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Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surfaceIdentification and Roles of Photosystem II Assembly, Stability, and Repair Factors in ArabidopsisProtein disulfide isomerases in neurodegeneration: from disease mechanisms to biomedical applicationsProtein folding and quality control in the ERStructural basis for heteromeric assembly and perinuclear organization of keratin filamentsEndoplasmic reticulum chaperones and their roles in the immunogenicity of cancer vaccinesResearch perspective: potential role of nitazoxanide in ovarian cancer treatment. Old drug, new purpose?Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signalingChanges in cell ultrastructure and inhibition of JAK1/STAT3 signaling pathway in CBRH-7919 cells with astaxanthinFrom structure to redox: The diverse functional roles of disulfides and implications in disease.Endocrine Imbalance Associated With Proteome Changes in Diabetes.A novel predicted calcium-regulated kinase family implicated in neurological disorders.Cystine-knot peptides targeting cancer-relevant human cytotoxic T lymphocyte-associated antigen 4 (CTLA-4).Requirements for mouse mammary tumor virus Rem signal peptide processing and functionThe garlic compound ajoene targets protein folding in the endoplasmic reticulum of cancer cells.Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells.Structural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion.ERManI (Endoplasmic Reticulum Class I α-Mannosidase) Is Required for HIV-1 Envelope Glycoprotein Degradation via Endoplasmic Reticulum-associated Protein Degradation PathwayCysteines in the stalk of the nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation.Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes.Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase for ovarian cancer treatment.Triggering the measles virus membrane fusion machinery.Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.Disulfide bonds in hepatitis C virus glycoprotein E1 control the assembly and entry functions of E2 glycoprotein.Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseHow early studies on secreted and membrane protein quality control gave rise to the ER associated degradation (ERAD) pathway: the early history of ERAD.CD4 and BST-2/tetherin proteins retro-translocate from endoplasmic reticulum to cytosol as partially folded and multimeric molecules.Stress sensing in plants by an ER stress sensor/transducer, bZIP28The mitochondrial translocator protein, TSPO, inhibits HIV-1 envelope glycoprotein biosynthesis via the endoplasmic reticulum-associated protein degradation pathway.The endoplasmic reticulum in cardiovascular health and disease.The endoplasmic reticulum and unfolded protein response in the control of mammalian recombinant protein production.The many functions of the endoplasmic reticulum chaperones and folding enzymes.HIV-1 Vpr increases Env expression by preventing Env from endoplasmic reticulum-associated protein degradation (ERAD).The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein.Cysteine Modifications in the Pathogenesis of ALS.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulumA Cysteine-Rich Protein Kinase Associates with a Membrane Immune Complex and the Cysteine Residues Are Required for Cell Death.Cellular compartmentation follows rules: The Schnepf theorem, its consequences and exceptions: A biological membrane separates a plasmatic from a non-plasmatic phase.Protein disulfide isomerases in the endoplasmic reticulum promote anchorage-independent growth of breast cancer cells.ALS-linked protein disulfide isomerase variants cause motor dysfunction.
P2860
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P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին 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
Disulfide bonds in ER protein folding and homeostasis
@ast
Disulfide bonds in ER protein folding and homeostasis
@en
Disulfide bonds in ER protein folding and homeostasis
@nl
type
label
Disulfide bonds in ER protein folding and homeostasis
@ast
Disulfide bonds in ER protein folding and homeostasis
@en
Disulfide bonds in ER protein folding and homeostasis
@nl
prefLabel
Disulfide bonds in ER protein folding and homeostasis
@ast
Disulfide bonds in ER protein folding and homeostasis
@en
Disulfide bonds in ER protein folding and homeostasis
@nl
P2860
P3181
P1476
Disulfide bonds in ER protein folding and homeostasis
@en
P2093
Linda M Hendershot
P2860
P304
P3181
P356
10.1016/J.CEB.2010.10.012
P407
P577
2011-04-01T00:00:00Z