HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.
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Selective targeting of the stress chaperome as a therapeutic strategyERK-regulated αB-crystallin induction by matrix detachment inhibits anoikis and promotes lung metastasis in vivo.Quantitative proteomic analysis shows differentially expressed HSPB1 in glioblastoma as a discriminating short from long survival factor and NOVA1 as a differentiation factor between low-grade astrocytoma and oligodendroglioma.iTRAQ Quantitative Proteomic Comparison of Metastatic and Non-Metastatic Uveal Melanoma TumorsA novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study.RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.Medical implications of understanding the functions of human small heat shock proteins.Comparative proteomics-network analysis of proteins responsible for ursolic acid-induced cytotoxicity in colorectal cancer cells.Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.Small heat shock proteins in ageing and age-related diseases.The growing world of small heat shock proteins: from structure to functions.Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer.Elevated expression of CRYAB predicts unfavorable prognosis in non-small cell lung cancer.Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides.The role of αB-crystallin in skeletal and cardiac muscle tissues.Effect of ovarian cancer ascites on SKOV-3 cells proteome: new proteins associated with aggressive phenotype in epithelial ovarian cancer.Heat shock proteins and cancer: intracellular chaperones or extracellular signalling ligands?The anti-cataract molecular mechanism study in selenium cataract rats for baicalin ophthalmic nanoparticles.Dysregulated chaperones associated with cell proliferation and negative apoptosis regulation in the uterine leiomyoma.
P2860
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P2860
HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
HspB1, HspB5 and HspB4 in Huma ...... Some of Their Client Proteins.
@en
type
label
HspB1, HspB5 and HspB4 in Huma ...... Some of Their Client Proteins.
@en
prefLabel
HspB1, HspB5 and HspB4 in Huma ...... Some of Their Client Proteins.
@en
P2860
P356
P1433
P1476
HspB1, HspB5 and HspB4 in Huma ...... Some of Their Client Proteins.
@en
P2093
André-Patrick Arrigo
Benjamin Gibert
P2860
P304
P356
10.3390/CANCERS6010333
P577
2014-02-07T00:00:00Z