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Heat shock 105kDa/110kDa protein 1

HSP110, HSP105, 105-kDa
Top mentioned proteins: HSP70, CAN, ACID, HAD, fibrillin-1
Papers on HSP110
Modulatory effect of betaine on expression dynamics of HSPs during heat stress acclimation in goat (Capra hircus).
Sarkar et al., Bareilly, India. In Gene, Feb 2016
When the groups were compared between different heat stress acclimatory phases, expression of all HSPs (HSP60, HSP70, HSP90 and HSP105/110) showed a similar pattern with a first peak on IHSA, reaching a basal level on STHSA followed by second peak on LTHSA.
Deficiency of heat shock transcription factor 1 suppresses heat stress-associated increase in slow soleus muscle mass of mice.
Goto et al., Toyohashi, Japan. In Acta Physiol (oxf), Dec 2015
On the other hand, heat stress upregulated heat shock proteins (HSPs) at the mRNA (HSP72) and protein (HSP72 and HSP110) levels in wild-type mice, but not in HSF1-null mice.
Localization of heat shock protein 110 in canine mammary gland tumors.
Sasai et al., Ōsaka, Japan. In Vet Immunol Immunopathol, Nov 2015
We previously confirmed that HSP110 is a canine mammary gland tumor antigen and reported that HSP110 mRNA expression significantly increased in tumor tissue.
Prophylactic Antitumor Effect of Mixed Heat Shock Proteins/Peptides in Mouse Sarcoma.
Peng et al., Beijing, China. In Chin Med J (engl), Sep 2015
Heat shock protein/peptides (HSP/Ps) are autoimmune factors that can induce both adaptive and innate immune responses; HSP/Ps isolated from tumors can induce antitumor immune activity when used as vaccines.
Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.
Bukau et al., Heidelberg, Germany. In Nature, Sep 2015
However, metazoans lack the key heat-shock protein disaggregase HSP100 of non-metazoan HSP70-dependent protein disaggregation systems, and the human HSP70 system alone, even with the crucial HSP110 nucleotide exchange factor, has poor disaggregation activity in vitro.
Co-evolutionary analysis implies auxiliary functions of HSP110 in Plasmodium falciparum.
Kumar et al., India. In Proteins, Aug 2015
We found that except HSP110, the parasite lost all other cytosolic nucleotide exchange factors essential for regulating HSP70 which is the centrum of the protein folding network.
Microsatellite instability: an update.
Imai et al., Kawasaki, Japan. In Arch Toxicol, Jun 2015
Moreover, microsatellite repeats in miRNA genes, such as hsa-miR-1273c, may be novel MSI targets for CRC, and mutations in noncoding regulatory regions of MRE11, BAX (BaxΔ2), and HSP110 (HSP110ΔE9) may affect the efficiency of chemotherapy.
Multi-layered molecular mechanisms of polypeptide holding, unfolding and disaggregation by HSP70/HSP110 chaperones.
Goloubinoff et al., Lausanne, Switzerland. In Front Mol Biosci, 2014
Members of the HSP70/HSP110 family (HSP70s) form a central hub of the chaperone network controlling all aspects of proteostasis in bacteria and the ATP-containing compartments of eukaryotic cells.
Extrapolation of Inter Domain Communications and Substrate Binding Cavity of Camel HSP70 1A: A Molecular Modeling and Dynamics Simulation Study.
Mohapatra et al., New Delhi, India. In Plos One, 2014
Heat shock protein 70 (HSP70) is an important chaperone, involved in protein folding, refolding, translocation and complex remodeling reactions under normal as well as stress conditions.
Protective mucosal immunity mediated by epithelial CD1d and IL-10.
Blumberg et al., Boston, United States. In Nature, 2014
Here we show in mice that whereas bone-marrow-derived CD1d signals contribute to NKT-cell-mediated intestinal inflammation, engagement of epithelial CD1d elicits protective effects through the activation of STAT3 and STAT3-dependent transcription of IL-10, heat shock protein 110 (HSP110; also known as HSP105), and CD1d itself.
Molecular and prognostic heterogeneity of microsatellite-unstable colorectal cancer.
Kang et al., Seoul, South Korea. In World J Gastroenterol, 2014
Here, we have reviewed and discussed the molecular and prognostic features of MSI-H CRCs, as well as several putative prognostic or predictive molecular markers, including HSP110 expression, beta2-microglobulin mutations, myosin 1a expression, CDX2/CK20 expression, SMAD4 expression, CIMP status and LINE-1 methylation levels.
Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels.
Wang et al., Toledo, United States. In J Biol Chem, 2012
The Hsp105-mediated multilevel regulation of DeltaF508 CFTR folding and quality control provides new opportunities to understand how chaperone machinery regulates the homeostasis and functional expression of misfolded proteins in the cell.
[Structure and function of HSP105 family proteins].
Saito et al., Kyoto, Japan. In Seikagaku, 2012
It restricts aggregation of denaturated proteins,plays a role in protein folding in cytoplasms,and enhance expression of hsp70 in cell nucleus.(review)
Serological identification of HSP105 as a novel non-Hodgkin lymphoma therapeutic target.
Di Nicola et al., Milano, Italy. In Blood, 2011
A direct correlation between HSP105 expression and lymphoma aggressiveness was also apparent.
Expression of a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy and improves disease prognosis.
Duval et al., Paris, France. In Nat Med, 2011
We identified a mutant of HSP110 (HSP110ΔE9) in colorectal cancer showing microsatellite instability (MSI CRC), generated from an aberrantly spliced mRNA and lacking the HSP110 substrate-binding domain.
Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells.
Hatayama et al., Kyoto, Japan. In Biochem Biophys Res Commun, 2011
Hsp105 may play an important role in the refolding of denatured proteins and protection against stress-induced cell death in mammalian cells.
Hsp105 reduces the protein aggregation and cytotoxicity by expanded-polyglutamine proteins through the induction of Hsp70.
Hatayama et al., Kyoto, Japan. In Exp Cell Res, 2010
Hsp105alpha and Hsp105beta suppressed the expanded polyQ tract-induced protein aggregation and apoptosis through the induction of Hsp70.
Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families.
Kampinga et al., Groningen, Netherlands. In Biochemistry, 2008
Here, we have reviewed the existing literature on the various members of the human HSPB (HSP27), HSPH (HSP110), HSPA (HSP70), and DNAJ (HSP40) families.
A postgenomic view of the heat shock proteins in kinetoplastids.
Requena et al., Madrid, Spain. In Fems Microbiol Rev, 2007
The HSP families described here are: HSP110, HSP104, group I chaperonins, HSP90, HSP70, HSP40 and small HSPs.
Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.
Lindquist et al., Chicago, United States. In Nature, 1991
The mammalian hsp110 protein is nucleolar and redistributes with growth state, nutritional conditions and heat shock.
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