Karakat Sabit
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Karakat Sabit has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Aiym Zhussipbekkyzy
Department of Biomedical Sciences, School of Medicine, Nazarbayev University, Astana 010000, Kazakhstan
1 shared publication - Assem Zhakupova
Department of Biomedical Sciences, School of Medicine, Nazarbayev University, Astana 010000, Kazakhstan
1 shared publication - Dilbara Balkybayeva
Department of Biomedical Sciences, School of Medicine, Nazarbayev University, Astana 010000, Kazakhstan
1 shared publication - Kamila Sagatbekova
Department of Biomedical Sciences, School of Medicine, Nazarbayaev University, Astana 010000, Kazakhstan
1 shared publication - Kamilla Khojayeva
Department of Biomedical Sciences, School of Medicine, Nazarbayev University, Astana, Kazakhstan
1 shared publication - Lucia Rossetti Lopes
Department of Pharmacology, Institute of Biomedical Sciences, University of Sao Paulo, Sao Paulo, Brazil
1 shared publication
Latest Publications
- Open Access
- 23 January 2026
- Published by MDPI AG in Biomedicines
- Vol. 14 (2) , 263
Targeting the Endoplasmic Reticulum Oxidoreductin-1 Alpha–Protein Disulfide Isomerase Redox Interface as a Therapeutic Strategy in Cancer
The endoplasmic reticulum (ER) is critical in aiding cells in ensuring that proteins are folded and processed correctly, particularly during stressful situations. ER oxidoreductin-1 alpha (ERO1α) is an enzyme that is responsible for the formation of disulfide bonds during protein folding, along with protein disulfide isomerase (PDI). This redox pathway is often highly upregulated in cancer cells, allowing tumors to survive harsh conditions such as hypoxia and nutrient deprivation. This review discusses the role of the ERO1α–PDI system in cancer development through the regulation of oxidative stress, redox homeostasis, and tumor plasticity. It further shows the therapeutic potential of interrupting the ERO1α–PDI axis, which could lead to protein misfolding; enhanced generation of reactive oxygen species (ROS); and, eventually, cancer cell death.
- 23 January 2026
- Published by MDPI AG in Biomedicines
- Vol. 14 (2) , 263
Open AccessTargeting the Endoplasmic Reticulum Oxidoreductin-1 Alpha–Protein Disulfide Isomerase Redox Interface as a Therapeutic Strategy in Cancer
The endoplasmic reticulum (ER) is critical in aiding cells in ensuring that proteins are folded and processed correctly, particularly during stressful situations. ER oxidoreductin-1 alpha (ERO1α) is an enzyme that is responsible for the formation of disulfide bonds during protein folding, along with protein disulfide isomerase (PDI). This redox pathway is often highly upregulated in cancer cells, allowing tumors to survive harsh conditions such as hypoxia and nutrient deprivation. This review discusses the role of the ERO1α–PDI system in cancer development through the regulation of oxidative stress, redox homeostasis, and tumor plasticity. It further shows the therapeutic potential of interrupting the ERO1α–PDI axis, which could lead to protein misfolding; enhanced generation of reactive oxygen species (ROS); and, eventually, cancer cell death.