Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf. - Wikidata - awgldk - TriplyDB

Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.

Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.

http://www.wikidata.org/entity/Q36890014

about

Orchestration of secretory protein folding by ER chaperones Acute ablation of PERK results in ER dysfunctions followed by reduced insulin secretion and cell proliferation.Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer.Neuroligin trafficking deficiencies arising from mutations in the alpha/beta-hydrolase fold protein family From Split to Sibenik: the tortuous pathway in the cholinesterase field Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.Dominant protein interactions that influence the pathogenesis of conformational diseases.UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum.A novel transgenic mouse model of growth plate dysplasia reveals that decreased chondrocyte proliferation due to chronic ER stress is a key factor in reduced bone growth.Defective protein folding and intracellular retention of thyroglobulin-R19K mutant as a cause of human congenital goiter Endoplasmic reticulum (ER) chaperone regulation and survival of cells compensating for deficiency in the ER stress response kinase, PERK The cholinesterase-like domain of thyroglobulin functions as an intramolecular chaperone.Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis.Importance of molecular genetic analysis in the diagnosis and classification of congenital hypothyroidism.

P2860

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P2860

Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf.

http://www.wikidata.org/entity/Q36890014

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2007 nî lūn-bûn

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Jaemin Lee

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Paul S Kim

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Peter Arvan

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Sen-Ichi Furudate

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Shekar Menon

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Sung-Eun Yoo

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Takashi Agui

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William A Abplanalp

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P2860

Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44

Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD)

ERAD: the long road to destruction

Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum

Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum

Unfolded protein response is involved in the pathology of human congenital hypothyroid goiter and rat non-goitrous congenital hypothyroidism

A single amino acid change in the acetylcholinesterase-like domain of thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog mouse: a model of human endoplasmic reticulum storage diseases

The mammalian unfolded protein response

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Quality control in the endoplasmic reticulum

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