a means of cell protection.

@nl

type

label

Autophagic elimination of misf ...... as a means of cell protection.

@en

Autophagic elimination of misf ...... as a means of cell protection.

@nl

prefLabel

Autophagic elimination of misf ...... as a means of cell protection.

@en

Autophagic elimination of misf ...... as a means of cell protection.

@nl

P1433

Q37207734-AAF62FD9-9220-4CEC-9867-33FA154A2685

P1476

Q37207734-176C7C01-93A8-4AE6-9BA9-4E749223F4E9

P2093

Q37207734-4364BFF0-C932-4970-99D6-C854803CB4A3

Q37207734-A78C2908-935D-4D27-9D1E-62BDF7112E25

Q37207734-B6845346-072F-40A7-A3B8-7E63FB6425D3

Q37207734-BEF857C5-10C0-4E70-B76E-166D48ABA339

Q37207734-C565BBFD-0686-40AD-A62E-9079EF71E523

Q37207734-EF808A3B-186A-4B5D-8047-10C731868CAD

Q37207734-F2CC07AA-25FC-49A4-B54B-653C259D3985

P2860

Q37207734-00033059-A1E5-48D6-B85E-977533234413

Q37207734-02D9844B-4B4D-45A9-BF85-E4CF5F4608A1

Q37207734-0F76208F-834B-49C9-A4A0-40D7615DA687

Q37207734-0FA5FD50-473E-4C7A-BAED-AFE9A88772A1

Q37207734-1919BA79-4E54-438E-8EFC-2DE4D06A6CDF

Q37207734-1A508481-DC82-43AC-AFDC-9CCD770C1BEC

Q37207734-1DC7141D-4C80-4FE4-BF7B-FBCC96EDB1E7

Q37207734-20BCE1AA-8CB7-4DF8-823C-3FFB9F2AFD02

Q37207734-27967BBF-0F8A-41F3-8A8F-F0EF598D02A6

Q37207734-28B273F5-CB61-4224-A37D-6F1F9B8B2FF2

P304

Q37207734-81B204A8-EE51-4557-8D6A-C09E4A1B5BD2

P31

Q37207734-D6865E0E-83C9-4DBB-8160-AE597C1F419F

P356

Q37207734-4EDB210E-39D2-4880-B6A1-5E5195154E60

P433

Q37207734-D24C4949-6656-442F-99CD-59F6D9F6811B

P478

Q37207734-E69B6433-225C-4EF5-B8F5-59EABC36C0E8

P50

Q37207734-9BDD6048-4E55-4D90-A739-561DE8D3BA2D

P577

Q37207734-D1AA1086-0F05-4F7F-8D94-944D38FBD976

P698

Q37207734-1C37C19E-F930-4416-B975-74A3FC116ED3

P921

Q37207734-69E7DF8E-AE60-4FE0-B12D-5ED977E512FE

Q37207734-E64E365F-51B1-4FDD-8BC0-B8BB0E83C349

P932

Q37207734-3EE6323A-79B9-4FE9-84BC-F7270E3029F8

P356

MBC.E08-11-1092

P1433

Molecular Biology of the Cell

P1476

Autophagic elimination of misf ...... as a means of cell protection.

@en

P2093

Akira Kitamura

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

Akitsugu Yamamoto

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

Hiroshi Kubota

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

John F Bateman

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

Kazuhiro Nagata

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

Shireen R Lamandé

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

Yoshihito Ishida

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

P2860

Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes

Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice

Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

One step at a time: endoplasmic reticulum-associated degradation

Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells

Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis

Signal integration in the endoplasmic reticulum unfolded protein response

Autophagy fights disease through cellular self-digestion

EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

P304

2744-2754

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

P31

scholarly article

P356

10.1091/MBC.E08-11-1092

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

P433

11

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

P478

20

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

P50

Tamotsu Yoshimori

P577

2009-04-08T00:00:00Z

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

P698

19357194

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

P921

endoplasmic reticulum

P932

2688553

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