The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis
about
ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1Coupling endoplasmic reticulum stress to the cell death program: role of the ER chaperone GRP78Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress - SelS is a novel glucose-regulated proteinInhibition of ICMT induces endothelial cell apoptosis through GRP94Expression of the pro-angiogenic factors vascular endothelial growth factor and interleukin-8/CXCL8 by human breast carcinomas is responsive to nutrient deprivation and endoplasmic reticulum stressThe Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsTargeted mutation of the mouse Grp94 gene disrupts development and perturbs endoplasmic reticulum stress signalingDifferential expression of molecular chaperones in brain of patients with Down syndromeER chaperones in mammalian development and human diseasesHonokiol induces calpain-mediated glucose-regulated protein-94 cleavage and apoptosis in human gastric cancer cells and reduces tumor growthA matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid.The C-terminal domain of human grp94 protects the catalytic subunit of protein kinase CK2 (CK2alpha) against thermal aggregation. Role of disulfide bonds.Pyrvinium targets the unfolded protein response to hypoglycemia and its anti-tumor activity is enhanced by combination therapy.Proteomic mapping of cytosol-facing outer mitochondrial and ER membranes in living human cells by proximity biotinylationThe stress protein/chaperone Grp94 counteracts muscle disuse atrophy by stabilizing subsarcolemmal neuronal nitric oxide synthase.Alterations in molecular chaperones and eIF2alpha during lung endothelial cell apoptosisThe carboxy-terminal domain of Grp94 binds to protein kinase CK2 alpha but not to CK2 holoenzyme.The effect of drugs and toxins on the process of apoptosis.Astragalus saponins modulates colon cancer development by regulating calpain-mediated glucose-regulated protein expression.Liver-specific knockout of GRP94 in mice disrupts cell adhesion, activates liver progenitor cells, and accelerates liver tumorigenesis.Unraveling amyloid toxicity pathway in NIH3T3 cells by a combined proteomic and 1 H-NMR metabonomic approach.Targeted deletion of ER chaperone GRP94 in the liver results in injury, repopulation of GRP94-positive hepatocytes, and spontaneous hepatocellular carcinoma development in aged miceTaxane-derived compounds protect SK-N-SH cells against oxidative stress injury induced by H2O2.Endoplasmic reticulum stress and apoptosis.Proteome alteration induced by hTERT transfection of human fibroblast cells.A Human Variant of Glucose-Regulated Protein 94 That Inefficiently Supports IGF Production.The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivationNovel interactions of GRP78: UPR and estrogen responses in the brain.Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potentialProtein expression profiling of normal and neoplastic canine prostate and bladder tissue.Discovery of Molecular Therapeutics for Glaucoma: Challenges, Successes, and Promising Directions.Glucose-regulated protein 94 mediates metastasis by CCT8 and the JNK pathway in hepatocellular carcinoma.Do iron chelators increase the antiproliferative effect of trichostatin A through a glucose-regulated protein 78 mediated mechanism?GRP78 mediates cell growth and invasiveness in endometrial cancer.Glucose-regulated protein 94 modulates the therapeutic efficacy to taxane in cervical cancer cells.Grp94 acts as a mediator of curcumin-induced antioxidant defence in myogenic cells.Upregulation of GRP78 and GRP94 and its function in chemotherapy resistance to VP-16 in human lung cancer cell line SK-MES-1.A molecular chaperone glucose-regulated protein 94 blocks apoptosis induced by virus infection.Network-based analysis of calcium-binding protein genes identifies Grp94 as a target in human oral carcinogenesis.Calcium-dependent regulation of NEMO nuclear export in response to genotoxic stimuli.
P2860
Q22254333-F9386048-8A55-4458-A4A4-EA39A167A11FQ24293643-C86836E3-CAB4-4BC6-8010-290CADCB43ACQ24323792-91D9A018-71E6-40C3-A12E-6BCEF0F5A111Q24683861-E9E149F5-D689-48D8-8815-D7377CA3B574Q24797535-B765FFD6-AD42-45E0-9FEC-A4F6546265D2Q27026256-1703C02B-60A3-428E-B25E-02B25F42DC75Q27326154-BB23A349-1FCA-47CF-B34A-445E3E351841Q28189535-E585153D-434E-4670-B4B8-2C3BEC74EB82Q28300625-A23CEF86-057F-4E2B-BAFA-1238F01DFA4AQ28469331-B4255AFA-4CC4-4842-8A9C-D8D6E15749AAQ30817232-2DCB8796-5593-4B39-937A-D141B5955FC0Q31896731-97C4A7E9-A051-4233-8396-6291D7C58E74Q33392721-3DF43CAE-3462-43D3-BDCB-AFCECB6C0A63Q33603020-D25F500E-5807-4347-86A4-64FA37394692Q33630112-B9C9D435-49F2-467C-A8DB-AA2A99B7E1DDQ33784115-8B7A38F1-2425-444C-862A-B7FCD643E7D6Q34091249-854227B8-B176-471D-81A6-E8C93DAE343AQ34346312-2A7ACDBD-E079-4151-9DC1-70406DA0AB7CQ34410183-D408A13A-CD16-4B49-9459-3AF020FBB7B4Q34426580-EFAAD9A5-ACF7-4AE7-95CA-DA353BA8DD32Q34495047-993534C4-378C-4992-9212-8DAB639CA305Q34529312-08F503AC-9D58-4938-8110-ACE36A2FE674Q36318778-34ECC686-D944-470F-B8AA-12A723ABCB79Q36594912-FEDC8A9C-1DC8-4FA6-9914-17B32120355FQ36661483-2200EF11-CB9B-4772-BA42-957653C3E704Q36911625-13BD5A2D-6510-4988-9146-BD25B1922054Q37127277-0189058E-7AD7-485E-B93C-145007CC69D2Q38089680-4AD573D1-93FF-4902-A03C-3C3E5EF93AADQ38198491-AF8633C6-9497-41FF-B88D-A02A8C3FB48DQ38462349-929336F5-B7A6-4971-A9C5-6A62EE948A41Q38584194-0A5D6F70-A0A1-4466-80F3-62FED3B64B8AQ38807896-403E4DAE-0578-408E-BAD9-EEDE2383E7A8Q39016184-C68469D9-9508-4213-AF45-6A49EC2D540FQ39024022-0F5B5DC1-0D80-40AF-B208-99595EDA8BC9Q39113189-A6D71B4D-F981-4407-9F1F-F8EC90F984ACQ39689699-233B6182-E88A-454C-8CFD-BCAB0E495924Q39884411-27BC3036-4BDB-4B46-95A6-9A2B30A3FC40Q40013272-8F0864BD-8677-4F77-B50A-6B4D3F9780A4Q40088141-A4BF94A5-C140-4A25-9B52-14888DB9534CQ40214079-E63423FE-338F-4E13-B8DC-74625598119B
P2860
The endoplasmic reticulum chaperone glycoprotein GRP94 with Ca(2+)-binding and antiapoptotic properties is a novel proteolytic target of calpain during etoposide-induced apoptosis
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@ast
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en-gb
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@nl
type
label
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@ast
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en-gb
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@nl
prefLabel
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@ast
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en-gb
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@nl
P2860
P921
P356
P1476
The endoplasmic reticulum chap ...... ng etoposide-induced apoptosis
@en
P2860
P304
28476-28483
P356
10.1074/JBC.274.40.28476
P407
P50
P577
1999-10-01T00:00:00Z