Relevant bibliographies by topics / Y-Box binding protein 1 (YB-1)

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  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
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Academic literature on the topic 'Y-Box binding protein 1 (YB-1)'

Author: Grafiati
Published: 10 September 2021
Last updated: 14 February 2022

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Journal articles on the topic "Y-Box binding protein 1 (YB-1)"

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Eliseeva, I. A., E. R. Kim, S. G. Guryanov, L. P. Ovchinnikov, and D. N. Lyabin. "Y-box-binding protein 1 (YB-1) and its functions." Biochemistry (Moscow) 76, no. 13 (December 2011): 1402–33. http://dx.doi.org/10.1134/s0006297911130049.

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Matsumoto, Ken, Kimio J. Tanaka, and Masafumi Tsujimoto. "An Acidic Protein, YBAP1, Mediates the Release of YB-1 from mRNA and Relieves the Translational Repression Activity of YB-1." Molecular and Cellular Biology 25, no. 5 (March 1, 2005): 1779–92. http://dx.doi.org/10.1128/mcb.25.5.1779-1792.2005.

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ABSTRACT Eukaryotic Y-box proteins are nucleic acid-binding proteins implicated in a wide range of gene regulatory mechanisms. They contain the cold shock domain, which is a nucleic acid-binding structure also found in bacterial cold shock proteins. The Y-box protein YB-1 is known to be a core component of messenger ribonucleoprotein particles (mRNPs) in the cytoplasm. Here we disrupted the YB-1 gene in chicken DT40 cells. Through the immunoprecipitation of an epitope-tagged YB-1 protein, which complemented the slow-growth phenotype of YB-1-depleted cells, we isolated YB-1-associated complexes that likely represented general mRNPs in somatic cells. RNase treatment prior to immunoprecipitation led to the identification of a Y-box protein-associated acidic protein (YBAP1). The specific association of YB-1 with YBAP1 resulted in the release of YB-1 from reconstituted YB-1-mRNA complexes, thereby reducing the translational repression caused by YB-1 in the in vitro system. Our data suggest that YBAP1 induces the remodeling of YB-1-mRNA complexes.
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Naumenko, Konstantin N., Mariya V. Sukhanova, Loic Hamon, Tatyana A. Kurgina, Elizaveta E. Alemasova, Mikhail M. Kutuzov, David Pastré, and Olga I. Lavrik. "Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1." Biomolecules 10, no. 9 (September 16, 2020): 1325. http://dx.doi.org/10.3390/biom10091325.

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Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg2+. However, in contrast to an Mg2+-dependent reaction, the activation of PARP1 by YB-1 is accompanied by overall up-regulation of protein PARylation and shortening of the PAR polymer. Therefore, YB-1 and cation co-factors stimulated PAR synthesis in divergent ways. PARP1 autoPARylation in the presence of YB-1 as well as trans-PARylation of YB-1 are greatly affected by the type of damaged DNA, suggesting that PARP1 activation depends on the formation of a PARP1–YB-1–DNA ternary complex. An unstructured C-terminal part of YB-1 involved in an interaction with PAR behaves similarly to full-length YB-1, indicating that both DNA and PAR binding are involved in the stimulation of PARP1 activity by YB-1. Thus, YB-1 is likely linked to the regulation of PARylation events in cells via an interaction with PAR and damaged DNA.
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Bader, Andreas G., and Peter K. Vogt. "Inhibition of Protein Synthesis by Y Box-Binding Protein 1 Blocks Oncogenic Cell Transformation." Molecular and Cellular Biology 25, no. 6 (March 15, 2005): 2095–106. http://dx.doi.org/10.1128/mcb.25.6.2095-2106.2005.

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ABSTRACT The multifunctional Y box-binding protein 1 (YB-1) is transcriptionally repressed by the oncogenic phosphoinositide 3-kinase (PI3K) pathway (with P3K as an oncogenic homolog of the catalytic subunit) and, when reexpressed with the retroviral vector RCAS, interferes with P3K- and Akt-induced transformation of chicken embryo fibroblasts. Retrovirally expressed YB-1 binds to the cap of mRNAs and inhibits cap-dependent and cap-independent translation. To determine the requirements for the inhibitory role of YB-1 in P3K-induced transformation, we conducted a mutational analysis, measuring YB-1-induced interference with transformation, subcellular localization, cap binding, mRNA binding, homodimerization, and inhibition of translation. The results show that (i) interference with transformation requires RNA binding and a C-terminal domain that is distinct from the cytoplasmic retention domain, (ii) interference with transformation is tightly correlated with inhibition of translation, and (iii) masking of mRNAs by YB-1 is not sufficient to block transformation or to inhibit translation. We identified a noncanonical nuclear localization signal (NLS) in the C-terminal half of YB-1. A mutant lacking the NLS retains its ability to interfere with transformation, indicating that a nuclear function is not required. These results suggest that YB-1 interferes with P3K-induced transformation by a specific inhibition of translation through its RNA-binding domain and a region in the C-terminal domain. Potential functions of the C-terminal region are discussed.
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Lyabin, Dmitry N., Alexander N. Doronin, Irina A. Eliseeva, Gelena P. Guens, Ivan V. Kulakovskiy, and Lev P. Ovchinnikov. "Alternative Forms of Y-Box Binding Protein 1 and YB-1 mRNA." PLoS ONE 9, no. 8 (August 12, 2014): e104513. http://dx.doi.org/10.1371/journal.pone.0104513.

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Ke, Ben, Chuqiao Fan, Weiping Tu, and Xiangdong Fang. "The Role of Y-Box Binding Protein 1 in Kidney Injury: Friend or Foe?" Cellular Physiology and Biochemistry 46, no. 1 (2018): 314–21. http://dx.doi.org/10.1159/000488432.

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Y-box-binding protein 1 (YB-1) is a multifunctional protein involved in various cellular processes via the transcriptional and translational regulation of target gene expression. YB-1 promotes acute or chronic kidney injury through multiple molecular pathways; however, accumulating evidence suggests that significantly increased YB-1 levels are of great importance in renoprotection. In addition, YB-1 may contribute to obesity-related kidney disease by promoting adipogenesis. Thus, the role of YB-1 in kidney injury is complicated, and no comprehensive review is currently available. In this review, we summarise recent progress in our understanding of the function of YB-1 in kidney injury and provide an overview of the dual role of YB-1 in kidney disease. Moreover, we propose that YB-1 is a potential therapeutic target to restrict kidney disease.
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Meyer, Nicole, Anne Schumacher, Urs Coenen, Katja Woidacki, Hannah Schmidt, Jonathan A. Lindquist, Peter R. Mertens, and Ana C. Zenclussen. "Y-Box Binding Protein 1 Expression in Trophoblast Cells Promotes Fetal and Placental Development." Cells 9, no. 9 (August 22, 2020): 1942. http://dx.doi.org/10.3390/cells9091942.

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Y-box binding protein 1 (YB-1) is pivotal for the regulation of cancerogenesis and inflammation. However, its involvement in pregnancy processes such as fetal and placental development remains to be elucidated. We studied Ybx1 (YB-1)+/− heterozygous intercrossings and compared them to YB-1+/+ wild-type (WT) combinations. Additionally, we generated trophoblast-specific YB-1-deficient mice by pairing FVB Cyp19-Cre females to YB-1fl/fl males. YB-1fl/fl-paired FVB WT females served as controls. Serial in vivo ultrasound measurements were performed to assess fetal and placental parameters. After sacrificing the females, implantation and abortion rates were recorded, spiral artery (SA) remodeling was analyzed and fetal and placental weights were determined. Compared to YB-1+/+ counterparts, YB-1+/− females showed reduced implantation areas at gestation day (GD)10, insufficiently remodeled SAs at GD12, increased placental diameter/thickness ratios at GD14 and reduced placental and fetal weights at GD14. Compared to WT, Cyp19-Cre females with YB-1-deficient placentas showed reduced implantation areas at GD8, 10 and 12; decreased placental areas and diameters at GD10 and 12; diminished placental thicknesses at GD12; as well as reduced placental weights at GD12 and 14. In conclusion, our data suggest haploinsufficiency of YB-1 resulting in disturbed fetal and placental development. Moreover, we provide the first evidence for the relevance of trophoblast-specific YB-1 for placentation.
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Kohno, Kimitoshi, Hiroto Izumi, Takeshi Uchiumi, Megumi Ashizuka, and Michihiko Kuwano. "The pleiotropic functions of the Y-box-binding protein, YB-1." BioEssays 25, no. 7 (June 13, 2003): 691–98. http://dx.doi.org/10.1002/bies.10300.

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Yang, Xiao-Juan, Hong Zhu, Shi-Rong Mu, Wen-Juan Wei, Xun Yuan, Meng Wang, Yanchao Liu, Jingyi Hui, and Ying Huang. "Crystal structure of a Y-box binding protein 1 (YB-1)–RNA complex reveals key features and residues interacting with RNA." Journal of Biological Chemistry 294, no. 28 (June 3, 2019): 10998–1010. http://dx.doi.org/10.1074/jbc.ra119.007545.

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The Y-box binding protein 1 (YB-1) is a member of the cold shock domain (CSD) protein family and is recognized as an oncogenic factor in several solid tumors. By binding to RNA, YB-1 participates in several steps of posttranscriptional regulation of gene expression, including mRNA splicing, stability, and translation; microRNA processing; and stress granule assembly. However, the mechanisms in YB-1–mediated regulation of RNAs are unclear. Previously, we used both systematic evolution of ligands by exponential enrichment (SELEX) and individual-nucleotide resolution UV cross-linking and immunoprecipitation coupled RNA-Seq (iCLIP-Seq) analyses, which defined the RNA-binding consensus sequence of YB-1 as CA(U/C)C. We also reported that through binding to its core motif CAUC in primary transcripts, YB-1 regulates the alternative splicing of a CD44 variable exon and the biogenesis of miR-29b-2 during both Drosha and Dicer steps. To elucidate the molecular basis of the YB-1–RNA interactions, we report high-resolution crystal structures of the YB-1 CSD in complex with different RNA oligos at 1.7 Å resolution. The structure revealed that CSD interacts with RNA mainly through π–π stacking interactions assembled by four highly conserved aromatic residues. Interestingly, YB-1 CSD forms a homodimer in solution, and we observed that two residues, Tyr-99 and Asp-105, at the dimer interface are important for YB-1 CSD dimerization. Substituting these two residues with Ala reduced CSD's RNA-binding activity and abrogated the splicing activation of YB-1 targets. The YB-1 CSD–RNA structures presented here at atomic resolution provide mechanistic insights into gene expression regulated by CSD-containing proteins.
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Shiota, Masaki, Ario Takeuchi, YooHyun Song, Akira Yokomizo, Eiji Kashiwagi, Takeshi Uchiumi, Kentaro Kuroiwa, et al. "Y-box binding protein-1 promotes castration-resistant prostate cancer growth via androgen receptor expression." Endocrine-Related Cancer 18, no. 4 (June 7, 2011): 505–17. http://dx.doi.org/10.1530/erc-11-0017.

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The androgen receptor (AR) is well known to play a central role in the pathogenesis of prostate cancer (PCa). In several studies, AR was overexpressed in castration-resistant PCa (CRPC). However, the mechanism of AR overexpression in CRPC is not fully elucidated. Y-box binding protein-1 (YB-1) is a pleiotropic transcription factor that is upregulated in CPRC. We aimed to elucidate the role of YB-1 in castration resistance of PCa and identify therapeutic potential of targeting YB-1. Using immunohistochemistry, we found that nuclear YB-1 expression significantly correlated with the Gleason score and AR expression in PCa tissues. In PCa cells, YB-1 regulated AR expression at the transcriptional level. Furthermore, YB-1 expression and nuclear localization were upregulated in CRPC cells. Overexpression of AR, as well as YB-1, conferred castration-resistant growth in LNCaP and 22Rv1 cells. Conversely, knocking down YB-1 resulted in suppressed cell growth and induced apoptosis, which was more efficient than knocking down AR in LNCaP cells. In other types of PCa cells, such as CRPC cells, knocking down YB-1 resulted in a significant reduction of cell growth. In conclusion, these findings suggested that YB-1 induces castration resistance in androgen-dependent PCa cells via AR expression. Thus, YB-1 may be a promising therapeutic target for PCa, as well as CRPC.
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Dissertations / Theses on the topic "Y-Box binding protein 1 (YB-1)"

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Astanehe, Arezoo. "Role of Y-box binding protein-1 (YB-1) in breast cancer." Thesis, University of British Columbia, 2011. http://hdl.handle.net/2429/36668.

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The Y-box binding protein-1 (YB-1) is a multifunctional protein with roles in transcription, translation, DNA repair, and a recently identified function as an extracellular mitogen. YB-1 is over-expressed in various malignancies including breast carcinoma. Previous work from our laboratory has shown that YB-1 is expressed in approximately 40% of invasive breast carcinomas, and its expression correlates with relapse and poor survival. Further, the oncogenic potential of YB-1 has been demonstrated in breast cancer. In the studies presented in this thesis, we sought to understand the contribution of YB-1 as an oncogenic transcription factor to breast cancer. We focused our studies on the basal-like breast carcinoma (BLBC) and the human epidermal growth factor receptor 2 (HER2) over-expressing breast cancers, as patients with these subtypes suffer the worst prognosis. Using BLBC cell lines, we demonstrated that YB-1 induces expression of MET and PIK3CA to promote anchorage-independent growth and invasion respectively. These studies further identified YB-1 as a potential therapeutic target in BLBC. We then directed our focus to the HER2 over-expressing breast cancers. Although the development of trastuzumab (Herceptin®), a targeted therapy against HER2, has provided a substantial advance in the care of affected patients, resistance remains a prevailing challenge. We identified a novel mechanism by which signalling proteins, mitogen activated protein kinase interacting kinase (MNK) and p90 ribosomal S6 kinase (RSK), interact to increase phosphorylation of YB-1. In turn, phosphorylation of YB-1 promotes its nuclear translocation where it regulates transcription of genes involved in trastuzumab resistance. These results further suggest YB-1 as a therapeutic target to improve outcome for women with trastuzumab refractory disease. As a whole, the studies outlined in this thesis have contributed to our understanding of breast cancer pathogenesis and have identified novel aspects of YB-1 function in BLBC and in HER2 over-expressing breast carcinomas.
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EL-Naggar, Amal Mohammad. "Investigation into the role of Y-box binding protein-1 (YB-1) in childhood sarcomas." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/45665.

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Davies, Alastair Henry. "Dissecting the function of Y-box binding protein-1 (YB-1) during the development of breast cancer." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/44202.

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The series of events that trigger the transformation of a normal cell into a malignant cell are unclear. One prospective driver of tumourigenesis is Y-box binding protein-1 (YB-1). BLG-YB-1 transgenic mice all form mammary tumours and the protein is expressed in over 40% of breast carcinomas. The studies presented in this thesis aimed to uncover the function of YB-1 during the transformation process. To this end, we conditionally expressed YB-1 in normal human mammary epithelial cells (HMECs). In agreement with tumours from the transgenic mice, genomic instability was manifested in the form of numerical and structural chromosomal abnormalities. To query the mechanism responsible for these phenotypes, we assessed global changes in signal transduction using an antibody microarray. Notably, we identified an increase in LIM kinase (LIMK1/2) activity that acted as a catalyst for cytokinesis failure. Subsequent cell cycle checkpoint slippage, due to cyclin E over-expression, potentiated centrosome amplification leading to mitotic spindle abnormalities. The resulting genomic instability was not stochastic but rather it increased susceptibility to cancer by promoting low-level HER2 amplification, as one example. Deeper interrogation revealed that YB-1 was capable of fully transforming HMECs. Through stabilization and upregulation of the histone acetyltransferase p300, YB-1 reprogrammed HMECs into stem/progenitor-like tumour-initiating cells (TICs). Mechanistically, the relaxation of promoter-centered chromatin permitted YB-1 to bind and transcriptionally regulate the TIC-associated genes BMI1, CD44, and CD49f. These cells formed DCIS-like luminal outgrowths in a three-dimensional model of breast acini. Over time, pressures exerted by YB-1 led to the emergence of cells expressing RSK2 and hTERT that had the capacity to form tumours in vivo. These cells were subtyped as triple-negative breast cancer (TNBC), a particularly aggressive form of the disease that is prone to relapse. We discovered that YB-1 regulates the multidrug resistance transporter ABCG2 to render the CD44⁺/CD49f⁺ TIC subpopulation refractory to traditional chemotherapy. However, these cells were responsive to RSK inhibitors, which prevent the activation of YB-1. As a whole, the studies outlined in this thesis indicate that YB-1 facilitates the genesis of TNBC through epigenetic reprogramming and targeting it has the potential to overcome drug resistance and prevent tumour recurrence.
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Lee, Cathy. "Y-box binding protein-1 (YB-1) is essential for the growth and survival of HER-2 over-expressing breast cancer cells." Thesis, University of British Columbia, 2007. http://hdl.handle.net/2429/220.

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The human epidermal growth factor receptor (HER-2) is over-expressed in 20-30% of breast carcinomas and is a prognostic marker for poor patient outcome. We previously identified the transcription/translation factor Y-box binding protein-1 (YB-1) to be a novel substrate of AKT which binds to epidermal growth factor receptor (EGFR) and HER-2 promoters once phosphorylated (Wu J et al. 2006). YB-1 is over-expressed in approximately 40% of breast cancers; its expression is strongly correlated with HER-2 and is associated with poor patient survival. In order to gain a deeper understanding of the functional role of YB-1 in HER-2 over-expressing breast cancer, we silenced the expression of this factor in BT474-m1 and MDA-MB-453 cells. The loss of YB-1 inhibited the growth of BT474-m1 and MDA-MB-453 cells in monolayer and/or in soft agar. Consistent with this, we found a decrease in the expression of YB-1 responsive gene egfr and/or her-2 in BT474-m1 and MDA-MB-453 cells, which could begin to explain how growth is promoted by this factor. Furthermore, loss of YB-1 expression induced apoptosis in BT474-m1 cells. Beyond its role in tumor growth, YB-1 is also strongly linked to drug resistance. We therefore addressed whether it could play a part in Herceptin sensitivity. Herceptin is currently being used to treat patients with HER-2 positive breast cancer; however, only 30% of the patients respond to the therapy and many of them develop resistance within the first year of treatment. Therefore, it is of utmost importance to understand the biology of HER-2 over-expressing breast cancer to develop novel therapies that can benefit more patients. First we established that Herceptin inhibited BT474-m1 cell growth in anchorage-independent conditions whereas MDA-MB-453 cells were resistant to this treatment. We subsequently demonstrated that knock-down of YB-1 increased sensitivity of BT474-m1 cells to Herceptin while MDA-MB-453 cells failed to respond to the combination treatment. The mechanism for Herceptin resistance in MDA-MB-453 cells still remains elusive and requires further investigation. Thus far, we conclude that YB-1 is needed for the growth and survival of HER-2 positive BT474-m1 and MDA-MB-453 breast cancer cells by inducing members of the HER family.
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Mahomedy, Tephney Gladness. "Investigation of the Stress-Induced Nuclear Localisation of Retinoblastoma Binding Protein 6 (Rbbp6) and its Role in Ubiquitination Of Y-Box Binding Protein-1 (Yb-1)." University of the Western Cape, 2017. http://hdl.handle.net/11394/5900.

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Magister Scientiae - MSc (Biotechnology)
Retinoblastoma Binding Protein 6 (RBBP6) is a 200 kDa RING finger-containing human protein known to serve as an E3 ubiquitin ligase, and to play a role in ubiquitination and suppression of the tumour suppressor p53. It also regulates the stability of mRNA transcripts by modulating 3'-polyadenylation.
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Habibi, Golareh. "Y-box binding protein-1 (YB-1) is a bio-marker of aggressiveness in breast cancer and is a potential target for therapeutic intervention." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/911.

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Early detection is one of the most important factors for successful treatment of cancer. Currently, scientists are searching for molecular markers that can help identify and predict outcome and chance of recurrence in patients. In this study, we demonstratet he potential impact of Y-Box binding protein-1 (YB-1) as a marker of aggressiveness and cancer recurrence in breast malignancies by screening one of the largest tissue microarrays in North America. YB-1 is an oncogenic transcription/translation factor, which is over-expressed in the majority of malignancies, including breast cancer. In the cohort of 4049 primary breast tumours, we show that YB-1 is a strong marker of aggressiveness, poor survival and cancer recurrence in all subtypes of human breast cancer with a particularly high frequency of expression in the ER negative basal-like and HER-2 breast cancer subtypes. This suggests that targeting YB-1 may provide a new avenue for therapeutic intervention in these breast cancers that are currently challenging to treat. Cox regression multivariate analysis indicates that YB-1 is second only to nodal status as a strong independent prognostic marker for poor outcome and relapse compared to established clinico-pathological biomarkers, including tumour size, age, grade, ER and HER-2 status. This finding suggests that YB-1 has great potential to be in a priority list of biomarkers for identifying the patients with a higher risk of relapse and poor outcome. Subsequently, we find an association between YB-1 and urokinase Plasminogen Activator (uPA) expression in the basal-like subtype. We then show that YB-1 is involved in the regulation of uPA expression. More importantly, silencing YB-1 or uPA results in a significant reduction in cancer cell invasion. As there are no commercially available YB-linibitors we examine the efficacy of BMS-536924, a small molecule inhibitor for activated IGF-1R/IR on SUM149 cells. We demonstrate that activated IGF-1R is associated with poor survival in primary breast tumours and, that BMS-536924 reduces uPA expression through inhibition YB-1 in SUM149 cells. We therefore conclude that YB-1 is a bio-marker for poor survival and relapse. We also indicate that YB-1 has potential use as a molecular marker in a clinical setting. Inhibiting YB-1 may provide an ideal opportunity for targeted therapy in breast cancer.
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Alidousty, Christina [Verfasser]. "Die Regulation der CCL5-Expression in der Monozytendifferenzierung durch post-translationale Modifikation des Y-Box Binding Protein-1 (YB-1) / Christina Alidousty." Aachen : Hochschulbibliothek der Rheinisch-Westfälischen Technischen Hochschule Aachen, 2015. http://d-nb.info/107100820X/34.

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Chan, Man Kid. "The interaction between Y box binding protein 1 and DNA replication proteins." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=66802.

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A coordinated response to DNA damage is vital to maintain cellular viability and prevent the onset of disease. In mammalian cells, the intra-S phase checkpoint regulator, ATR (Ataxia-telangiectasia mutated and RAD3-related) kinase coordinates the response to DNA damage to ensure the genome is accurately and completely replicated before the cell enters mitosis. Y box Binding Protein 1 (YB-1), a transcription and translation factor, has previously been implicated in cell proliferation and the development of chemotherapeutic resistance. YB-1 has been linked to a wide variety of cellular stresses, but has not been studied in the context of DNA replication. In this study, we determined that YB-1 associates to both the β-globin replication origin (origin-containing) and the control (origin-lacking) DNA regions. This observation suggested that YB-1 may be involved in DNA replication elongation instead of initiation. By immunoprecipiating YB-1, we identified that PCNA and MCM7 preferentially interact with YB-1 during S phase. The examination of the spatial and temporal dynamics of these interactions by immunofluorescence microscopy, however, did not reveal nuclear colocalization of these proteins. By treating cells with hydroxyurea to stall the replication fork, we re-examined the protein-protein interaction between YB-1 and MCM7 and found that following 8 hours of hydroxyurea treatment, YB-1 and MCM7 exhibited diffuse colocalization in the cell nucleus. This finding may implicate YB-1 in exerting a late-onset response to prolonged replication fork arrest either directly at stalled replication forks or at "dormant" origins bound by MCM complexes. A number of roles for YB-1 can be postulated, such as the requirement of YB-1 in facilitating the resumption of DNA replication, or the activation of additional origins to duplicate the genome in the presence of a replication stress. This finding may in turn account fo
Une réponse coordonnée lors de dommages à l'ADN est vitale pour le maintien de la viabilité cellulaire et pour éviter l'installation de maladies. Dans les cellules de mammifères, le point de contrôle de la phase S, la protéine kinase ATR (Ataxia-telangiectasia mutated and RAD3-related), coordonne la réponse aux dommages de l'ADN afin d'assurer une réplication complète et fidèle du génome avant l'entrée en mitose. La protéine YB-1 (Y box Binding Protein 1), un facteur de transcription et de traduction, est impliqué dans la prolifération cellulaire et la résistance aux chimiothérapies. YB-1 est également lié à une large variété de stress cellulaires but aucune donnée n'est disponible quant à son rôle dans la réplication de l'ADN. Lors de mon travail de Master, j'ai pu montrer qu'YB-1 s'associe à la fois à l'origine de réplication de la β-globine et dans les régions contrôles de l'ADN. Ce résultat suggère qu'YB-1 pourrait être impliqué dans la phase d'élongation de la réplication de l'ADN plutôt que dans celui de l'initiation. Par immunoprécipitation, j'ai identifié PCNA et MCM7 comme interacteurs préférentiels d'YB-1 en phase S. Par contre, en immunofluorescence, je n'observe pas de colocalisation nucléaire entre ces protéines. Lors du blocage de la fourche de réplication par un traitement à l'hydroxyurée, l'interaction entre YB-1 et MCM7 a été réexaminée et j'ai mis en évidence que 8h après le traitement, ces deux protéines présentent une co-localisation diffuse dans le noyau. Ces données indiquent qu'YB-1 pourrait être impliqué dans une réponse tardive suite à un arrêt prolongé de la fourche de réplication soit directement au point d'arrêt soit au niveau d'origines « dormantes » liées aux complexes MCM. YB-1 peut donc avoir plusieurs rôles tels que l'aide à la reprise de la réplication de l'ADN ou l'activation d'origines de réplicatio
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Khandelwal, Payal. "The N-terminal domain of the Y-box binding protein YB-1 plays a major role in cell proliferation and apoptosis." View the abstract Download the full-text PDF version, 2008. http://etd.utmem.edu/ABSTRACTS/2008-016-Khandelwal-index.html.

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Thesis (Ph.D.)--University of Tennessee Health Science Center, 2008.
Title from title page screen (viewed on July, 31, 2008). Research advisor: Ramareddy V. Guntaka, Ph.D. Document formatted into pages (xiii, 111 p. : ill.). Vita. Abstract. Includes bibliographical references (p. 90-111).
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Nashchekin, Dmitri. "A Y-box protein/RNA helicase complex links mRNP assembly on the gene to mRNA translation /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-811-8/.

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Book chapters on the topic "Y-Box binding protein 1 (YB-1)"

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"TATA Box Binding Protein." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 1935. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_16708.

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"TRF1 (TATA-box-binding protein related factor)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 2026. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_17426.

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Kelaini, Sophia, Rachel Caines, Lingfang Zeng, and Andriana Margariti. "X-Box-Binding Protein 1 Splicing Induces an Autophagic Response in Endothelial Cells." In Autophagy: Cancer, Other Pathologies, Inflammation, Immunity, Infection, and Aging, 259–68. Elsevier, 2017. http://dx.doi.org/10.1016/b978-0-12-805420-8.00013-5.

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Keni, Jyotsna, and Anna Pawlikowska –. Haddal. "Growth Regulation." In Textbook of Endocrine Physiology. Oxford University Press, 2011. http://dx.doi.org/10.1093/oso/9780199744121.003.0014.

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While multiple hormones influence somatic growth, the main regulator of postnatal growth is growth hormone. Growth hormone (GH) is secreted in a pulsatile manner from the anterior pituitary primarily as a 22-kilodalton molecule (although other forms may be found). The development of the pituitary gland as well as GH gene expression is regulated by the multiple pituitary transcription factors listed in Table11-1. The Pit-1 and Prop-1 genes encode proteins that are often mutated or deleted in cases of congenital hypopituitarism. Under normal waking conditions, GH levels are often low or undetectable, but several times during the day, and particularly at night during stage 3 of sleep, surges of GH secretion occur. The pulsatile pattern characteristic of GH secretion largely reflects the interaction of multiple regulators, including two hypothalamic regulatory peptides: GH-releasing hormone (GHRH), which stimulates GH secretion, and somatostatin (somatotropin release–inhibiting factor [SRIF]), which inhibits GH secretion. Multiple neurotransmitters and neuropeptides are involved in regulation of release of these hypothalamic factors, including, but not limited to, serotonin, histamine, norepinephrine, dopamine, acetylcholine, γ -aminobutyric acid (GABA), thyroid-releasing hormone, vasoactive intestinal peptide, gastrin, neurotensin, substance P, calcitonin, neuropeptide Y, vasopressin, corticotropinreleasing hormone, and galanin. Many factors influence GH secretion; notably, glucose that inhibits, and certain amino acids and Ghrelin that stimulate GH secretion. GH secretion is also impacted by a variety of nonpeptide hormones, including androgens, estrogens, thyroxine, and glucocorticoids. The precise mechanisms by which these hormones regulate GH secretion are complex, potentially involving actions at both the hypothalamic and pituitary levels. Exogenous physiological and pharmacological factors are known to stimulate GH secretion. Some of these agents, including clonidine, L-dopa, and exercise, are used in GH stimulation tests. In plasma, the majority of GH is bound with high specificity and affinity, but with relatively low capacity to a carrier protein termed GH binding protein (GHBP). The GHBP is a cleavage product of the extracellular domain of the GH receptor.
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Milhé, C. "Determination by 1H NMR of a Slow Conformational Transition and Hydration Change in the Consensus TATAAT Prsbnow Box." In Biological NMR Spectroscopy. Oxford University Press, 1997. http://dx.doi.org/10.1093/oso/9780195094688.003.0027.

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The conformational dynamics and hydration of a DNA 14-mer containing the consensus Pribnow box sequence TATAAT have been measured using rotating frame T1 measurements and NOESY and ROESY in water. The H2 proton resonances of adenines show fast intermediate exchange behavior which can be attributed to a conformational transition that affects the distances between H2 protons of neighboring adenine residues, both sequential and cross-strand. The relaxation rate constant of the transition was measured at 4000s-1 at 25°C. Bound water close to the H2 proton of adenines was observed with residence times of >lns. At low temperature (5°C), the Pribnow box is in a closed state in which hydration water in the minor groove is tightly bound. At higher temperatures, the conformation opens up as judged by the increase in separation between sequential H2 protons of adenines and water exchanges freely from the minor groove. The conformational transition and the altered hydration pattern may be related to promoter function. The control of gene expression in procaryotes depends on the specific recognition by RNA polymerase of a six base-pair sequence (consensus: TTGACA) located at -35 from the transcription site, and a second one, named the Pribnow box (consensus: TATAAT) at about 10 base-pairs upstream the initiation site (Rosenberg and Court, 1979). It has been shown (Hawley and McClure, 1983) that strong promoters exhibit a high degree of homology with the consensus sequences, separated by an optimum consensus spacer length of 17 base pairs. The strength of a promoter depends on, among other thing, the rate of the initiation of transcription. This rate depends on the product between the thermodynamic and kinetic constants KB and k2 (McClure, 1980). The initial binding of RNA polymerase to the promoter results in the formation of a transcriptionally inactive ‘closed’ complex, characterized by the association constant KB. Isomerization to the active ‘open’ complex then occurs, and is characterized by the first order rate constant k2. Hence, the frequency of transcription initiation depends both on the strength of the polymerase-promoter interaction, and the ease with which this complex can isomerize to the productive state. Both of these events are likely to depend on the physical properties of the promoter.
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Conference papers on the topic "Y-Box binding protein 1 (YB-1)"

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Reipas, Kristen, Anna Stratford, Arezoo Astanehe, Kaiji Hu, and Sandra Dunn. "Abstract 506: Targeting Y-box binding protein-1 (YB-1) overcomes drug resistance in triple-negative breast cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-506.

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"Y-box-binding protein 1 as regulator of poly(ADP-ribose) polymerase 1 activity." In SYSTEMS BIOLOGY AND BIOINFORMATICS (SBB-2020). Institute of Cytology and Genetics, Siberian Branch of the Russian Academy of Sciences., 2020. http://dx.doi.org/10.18699/sbb-2020-26.

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Fotovati, Abbas, Sam Abu-Ali, Pei-Shan Wang, Loic Deleyrolle, Cathy Lee, Joanna Tricott, James Chen, et al. "Abstract LB-101: Y-box binding protein-1 (YB-1) inhibition triggers differentiation of normal and cancer stem cells from the brain." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-lb-101.

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Shibata, Tomohiro, Hiroto Izumi, Akihiko Kawahara, Satoshi Hattori, Chihiro Fukumitsu, Ryuji Takahashi, Kosuke Watari, et al. "Abstract LB-183: Y-box binding protein-1 YB-1 negatively regulates ERα expression accompanying by enhanced HER2/ErbB2 expression in breast cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-lb-183.

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Lim, Jia Pei, Sunitha Nair, Sukanya Shyamasundar, Jayantha Gunaratne, and Boon Huat Bay. "Abstract 1061: Advanced quantitative mass-spectrometry-based SILAC proteome profiling of Y-box binding protein-1 (YB-1) overexpressing breast cancer cells unravels proteins involved in metastasis." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1061.

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D'Costa, Ninadh M., Peter Raven, Zheng Tan, Werner Struss, Sebastian Frees, Claudia Chavez-Munoz, and Alan I. So. "Abstract 3080: Y-box binding protein 1 is crucial in acquiring drug resistance in advanced renal cell carcinoma." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3080.

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Yu, Yingnan, George Wai-Cheong Yip, Puay-Hoon Tan, Ken Matsumoto, Masafumi Tsujimoto, and Boon-Huat Bay. "Abstract 2248: The Y-box-binding protein 1 is associated with breast cancer progression and metastasis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2248.

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Veinotte, Chansey J., Dale Corkery, Graham Dellaire, Amal El-Naggar, Kirk Sinclair, Mark L. Bernstein, Poul B. Sorensen, and Jason N. Berman. "Abstract 1398: Using zebrafish xenotransplantation to study the role of Y-Box binding protein (YB-1) in the metastasis of Ewing family tumors." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1398.

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Guo, TianTian, Yingnan Yu, George Wai-Cheong Yip, Gyeong Hun Baeg, Aye Aye Thike, Puay-Hoon Tan, Ken Matsumoto, and Boon Huat Bay. "Abstract 47: Y-box binding protein 1 is correlated with lymph node metastasis in intestinal type of gastric cancer." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-47.

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Ito, T., S. Kamijo, H. Izumi, K. Kohno, and K.-I. Ito. "P4-01-15: Alteration of Y-box Binding Protein-1 Expression Modifies the Response to Endocrine Therapy in Estrogen Receptor Positive Breast Cancer." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p4-01-15.

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Reports on the topic "Y-Box binding protein 1 (YB-1)"

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Clarke, Robert. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2005. http://dx.doi.org/10.21236/ada446755.

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Clarke, Robert. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2006. http://dx.doi.org/10.21236/ada460787.

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Clarke, Robert R. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2003. http://dx.doi.org/10.21236/ada421992.

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Clarke, Robert R. X-Box Binding Protein-1 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, August 2004. http://dx.doi.org/10.21236/ada433869.

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Hu, Rong. Role of NF-Kappa B Signaling in X-Box Binding Protein 1 (XBP1)-Mediated Antiestrogen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2012. http://dx.doi.org/10.21236/ada569450.

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Hu, Rong. Role of NF-Kappa B Signaling in X-Box Binding Protein 1 (XBP1)-Mediated Antiestrogen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2011. http://dx.doi.org/10.21236/ada555915.

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Hu, Rong. Role of NF-Kappa B Signaling in X-Box Binding Protein 1 (XBP1)-Mediated Antiestrogen Resistance in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, October 2013. http://dx.doi.org/10.21236/ada594159.

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