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Heat shock 27kDa protein 1

HSP27, HSP25
The protein encoded by this gene is induced by environmental stress and developmental changes. The encoded protein is involved in stress resistance and actin organization and translocates from the cytoplasm to the nucleus upon stress induction. Defects in this gene are a cause of Charcot-Marie-Tooth disease type 2F (CMT2F) and distal hereditary motor neuropathy (dHMN). [provided by RefSeq, Oct 2008] (from NCBI)
Top mentioned proteins: HSP70, CAN, p38, V1a, HAD
Papers using HSP27 antibodies
The structure of native G-actin
Graceffa Philip, In Biochemistry Research International, 2009
... Full-length Hsp27 was prepared by bacterial expression and purification using the New England Biolabs IMPACT-CN intein system, as ...
Histone deacetylase inhibitors and neurodegenerative disorders: holding the promise.
Saks Valdur, In PLoS ONE, 2008
... Rabbit polyclonal anti-phospho-Hsp27 (Ser 15) antibody, rabbit polyclonal anti-Hsp27 antibody and horseradish peroxidase–conjugated secondary goat anti-rabbit IgG were purchased from Santa Cruz (Santa Cruz Biotechnology, Santa Cruz, CA, USA) ...
Regulation of p21Waf1 expression and TNFa biosynthesis by glutathione modulators in PMA induced-THP1 differentiation: Involvement of JNK and ERK pathways
Moens Ugo et al., In Journal of Molecular Signaling, 2006
... PhosphoSer-15 Hsp27 antibody was from Cell Signaling technology (cat ...
Polyethylenimine, a cost-effective transfection reagent.
Kampinga Harm, In PLoS ONE, 2005
... ERK2 (sc-1647) and Hsp27 (sc-1048) antibodies were from Santa Cruz Biotechnology, Other antibodies used were ...
Preclinical evaluation of a potent novel DNA-dependent protein kinase inhibitor NU7441
Costanzo Vincenzo et al., In The EMBO Journal, 2005
... The antibodies used were anti-human G6PD goat polyclonal (Abcam), anti-Hsp27 mouse monoclonal (Santa Cruz Biotechnology) for immunoprecipitation, anti-Hsp27 rabbit ...
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Papers on HSP27
Inhibition of heat shock protein 27 phosphorylation promotes sensitivity to 5-fluorouracil in colorectal cancer cells.
Kitagawa et al., Tokyo, Japan. In Oncol Lett, 31 Dec 2014
UNLABELLED: The aim of the present study was to investigate whether the inhibition of HSP27 phosphorylation, which affects certain cellular functions, modulates sensitivity to 5-fluorouracil (5-FU) in colorectal cancer cells.
Preanalytical variables and phosphoepitope expression in FFPE tissue: quantitative epitope assessment after variable cold ischemic time.
Neumeister et al., New Haven, United States. In Lab Invest, 24 Dec 2014
Some phosphorylated proteins, such as phospho-HSP27 and phospho-S6 RP, involved in post-translational modification and stress response pathways increased in expression or phosphorylation levels.
Simultaneous Quantification of Protein Phosphorylation Sites using Liquid Chromatography-Tandem Mass Spectrometry-Based Targeted Proteomics: A Linear Algebra Approach for Isobaric Phosphopeptides.
Chen et al., Nanjing, China. In J Proteome Res, 17 Dec 2014
Finally, we applied this approach to determine the phosphorylation stoichiometry of heat shock protein 27 (HSP27) at Ser78 and Ser82 in breast cancer cells and tissue samples.
Heat shock protein 27 phosphorylation in the proliferation and apoptosis of human umbilical vein endothelial cells induced by high glucose through the phosphoinositide 3‑kinase/Akt and extracellular signal‑regulated kinase 1/2 pathways.
Chen et al., Fuzhou, China. In Mol Med Report, 06 Dec 2014
UNLABELLED: In the present study, the effect of the heat shock protein 27 (HSP27) signaling pathway on the proliferation and apoptosis of human umbilical vein endothelial cells (HUVECs) induced by high glucose (HG) was investigated.
Differential impact of bortezomib on HL-60 and K562 cells.
Račay et al., Martin, Slovakia. In Gen Physiol Biophys, 04 Dec 2014
The relative resistance of K562 cells to bortezomib correlated well with significantly higher expression of HSP27, HSP70, HSP90α, HSP90β and GRP75 in these cells.
Chronic neuroprotective effects of low concentration lithium on SH-SY5Y cells: possible involvement of stress proteins and gene expression.
Croute et al., Toulouse, France. In Neural Regen Res, May 2014
Besides, western blot analysis of stress proteins (HSP27, HSP70, GRP78 and GRP94) showed an over-expression of two proteins: a 105 kDa protein which is a hyper-phosphorylated isoform of GRP94, and a 108 kDa protein which is a phosphorylated tetramer of HSP27.
Prognostic biomarkers in patients with resected cholangiocarcinoma: a systematic review and meta-analysis.
van Gulik et al., Amsterdam, Netherlands. In Ann Surg Oncol, Feb 2014
Other markers showed promising results in single studies, including HSP27, Akt, HDGF, MUC6, p16, p-4EBP1, S100A4, α-SMA, Keratin 903, and TROP2.
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.
Hisamitsu et al., Yangzhou, China. In Bmc Complement Altern Med, Dec 2013
Overexpression of heat shock protein 27 (HSP27) was performed by transfected with the recombinant retroviral expression plasmid.
The role of heat shock proteins in bladder cancer.
So et al., Vancouver, Canada. In Nat Rev Urol, Jul 2013
A combination of OGX-427 (an antisense oligonucleotide that targets HSP27), gemcitabine, and cisplatin is currently being investigated in a phase II trial of patients with advanced bladder cancer.
Peptide aptamers: tools to negatively or positively modulate HSPB1(27) function.
Arrigo et al., Lyon, France. In Philos Trans R Soc Lond B Biol Sci, Jun 2013
Human HSP27 (HSPB1) is a molecular chaperone sensor which, through dynamic changes in its phosphorylation and oligomerization, allows cells to adapt to changes in their physiology and/or mount a protective response to injuries.
Heat shock proteins 27, 40, and 70 as combinational and dual therapeutic cancer targets.
McAlpine et al., Sydney, Australia. In Bioorg Med Chem Lett, May 2013
Examples of efficacious strategies include the inhibition of hsp27, which prevents protein aggregation, controlling hsp40's role as an ATPase modulator, and inhibiting hsp70 from acting as a molecular chaperone.
HSPB1 gene polymorphisms predict risk of mortality for US patients after radio(chemo)therapy for non-small cell lung cancer.
Liao et al., Changsha, China. In Int J Radiat Oncol Biol Phys, 2012
results demonstrate significant associations between overall survival and SNPs in HSPB1 rs2868371 in USA patients with NSCLC after radio(chemo)therapy.
The protective roles of phosphorylated heat shock protein 27 in human cells harboring myoclonus epilepsy with ragged-red fibers A8344G mtDNA mutation.
Hsieh et al., Taiwan. In Febs J, 2012
our results demonstrate that p-HSP27 provides significant protection when cells are exposed to different stresses in the cell model of MERRF syndrome
Increased expression of heat shock protein 27 correlates with peritoneal metastasis in epithelial ovarian cancer.
Chen et al., Wuxi, China. In Reprod Sci, 2012
Data suggest that higher levels of HSP27 in tumor tissue from patients with epithelial ovarian cancer are associated with peritoneal metastasis; thus, tumor HSP27 level may be useful prognostic marker of poor survival.
p38MAPK suppresses chronic pancreatitis by regulating HSP27 and BAD expression.
Sakurai et al., Ōsaka, Japan. In Free Radic Biol Med, 2012
p38MAPK suppresses chronic pancreatitis by upregulating HSP27 expression and downregulating BAD expression.
A novel p.Glu175X premature stop mutation in the C-terminal end of HSP27 is a cause of CMT2.
Reilly et al., London, United Kingdom. In J Peripher Nerv Syst, 2012
we present a family with a novel mutation in the C-terminus of HSP27 (p.Glu175X) with a motor predominant distal neuropathy but with definite sensory involvement compatible with axonal Charcot-Marie-Tooth disease
Large potentials of small heat shock proteins.
Gusev et al., Moscow, Russia. In Physiol Rev, 2011
Ubiquitously expressed HSPB1 (HSP27) is involved in the control of protein folding and, when mutated, plays a significant role in the development of certain neurodegenerative disorders.
High-mobility group box 1 is essential for mitochondrial quality control.
Lotze et al., Pittsburgh, United States. In Cell Metab, 2011
We show that heat shock protein beta-1 (HSPB1 or HSP27) is the downstream mediator of this effect.
Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy.
Timmerman et al., New York City, United States. In Nat Genet, 2004
missense mutation in the gene encoding 27-kDa small heat-shock protein B1 (HSPB1, also called HSP27) that segregates in a family with Charcot-Marie-Tooth disease
Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27.
Saklatvala et al., Cambridge, United Kingdom. In Cell, 1994
An IL-1-stimulated protein kinase cascade resulting in phosphorylation of the small heat shock protein hsp27 has been identified in KB cells.
More papers using HSP27 antibodies
The PANTHER database of protein families, subfamilies, functions and pathways
Weiss Robert H et al., In Molecular Cancer, 2004
... Goat polyclonal Hsp-27 and rabbit polyclonal phospho-Hsp27 antibodies were obtained from Santa Cruz Biotechnology and used at a 1:1000 ...
Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein
Sugden Peter H. et al., In The Journal of Cell Biology, 1994
... The antibody to HSP25/27 (sc-1049) was from Santa Cruz Biotechnology Inc. ...
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