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Molecular Oncology: Deciphering the Molecular Landscape of Cancer Treatment
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Molecular Oncology: Deciphering the Molecular Landscape of Cancer Treatment

A special issue of Genes (ISSN 2073-4425). This special issue belongs to the section "Molecular Genetics and Genomics".

Deadline for manuscript submissions: closed (25 October 2024) | Viewed by 3252

Special Issue Editors

Dr. Keiko Kawauchi

E-Mail Website
Guest Editor
Faculty of Frontiers of Innovative Research in Science and Technology (FIRST), Konan University, Kobe 658-8501, Hyogo, Japan
Interests: tumor suppressor; oncogene; signal transduction; actin cytoskeleton; mechanosignal transduction
Special Issues, Collections and Topics in MDPI journals
Dr. Kiyoshi Ohtani

E-Mail Website
Guest Editor
Department of Biomedical Sciences, School of Biological and Environmental Sciences, Kwansei Gakuin University, 1 Gakuen Uegahara, Sanda 669-1330, Hyogo, Japan
Interests: cancer cell biology; RB; E2F; ARF; p53
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Recent advances in molecular oncology have significantly extended prognosis through the development of targeted molecular therapies, diagnostic technologies, innovative gene therapy approaches, and the application of nucleic acid medicines. Despite these advances, the need for diverse therapeutic strategies remains critical for enhancing patient survival, given the complexities of achieving a complete cure with existing treatments.

This Special Issue aims to deepen our understanding of cancer by exploring the multifaceted interactions at the molecular level. It will focus on the molecular mechanisms involved in the initiation, progression, and treatment of cancer, emphasizing the dynamics of gene expression and subcellular structural changes in cancer cells and their microenvironment. Contributions may include original research papers and review articles discussing how factors such as fibroblasts influence cancer cell behaviors—proliferation, invasion, metastasis, and treatment response. Additionally, studies on cancer cell responses to therapeutic interventions, including gene therapy and nucleic acid medicines, and drug development are highly encouraged.

Dr. Keiko Kawauchi
Dr. Kiyoshi Ohtani
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Genes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2600 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • cancer
  • gene mutation
  • oncogene
  • tumor suppressor
  • metabolism
  • organelle
  • cytoskeleton
  • microenvironment
  • epigenetic regulation
  • gene expression
  • signal transduction
  • mechanosignal transduction
  • gene therapy
  • nucleic acid medicine

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Published Papers (2 papers)

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12 pages, 2371 KiB  
Article
Bioinformatic Analysis of Actin-Binding Proteins in the Nucleolus During Heat Shock
by Shinya Taniguchi, Takeru Torii, Toshiyuki Goto, Kohei Takeuchi, Rine Katsumi, Mako Sumida, Sunmin Lee, Wataru Sugimoto, Masaya Gessho, Katsuhiko Itoh, Hiroaki Hirata, Junji Kawakami, Daisuke Miyoshi and Keiko Kawauchi
Genes 2024, 15(12), 1580; https://doi.org/10.3390/genes15121580 - 9 Dec 2024
Cited by 1 | Viewed by 1370
Abstract
Background/Objectives: Actin plays a crucial role not only in the cytoplasm, but also in the nucleus, influencing various cellular behaviors, including cell migration and gene expression. Recent studies reveal that nuclear actin dynamics is altered by cellular stresses, such as DNA damage; however, [...] Read more.
Background/Objectives: Actin plays a crucial role not only in the cytoplasm, but also in the nucleus, influencing various cellular behaviors, including cell migration and gene expression. Recent studies reveal that nuclear actin dynamics is altered by cellular stresses, such as DNA damage; however, the effect of heat shock on nuclear actin dynamics, particularly in the nucleolus, remains unclear. This study aims to elucidate the contribution of nucleolar actin to cellular responses under heat shock conditions. Methods: Nuclear actin dynamics in response to heat shock were investigated using nAC-GFP, a GFP-tagged actin chromobody, to visualize nuclear actin in HeLa cells. Bioinformatic analyses were also performed. Results: Heat shock induced the reversible assembly of nAC-GFP in the nucleolus, with disassembly occurring upon recovery in a heat shock protein (Hsp) 70-dependent manner. Because the nucleolus, formed via liquid–liquid phase separation (LLPS), sequesters misfolded proteins under heat shock to prevent irreversible aggregation, we hypothesized that nucleolar actin-binding proteins might also be sequestered in a similar manner. Using several databases, we identified 47 actin-binding proteins localized in the nucleolus and determined the proportion of intrinsically disordered regions (IDRs) known to promote LLPS. Our analysis revealed that many of these 47 proteins exhibited high levels of IDRs. Conclusions: The findings from our bioinformatics analysis and further cellular studies may help elucidate new roles for actin in the heat shock response. Full article
(This article belongs to the Special Issue Molecular Oncology: Deciphering the Molecular Landscape of Cancer Treatment)
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9 pages, 1507 KiB  
Article
L-Histidine Modulates the Catalytic Activity and Conformational Changes of the HD3 Deoxyribozyme
by Nae Sakimoto, Hirofumi Imanaka, Elisa Tomita-Sudo, Tomoka Akita and Junji Kawakami
Genes 2024, 15(11), 1481; https://doi.org/10.3390/genes15111481 - 17 Nov 2024
Viewed by 1105
Abstract
Background/Objectives: Riboswitches are functional nucleic acids that regulate biological processes by interacting with small molecules, such as metabolites, influencing gene expression. Artificial functional nucleic acids, including deoxyribozymes, have been developed through in vitro selection for various catalytic functions. In a previous study, [...] Read more.
Background/Objectives: Riboswitches are functional nucleic acids that regulate biological processes by interacting with small molecules, such as metabolites, influencing gene expression. Artificial functional nucleic acids, including deoxyribozymes, have been developed through in vitro selection for various catalytic functions. In a previous study, an l-histidine-dependent deoxyribozyme was identified, exhibiting RNA cleavage activity in the presence of l-histidine resembling ribonuclease catalytic mechanisms. This study aims to clarify the role of l-histidine in the activity and structural formation of the l-histidine-dependent deoxyribozyme (HD), focusing on the binding properties and conformational changes of its derivative HD3. Methods: Conformational changes in HD3 were analyzed using circular dichroism (CD) under varying concentrations of l-histidine. Direct binding analysis was conducted using carbon-14 (14C)-labeled l-histidine and a liquid scintillation counter. The catalytic activity of HD3 in the presence of different l-histidine concentrations was measured. Results: The binding constant for l-histidine-induced conformational changes (Ka(CD)) was found to be 2.0 × 103 (M−1), whereas for catalytic activity (Ka(Rxn)) and scintillation counting (Ka(RI)), it was approximately 1.0 × 103 (M−1). Conclusions: l-Histidine plays an essential role in both the catalytic activity and structural formation of the HD3 deoxyribozyme. The consistent binding constants across different experimental methods highlight the significant contribution of l-histidine to the active folding of deoxyribozymes. Full article
(This article belongs to the Special Issue Molecular Oncology: Deciphering the Molecular Landscape of Cancer Treatment)
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