Targeting heat shock protein 27 (HspB1) interferes with bone metastasis and tumour formation in vivo.
about
Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular InflammationHuman small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an updateHeat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateExpression of the molecular chaperone αB-crystallin in infiltrating ductal breast carcinomas and the significance thereof: an immunohistochemical and proteomics-based strategy.Research on the efficacy of Celastrus Orbiculatus in suppressing TGF-β1-induced epithelial-mesenchymal transition by inhibiting HSP27 and TNF-α-induced NF-κ B/Snail signaling pathway in human gastric adenocarcinoma.Calreticulin expression in infiltrating ductal breast carcinomas: relationships with disease progression and humoral immune responses.The forkhead transcription factor FOXM1 promotes endocrine resistance and invasiveness in estrogen receptor-positive breast cancer by expansion of stem-like cancer cellsA Targetable Molecular Chaperone Hsp27 Confers Aggressiveness in Hepatocellular CarcinomaHeat Shock Proteins Promote Cancer: It's a Protection RacketPathology-dependent effects linked to small heat shock proteins expression: an updateHeat shock protein 27 is a potential indicator for response to YangZheng XiaoJi and chemotherapy agents in cancer cells.RAD51 inhibition in triple negative breast cancer cells is challenged by compensatory survival signaling and requires rational combination therapy.Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.Heat shock proteins in multiple myelomaRegulation of cytokinesis and its clinical significance.HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.Targeting the testis-specific heat-shock protein 70-2 (HSP70-2) reduces cellular growth, migration, and invasion in renal cell carcinoma cells.Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.Increased expression of HSP27 inhibits invasion and metastasis in human esophageal squamous cell carcinoma.Small heat shock proteins in ageing and age-related diseases.Exosomes in cancer theranostic: Diamonds in the rough.Upregulation of heat shock protein 27 confers resistance to actinomycin D-induced apoptosis in cancer cells.Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer.Introducing differential expression of human heat shock protein 27 in hepatocellular carcinoma: moving toward identification of cancer biomarker.The effects of Hsp90 expression alteration on spinal metastases of breast carcinoma.Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides.A randomized phase 2 study of a HSP27 targeting antisense, apatorsen with prednisone versus prednisone alone, in patients with metastatic castration resistant prostate cancer.A phase I dose-escalation study of apatorsen (OGX-427), an antisense inhibitor targeting heat shock protein 27 (Hsp27), in patients with castration-resistant prostate cancer and other advanced cancers.Prevalence and risk factors of bone metastasis and skeletal related events in patients with primary breast cancer in Japan.Heat shock proteins and cancer: intracellular chaperones or extracellular signalling ligands?Expression of Antioxidant Molecules and Heat Shock Protein 27 in Thyroid Tumors.HSP27 is required for invasion and metastasis triggered by hepatocyte growth factor.Hsp27 regulates epithelial mesenchymal transition, metastasis and proliferation in colorectal carcinoma
P2860
Q26738276-B85F11AC-D56C-4666-A319-03897FD8D1DFQ26999062-6B5A9C55-A125-42A8-A46E-9AFFF9995381Q28272905-C5DD4B59-6B07-46F0-87FC-CD12E1AF9025Q34413448-3F348835-60F8-412D-90C6-C8CC485AF108Q34515164-7A561E8C-3B87-4789-A704-828836DDA82AQ34555318-6398ED44-47FB-4F16-9570-A53ECCE6F769Q35000256-F07E8540-4A61-4D57-9788-8AAD451199B0Q36644350-D865F81C-6062-40FA-A4FD-A9EEAFEE0FD1Q37013952-63C1EF6A-55CD-4DA6-BCA4-B9B50D05C9D9Q37288545-7125034F-E156-4E0D-86AB-3B4B2371D21BQ37337809-A8B28820-0D55-48A5-8104-4CBF4C5873EAQ37644990-92AF599F-445D-4E85-B673-654C803EB396Q38108621-EAD352C9-70C8-4446-80FB-874B7FC1359CQ38199919-780AE210-B031-4988-9A6A-53AD1644396DQ38535644-6BBF83E6-CDAE-4D80-A1BF-D5585D274EBFQ38671885-4E2FE169-6132-4E5C-94B9-14565F9AF51CQ38957319-FF780EED-9968-4861-95ED-DA2C68F34F39Q38987805-4623A81D-CD77-40EF-B0C5-8EECB1ABE646Q39002648-664103A3-8421-496E-9579-8374A60D6916Q39078958-AC5232A4-4381-401B-A10C-737D16351B54Q39122582-A9681F01-C7E6-44F2-940A-9E43745443DFQ39126758-C8F87A37-CB23-4732-AC29-4F932AA6178DQ40615449-30061F7C-75C0-417A-A017-DE5BFA346BC5Q41515060-3491A316-F198-422B-804E-3C1F03FEE0E4Q46167922-D5510DBB-411F-47F6-B6A4-06DD1C90EE97Q46253811-23D24557-A1D6-4AAA-AC06-17A134FECF0BQ47282786-0322AF12-85E9-4EC8-8E72-3CF16FD7AE54Q47447879-525503A9-0A23-4A48-BCAB-607E92849C79Q48125689-14D0BC3E-0892-42FD-B9DA-EB1F23EB366DQ50567847-AFFB90EF-7351-4E4B-93CE-7B413987F376Q53150001-3E6CA072-D7D5-4CDB-9074-714019530F5CQ54245240-A452BC78-1D20-4E31-8699-451364F67B97Q58792082-FDFCB8F8-AD07-488F-B599-0CBC17D2C325
P2860
Targeting heat shock protein 27 (HspB1) interferes with bone metastasis and tumour formation in vivo.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@ast
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@en
type
label
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@ast
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@en
prefLabel
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@ast
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@en
P2093
P2860
P356
P1476
Targeting heat shock protein 2 ...... and tumour formation in vivo.
@en
P2093
A-P Arrigo
C Diaz-Latoud
D Goldschneider
J Fombonne
P Clézardin
P2860
P2888
P356
10.1038/BJC.2012.188
P407
P577
2012-05-24T00:00:00Z