| HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells. | HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells.
Youn CK, Lee JH, Hariharasudhan G, Kim HB, Kim J, Lee S, Lim SC, Yoon SP, Park SG, Chang IY, You HJ., Free PMC Article | 04/16/2022 |
| HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I. | HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I.
Yang YX, Huang JP, Li SN, Li J, Ling T, Xie T, Xu LG. | 07/31/2021 |
| The Co-Chaperone HspBP1 Is a Novel Component of Stress Granules that Regulates Their Formation. | The Co-Chaperone HspBP1 Is a Novel Component of Stress Granules that Regulates Their Formation.
Mahboubi H, Moujaber O, Kodiha M, Stochaj U., Free PMC Article | 02/27/2021 |
| Circulating HspBp1 is associated with progression of HIV infection and can be used as a new marker to predict the prognosis and management of HIV infection | HspBP1 and anti-HspBP1 levels in the serum of HIV-infected individuals are associated to the disease progression.
Ceccin ADF, Souza APD, Hilário GT, Muller DM, Romão PRT, Rodrigues Junior LC. | 09/14/2019 |
| Findings indicate a critical role of HspBP1 in differential CHIP/Hsp70 activities in neuronal and glial cells and the greater neuronal vulnerability to misfolded proteins in neurodegenerative diseases. | Differential HspBP1 expression accounts for the greater vulnerability of neurons than astrocytes to misfolded proteins.
Zhao T, Hong Y, Yin P, Li S, Li XJ., Free PMC Article | 06/30/2018 |
| downregulation of Hsp70 and HspBP1 represents a unique feature of patients with preterm prelabor rupture of membranes | Expression profile of heat shock proteins in placental tissues of patients with preterm prelabor rupture of membranes and spontaneous preterm labor with intact membranes.
Dvorakova L, Ivankova K, Krofta L, Hromadnikova I. | 05/26/2018 |
| our results clearly show that HspBP1 acts as an endogenous negative regulator of HIV-1 gene-expression and replication by suppressing NF-kappaB-mediated activation of viral transcription. | HSP70 binding protein 1 (HspBP1) suppresses HIV-1 replication by inhibiting NF-κB mediated activation of viral gene expression.
Chaudhary P, Khan SZ, Rawat P, Augustine T, Raynes DA, Guerriero V, Mitra D., Free PMC Article | 07/30/2016 |
| Oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1. | Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1.
Chalova AS, Sudnitsyna MV, Semenyuk PI, Orlov VN, Gusev NB., Free PMC Article | 07/4/2015 |
| BAG-1M and HspBP1 had differential impacts on the dynamic composition of steroid receptor folding complexes | Hsp70 cochaperones HspBP1 and BAG-1M differentially regulate steroid hormone receptor function.
Knapp RT, Wong MJ, Kollmannsberger LK, Gassen NC, Kretzschmar A, Zschocke J, Hafner K, Young JC, Rein T., Free PMC Article | 09/20/2014 |
| shown that HspBP1 binds Tag7 in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7-Hsp70 complex | Extracellular HspBP1 inhibits formation of a cytotoxic Tag7-Hsp70 complex in vitro and in human serum.
Yashin DV, Dukhanina EA, Kabanova OD, Romanova EA, Lukyanova TI, Tonevitskii AG, Belogurov AA, Raynes DA, Sheludchenkov AA, Gnuchev NV, Guerriero V, Georgiev GP, Sashchenko LP. | 04/21/2012 |
| High gene expression of HspBP1 is associated with leukemia. | Heat-shock protein expression in leukemia.
Sedlackova L, Spacek M, Holler E, Imryskova Z, Hromadnikova I. | 01/29/2011 |
| HspBP1 may play a role in tumor (dys)regulation of chaperone proteins | Heat shock protein 70-binding protein 1 is highly expressed in high-grade gliomas, interacts with multiple heat shock protein 70 family members, and specifically binds brain tumor cell surfaces.
Graner MW, Raynes DA, Bigner DD, Guerriero V., Free PMC Article | 01/21/2010 |
| The two chaperones, HSP72 and HSPBP1, interact both physically and functionally, leading to the activation of th EGFR-ERK1/2 signalling pathway. | Extracellular HspBP1 and Hsp72 synergistically activate epidermal growth factor receptor.
Evdonin A, Kinev A, Tsupkina N, Guerriero V, Raynes DA, Medvedeva N. | 01/21/2010 |
| Results indicate that low HspBP1 expression could be a marker of tumor aggressiveness. | HspBP1 levels are elevated in breast tumor tissue and inversely related to tumor aggressiveness.
Souza AP, Albuquerque C, Torronteguy C, Frasson A, Maito F, Pereira L, Duval da Silva V, Zerwes F, Raynes D, Guerriero V, Bonorino C., Free PMC Article | 01/21/2010 |
| Our data suggest that HIP may prevent inclusion formation by facilitating the constitutive HSC70 refolding cycle and possibly by preventing aggregation. | HSP70 interacting protein prevents the accumulation of inclusions in polyglutamine disease.
Howarth JL, Glover CP, Uney JB., Free PMC Article | 01/21/2010 |
| Association between endogenous LAP2alpha and Hsp70 in non-transfected cells was confirmed by co-immunoprecipitation. | Lamina-associated polypeptide 2alpha forms complexes with heat shock proteins Hsp70 and Hsc70 in vivo.
Snyers L, Schöfer C. | 01/21/2010 |
| that HspBP1, by antagonizing the prosurvival activity of Hsp70, sensitizes tumor cells to cathepsin-mediated cell death. | Anticancer drugs up-regulate HspBP1 and thereby antagonize the prosurvival function of Hsp70 in tumor cells.
Tanimura S, Hirano AI, Hashizume J, Yasunaga M, Kawabata T, Ozaki K, Kohno M. | 01/21/2010 |
| Stress-induced heat shock protein 70 (Hsp70) effectively protects cells against ultraviol ray-induced apoptosis in melanocytes bu penetrating mitchondrial and lysosomal membranes. | Hsp70 protects against UVB induced apoptosis by preventing release of cathepsins and cytochrome c in human melanocytes.
Bivik C, Rosdahl I, Ollinger K. | 01/21/2010 |
| The results demonstrate that Hsp70 and HspBP1 are not coordinately regulated but provide evidence that an increase in the ratio of HspBP1 to Hsp70 correlates with apoptosis, in a similar way to reducing the amount of Hsp70. | Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression.
Gottwald E, Herschbach M, Lahni B, Miesfeld RL, Kunz S, Raynes DA, Guerriero V. | 01/21/2010 |
| Here, we report that upon the formation of huntingtin aggregates; endogenous cytosolic huntingtin, Hsc70/Hsp70 (heat shock protein and cognate protein of 70kDa) and syntaxin 1A become aggregate-centered. | Aggregate-centered redistribution of proteins by mutant huntingtin.
Swayne LA, Braun JE. | 01/21/2010 |
| HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR) and stimulates CFTR maturation. | The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.
Alberti S, Böhse K, Arndt V, Schmitz A, Höhfeld J., Free PMC Article | 01/21/2010 |
| Results report cooperative interactions involving Hsp70, Hsp40, and TPR1 that enhance Hsp70-dependent folding of chemically denatured substrates. | Cooperative interaction of Hsp40 and TPR1 with Hsp70 reverses Hsp70-HspBp1 complex formation.
Oh WK, Song J. | 01/21/2010 |
| BAG2 binds to the carboxyl terminus of Hsp70-interacting protein (CHIP) and provides a cochaperone-dependent regulatory mechanism for preventing unregulated ubiquitylation of misfolded proteins by CHIP | Regulation of the cytoplasmic quality control protein degradation pathway by BAG2.
Dai Q, Qian SB, Li HH, McDonough H, Borchers C, Huang D, Takayama S, Younger JM, Ren HY, Cyr DM, Patterson C. | 01/21/2010 |
| Detection of hsp70 may be used as the screening marker for diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer related lung cancer, and may supplement the diagnostic value of conventional cytology. | [Co-detection of P21, P53 and HSP70 and their possible role in diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer].
Lu QF, Bai M, Zhang HJ, Li JC, Xiao CF, Chen S, Wu TC. | 01/21/2010 |
| The cochaperone HspBP1 binds to and inhibits Hsp70 activity. | Inhibition of Hsp70 ATPase activity and protein renaturation by a novel Hsp70-binding protein.
Raynes DA, Guerriero V Jr. | 10/26/2005 |