Home / Advanced Search

  • Title/Keywords

  • Author/Affliations

  • Journal

  • Article Type

  • Start Year

  • End Year

Update SearchingClear
  • Articles
  • Online
Search Results (2)
  • Open Access

    ARTICLE

    Knockdown of RCN1 contributes to the apoptosis of colorectal cancer via regulating IP3R1

    XUAN SHI1,2, YUFEN WANG1, CHENYU LI1, WANGSHU FU3, XINYUE ZHANG3, AIXIA GONG1,*

    BIOCELL, Vol.48, No.5, pp. 835-845, 2024, DOI:10.32604/biocell.2024.048076

    Abstract Background: The incidence of colorectal cancer (CRC) has been increasing in recent years. Thus, the discovery of factors that can assist in alleviating CRC is urgently warranted. Methods: To identify a potential factor involved in the development of CRC, we screened the upregulated genes in tumor tissues through four datasets from an online database. The expression of reticulocalbin 1 (RCN1), a Ca-binding protein, was upregulated in the four datasets. Based on loss-of-function experiments, the effect of RCN1 on cell viability was assessed by Cell Counting Kit-8 (CCK-8) assay. The regulatory effect of RCN1 on apoptosis… More > Graphic Abstract

    Knockdown of RCN1 contributes to the apoptosis of colorectal cancer via regulating IP3R1

  • Open Access

    REVIEW

    ER exit pathways and the control of proteostasis: Crucial role of the UPR, COPII, and ER-phagy in the secretory pathway

    GIUSEPPINA AMODIO1, VALENTINA PAGLIARA1, PAOLO REMONDELLI1,*, ORNELLA MOLTEDO2

    BIOCELL, Vol.46, No.5, pp. 1131-1137, 2022, DOI:10.32604/biocell.2022.018638

    Abstract The endoplasmic reticulum (ER) is the site of entry of all proteins that function in the secretory pathway including the extracellular environment. Because it controls the folding of newly synthesized secretory proteins, the ER is indispensable for the maintenance of proteostasis in the secretory pathway. Within the ER and, in part, in post-ER compartments, the quality control of protein folding is under the regulation of the unfolded protein response (UPR) pathways. The UPR strategy is to enhance protein folding, increase the ER degradation pathway of misfolded proteins, and allow the exit from the ER of More >

Displaying 1-10 on page 1 of 2. Per Page