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  • 1.
    Groza, Paula
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Kumari, Kanchan
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Destefanis, Eliana
    Department of Cellular, Computational and Integrative Biology (CIBIO), University of Trento, Italy.
    Williams, Chloe
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk och translationell biologi.
    Marchand, Virginie
    IMoPA (UMR7365), and INSERM, IBSLor (UMS2008/US40), Epitranscriptomics and RNA Sequencing Core Facility, University of Lorraine, France.
    Motorin, Yuri
    IMoPA (UMR7365), and INSERM, IBSLor (UMS2008/US40), Epitranscriptomics and RNA Sequencing Core Facility, University of Lorraine, France.
    Mateus, André
    Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen. Umeå universitet, Medicinska fakulteten, Molekylär Infektionsmedicin, Sverige (MIMS).
    Gilthorpe, Jonathan D.
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk och translationell biologi.
    Dassi, Erik
    Department of Cellular, Computational and Integrative Biology (CIBIO), University of Trento, Italy.
    Schott, Johanna
    Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, and Division of Biochemistry, Mannheim Institute for Innate Immunoscience (MI3), Mannheim Cancer Center (MCC), Medical Faculty Mannheim, Heidelberg University, Germany.
    Tuorto, Francesca
    Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, and Division of Biochemistry, Mannheim Institute for Innate Immunoscience (MI3), Mannheim Cancer Center (MCC), Medical Faculty Mannheim, Heidelberg University, Germany.
    Aguilo, Francesca
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Fibrillarin regulates oncogenic protein pools and ribosome protein composition in triple-negative breast cancerManuskript (preprint) (Annet vitenskapelig)
  • 2.
    Kar, Avishek
    et al.
    DNA Nanotechnology and Application Laboratory, CSIR-Institute of Minerals and Materials Technology, Bhubaneswar, India; Academy of Scientific and Innovative Research (AcSIR), Uttar Pradesh, Ghaziabad, India.
    Kumari, Kanchan
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). DNA Nanotechnology and Application Laboratory, CSIR-Institute of Minerals and Materials Technology, Bhubaneswar, India.
    Mishra, Sandip K.
    Cancer Biology Laboratory, Institute of Life Sciences, Bhubaneswar, India.
    Subudhi, Umakanta
    DNA Nanotechnology and Application Laboratory, CSIR-Institute of Minerals and Materials Technology, Bhubaneswar, India; Academy of Scientific and Innovative Research (AcSIR), Uttar Pradesh, Ghaziabad, India.
    Self-assembled DNA nanostructure containing oncogenic miRNA-mediated cell proliferation by downregulation of FOXO1 expression2022Inngår i: BMC Cancer, ISSN 1471-2407, E-ISSN 1471-2407, Vol. 22, nr 1, artikkel-id 1332Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    FOXO1 transcription factor not only limits the cell cycle progression but also promotes cell death as a tumor suppressor protein. Though the expression of FOXO1 is largely examined in breast cancer, the regulation of FOXO1 by miRNA is yet to be explored. In the current study, self-assembled branched DNA (bDNA) nanostructures containing oncogenic miRNAs were designed and transfected to the MCF7 cell line to decipher the FOXO1 expression. bDNA containing oncogenic miRNAs 27a, 96, and 182 synergistically downregulate the expression of FOXO1 in MCF7 cells. The down-regulation is evident both in mRNA and protein levels suggesting that bDNA having miRNA sequences can selectively bind to mRNA and inhibit translation. Secondly, the downstream gene expression of p21 and p27 was also significantly downregulated in presence of miR-bDNA nanostructures. The cell proliferation activity was progressively increased in presence of miR-bDNA nanostructures which confirms the reduced tumor suppression activity of FOXO1 and the downstream gene expression. This finding can be explored to design novel bDNA structures which can downregulate the tumor suppressor proteins in normal cells and induce cell proliferation activity to identify early-phase markers of cancer.

    Fulltekst (pdf)
    fulltext
  • 3.
    Kumari, Kanchan
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). CSIR-Institute of Minerals & Materials Technology, Odisha, India.
    Chainy, Gagan B. N.
    Subudhi, Umakanta
    Prospective role of thyroid disorders in monitoring COVID-19 pandemic2020Inngår i: Heliyon, E-ISSN 2405-8440, Vol. 6, nr 12, artikkel-id e05712Artikkel, forskningsoversikt (Fagfellevurdert)
    Abstract [en]

    COVID-19 pandemic has affected more than 200 countries and 1.3 million individuals have deceased within eleven months. Intense research on COVID-19 occurrence and prevalence enable us to understand that comorbidities play a crucial role in spread and severity of SARS-CoV-2 infection. Chronic kidney disease, diabetes,respiratory diseases and hypertension are among the various morbidities that are prevalent in symptomatic COVID-19 patients. However, the effect of altered thyroid-driven disorders cannot be ignored. Since thyroid hormone critically coordinate and regulate the major metabolism and biochemical pathways, this review is on the potential role of prevailing thyroid disorders in SARS-CoV-2 infection. Direct link of thyroid hormone with several disorders such as diabetes, vitamin D deficiency, obesity, kidney and liver disorders etc. suggests that the prevailing thyroid conditions may affect SARS-CoV-2 infection. Further, we discuss the oxidative stress-induced aging is associated with the degree of SARS-CoV-2 infection. Importantly, ACE2 protein which facilitates the host-cell entry of SARS-CoV-2 using the spike protein, are highly expressed in individuals with abnormal level of thyroid hormone. Altogether, we report that the malfunction of thyroid hormone synthesis may aggravate SARS-CoV-2 infection and thus monitoring the thyroid hormone may help in understanding the pathogenesis of COVID-19.

    Fulltekst (pdf)
    fulltext
  • 4.
    Kumari, Kanchan
    et al.
    Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
    Groza, Paula
    Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
    Aguilo, Francesca
    Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM). Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten).
    Regulatory roles of RNA modifications in breast cancer2021Inngår i: NAR Cancer, E-ISSN 2632-8674, Vol. 3, nr 3, artikkel-id zcab036Artikkel, forskningsoversikt (Fagfellevurdert)
    Abstract [en]

    Collectively referred to as the epitranscriptome, RNA modifications play important roles in gene expression control regulating relevant cellular processes. In the last few decades, growing numbers of RNA modifications have been identified not only in abundant ribosomal (rRNA) and transfer RNA (tRNA) but also in messenger RNA (mRNA). In addition, many writers, erasers and readers that dynamically regulate the chemical marks have also been characterized. Correct deposition of RNA modifications is prerequisite for cellular homeostasis, and its alteration results in aberrant transcriptional programs that dictate human disease, including breast cancer, the most frequent female malignancy, and the leading cause of cancer-related death in women. In this review, we emphasize the major RNA modifications that are present in tRNA, rRNA and mRNA. We have categorized breast cancer-associated chemical marks and summarize their contribution to breast tumorigenesis. In addition, we describe less abundant tRNA modifications with related pathways implicated in breast cancer. Finally, we discuss current limitations and perspectives on epitranscriptomics for use in therapeutic strategies against breast and other cancers.

    Fulltekst (pdf)
    fulltext
  • 5.
    Malla, Sandhya
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap. Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Kumari, Kanchan
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Martinez Gamero, Carlos
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Achour, Cyrinne
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Mermelekas, Georgios
    Science for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, 171 21, Solna, Sweden.
    Coege, Alba
    Center for Research in Molecular Medicine and Chronic Diseases (CIMUS), Universidade de Santiago de Compostela (USC)-Health Research Institute (IDIS), Santiago de Compostela, Spain.
    Guallar, Diana
    Center for Research in Molecular Medicine and Chronic Diseases (CIMUS), Universidade de Santiago de Compostela (USC)-Health Research Institute (IDIS), Santiago de Compostela, Spain; Department of Biochemistry and Molecular Biology, USC, Santiago de Compostela, Spain.
    Roman, Angel
    Department of Biochemistry, Molecular Biology and Genetics, University of Extremadura, Badajoz, Spain.
    Aguilo, Francesca
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    LSD1 interacts with CHD7 to regulate the chromatin landscape in mouse embryonic stem cellsManuskript (preprint) (Annet vitenskapelig)
    Abstract [en]

     

     

     

  • 6.
    Malla, Sandhya
    et al.
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Kumari, Kanchan
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Martinez Gamero, Carlos
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    García-Prieto, carlos A.
    Josep Carreras Leukaemia Research Institute, 08916 Barcelona, Spain .
    Álvarez-Errico3, Damiana
    Josep Carreras Leukaemia Research Institute, 08916 Barcelona, Spain .
    Stransky, Stephanie
    4Department of Biochemistry, Albert Einstein College of Medicine, 10461 Bronx, NY, USA.
    Caroli, Jonatan
    5Department of Biology and Biotechnology, University of Pavia, 27100 Pavia, Italy.
    Saiki, Paulina Avovome
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    Lai, Weiyi
    State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China.
    Lyu, Cong
    6State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China.
    Mattevi, Andrea
    Department of Biology and Biotechnology, University of Pavia, 27100 Pavia, Italy.
    Gilthorpe, Jonathan D.
    Umeå universitet, Medicinska fakulteten, Institutionen för integrativ medicinsk biologi (IMB).
    Wang, Hailin
    State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China.
    Sidoli, Simone
    4Department of Biochemistry, Albert Einstein College of Medicine, 10461 Bronx, NY, USA.
    Esteller, Manel
    Centro de Investigacion Biomedica en Red Cancer (CIBERONC, 28029 Madrid, Spain; Institucio Catalana de Recerca i Estudis Avançats (ICREA), Barcelona, Spain; Physiological Sciences Department, School of Medicine and Health Sciences, University of Barcelona (UB), Barcelona, Spain.
    Roman, Angel
    Department of Biochemistry, Molecular Biology and Genetics, University of Extremadura, Badajoz, 06071, Spain.
    Aguilo, Francesca
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). Umeå universitet, Medicinska fakulteten, Wallenberg centrum för molekylär medicin vid Umeå universitet (WCMM).
    The catalytic-independent function of LSD1 modulates the epigenetic landscape of mouse embryonic stem cellsManuskript (preprint) (Annet vitenskapelig)
  • 7.
    Samal, Rashmi R.
    et al.
    CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India; Academy of Scientific & Innovative Research (AcSIR), Uttar Pradesh, Ghaziabad, India.
    Kumari, Kanchan
    Umeå universitet, Medicinska fakulteten, Institutionen för molekylärbiologi (Medicinska fakulteten). CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India.
    Sahoo, Yashaswinee
    CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India.
    Mishra, Sandip K.
    Cancer Biology Laboratory, DBT-Institute of Life Sciences, Bhubaneswar, India.
    Subudhi, Umakanta
    CSIR-Institute of Minerals & Materials Technology, Bhubaneswar, India; Academy of Scientific & Innovative Research (AcSIR), Uttar Pradesh, Ghaziabad, India.
    Interaction of artemisinin protects the activity of antioxidant enzyme catalase: a biophysical study2021Inngår i: International Journal of Biological Macromolecules, ISSN 0141-8130, E-ISSN 1879-0003, Vol. 172, s. 418-428Artikkel i tidsskrift (Fagfellevurdert)
    Abstract [en]

    The major antioxidant enzyme catalase is downregulated and the enzyme activity is compromised in various disease conditions such as malarial and cancer. Hence, the restoration and protection of catalase is a promising therapeutic strategy in disease management. In the present study, for the first time we have demonstrated the protective role of well-known anti-malarial drug Artemisinin (ART) on the time and temperature-induced degradation of bovine liver catalase (BLC) activity. The findings at different time intervals and at higher temperature showed the protective role of ART on BLC activity. Molecular docking studies suggested specific binding of ART on BLC through heme group interface which was further supported by cyclic voltammetry and dynamic light scattering study. The stabilization of BLC in presence of ART was mediated through forming a BLC-ART complex with reduced and shifted electrochemical peak and increased hydrodynamic diameter. ART substantially prevents the temperature-induced reduction in α-helical content with simultaneous increment in other secondary structures like antiparallel, parallel, β-turn and random coils. Nevertheless, the protective role of ART was accepted from the enhanced thermal stability and increased Tm value of BLC in presence of ART at higher temperatures. Our results uncover the mechanism of interaction between ART with BLC and suggest the protective role of ART towards spatiotemporal alteration of BLC by preventing the structural and molecular change in BLC. Thus, the findings advocate ART as a potential therapeutic drug for diseases associated with reduced catalase activity.

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