The Experts below are selected from a list of 579 Experts worldwide ranked by ideXlab platform
Hong Yang - One of the best experts on this subject based on the ideXlab platform.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Lanqin Wu, Jinan Feng, Yuanlin Qi, Xinrui Wang, Enrun Zheng, Wei Wang, Cheng Yu, Yan He, Yan Xu, Hong YangAbstract:Background Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Yingying Lin, Jinan Feng, Xinrui Wang, Enrun Zheng, Wei Wang, Qiaofa Lin, Wanyan Shi, Zhenzhu Hou, Hanbin Lin, Hong YangAbstract:Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation. The immunoprecipitation was used to determine the interaction between OTUD1 and MCL1. The ubiquitination assays was performed to determine the regulation of MCL1 by OTUD1. The cell viability was used to determine the regulation of BH3-mimetic inhibitor induced cell death by OTUD1. The survival analysis was used to determine the relationship between OTUD1 expression levels and the survival rate of cancer patients. By screening a DUB expression library, we determined that the deubiquitinating enzyme OTUD1 regulates MCL1 protein stability in an enzymatic-activity dependent manner. OTUD1 interacts with MCL1 and promotes its deubiquitination. Knockdown of OTUD1 increases the sensitivity of tumour cells to the BH3-mimetic inhibitor ABT-263, while overexpression of OTUD1 increases tumour cell tolerance of ABT-263. Furthermore, bioinformatics analysis data reveal that OTUD1 is a negative prognostic factor for liver cancer, ovarian cancer and specific subtypes of breast and cervical cancer. The deubiquitinating enzyme OTUD1 antagonizes BH3-mimetic inhibitor induced cell death through regulating the stability of the MCL1 protein. Thus, OTUD1 could be considered as a therapeutic target for curing these cancers.
Enrun Zheng - One of the best experts on this subject based on the ideXlab platform.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Lanqin Wu, Jinan Feng, Yuanlin Qi, Xinrui Wang, Enrun Zheng, Wei Wang, Cheng Yu, Yan He, Yan Xu, Hong YangAbstract:Background Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Yingying Lin, Jinan Feng, Xinrui Wang, Enrun Zheng, Wei Wang, Qiaofa Lin, Wanyan Shi, Zhenzhu Hou, Hanbin Lin, Hong YangAbstract:Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation. The immunoprecipitation was used to determine the interaction between OTUD1 and MCL1. The ubiquitination assays was performed to determine the regulation of MCL1 by OTUD1. The cell viability was used to determine the regulation of BH3-mimetic inhibitor induced cell death by OTUD1. The survival analysis was used to determine the relationship between OTUD1 expression levels and the survival rate of cancer patients. By screening a DUB expression library, we determined that the deubiquitinating enzyme OTUD1 regulates MCL1 protein stability in an enzymatic-activity dependent manner. OTUD1 interacts with MCL1 and promotes its deubiquitination. Knockdown of OTUD1 increases the sensitivity of tumour cells to the BH3-mimetic inhibitor ABT-263, while overexpression of OTUD1 increases tumour cell tolerance of ABT-263. Furthermore, bioinformatics analysis data reveal that OTUD1 is a negative prognostic factor for liver cancer, ovarian cancer and specific subtypes of breast and cervical cancer. The deubiquitinating enzyme OTUD1 antagonizes BH3-mimetic inhibitor induced cell death through regulating the stability of the MCL1 protein. Thus, OTUD1 could be considered as a therapeutic target for curing these cancers.
Jinan Feng - One of the best experts on this subject based on the ideXlab platform.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Lanqin Wu, Jinan Feng, Yuanlin Qi, Xinrui Wang, Enrun Zheng, Wei Wang, Cheng Yu, Yan He, Yan Xu, Hong YangAbstract:Background Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Yingying Lin, Jinan Feng, Xinrui Wang, Enrun Zheng, Wei Wang, Qiaofa Lin, Wanyan Shi, Zhenzhu Hou, Hanbin Lin, Hong YangAbstract:Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation. The immunoprecipitation was used to determine the interaction between OTUD1 and MCL1. The ubiquitination assays was performed to determine the regulation of MCL1 by OTUD1. The cell viability was used to determine the regulation of BH3-mimetic inhibitor induced cell death by OTUD1. The survival analysis was used to determine the relationship between OTUD1 expression levels and the survival rate of cancer patients. By screening a DUB expression library, we determined that the deubiquitinating enzyme OTUD1 regulates MCL1 protein stability in an enzymatic-activity dependent manner. OTUD1 interacts with MCL1 and promotes its deubiquitination. Knockdown of OTUD1 increases the sensitivity of tumour cells to the BH3-mimetic inhibitor ABT-263, while overexpression of OTUD1 increases tumour cell tolerance of ABT-263. Furthermore, bioinformatics analysis data reveal that OTUD1 is a negative prognostic factor for liver cancer, ovarian cancer and specific subtypes of breast and cervical cancer. The deubiquitinating enzyme OTUD1 antagonizes BH3-mimetic inhibitor induced cell death through regulating the stability of the MCL1 protein. Thus, OTUD1 could be considered as a therapeutic target for curing these cancers.
Wei Wang - One of the best experts on this subject based on the ideXlab platform.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Lanqin Wu, Jinan Feng, Yuanlin Qi, Xinrui Wang, Enrun Zheng, Wei Wang, Cheng Yu, Yan He, Yan Xu, Hong YangAbstract:Background Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Yingying Lin, Jinan Feng, Xinrui Wang, Enrun Zheng, Wei Wang, Qiaofa Lin, Wanyan Shi, Zhenzhu Hou, Hanbin Lin, Hong YangAbstract:Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation. The immunoprecipitation was used to determine the interaction between OTUD1 and MCL1. The ubiquitination assays was performed to determine the regulation of MCL1 by OTUD1. The cell viability was used to determine the regulation of BH3-mimetic inhibitor induced cell death by OTUD1. The survival analysis was used to determine the relationship between OTUD1 expression levels and the survival rate of cancer patients. By screening a DUB expression library, we determined that the deubiquitinating enzyme OTUD1 regulates MCL1 protein stability in an enzymatic-activity dependent manner. OTUD1 interacts with MCL1 and promotes its deubiquitination. Knockdown of OTUD1 increases the sensitivity of tumour cells to the BH3-mimetic inhibitor ABT-263, while overexpression of OTUD1 increases tumour cell tolerance of ABT-263. Furthermore, bioinformatics analysis data reveal that OTUD1 is a negative prognostic factor for liver cancer, ovarian cancer and specific subtypes of breast and cervical cancer. The deubiquitinating enzyme OTUD1 antagonizes BH3-mimetic inhibitor induced cell death through regulating the stability of the MCL1 protein. Thus, OTUD1 could be considered as a therapeutic target for curing these cancers.
Xinrui Wang - One of the best experts on this subject based on the ideXlab platform.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Lanqin Wu, Jinan Feng, Yuanlin Qi, Xinrui Wang, Enrun Zheng, Wei Wang, Cheng Yu, Yan He, Yan Xu, Hong YangAbstract:Background Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation.
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the deubiquitinating enzyme otud1 antagonizes bh3 mimetic inhibitor induced cell death through regulating the stability of the mcl1 protein
Cancer Cell International, 2019Co-Authors: Yingying Lin, Jinan Feng, Xinrui Wang, Enrun Zheng, Wei Wang, Qiaofa Lin, Wanyan Shi, Zhenzhu Hou, Hanbin Lin, Hong YangAbstract:Myeloid cell leukaemia 1 (MCL1) is a pro-survival Bcl-2 family protein that plays important roles in cell survival, proliferation, differentiation and tumourigenesis. MCL1 is a fast-turnover protein that is degraded via an ubiquitination/proteasome-dependent mechanism. Although several E3 ligases have been discovered to promote the ubiquitination of MCL1, the deubiquitinating enzyme (DUB) that regulates its stability requires further investigation. The immunoprecipitation was used to determine the interaction between OTUD1 and MCL1. The ubiquitination assays was performed to determine the regulation of MCL1 by OTUD1. The cell viability was used to determine the regulation of BH3-mimetic inhibitor induced cell death by OTUD1. The survival analysis was used to determine the relationship between OTUD1 expression levels and the survival rate of cancer patients. By screening a DUB expression library, we determined that the deubiquitinating enzyme OTUD1 regulates MCL1 protein stability in an enzymatic-activity dependent manner. OTUD1 interacts with MCL1 and promotes its deubiquitination. Knockdown of OTUD1 increases the sensitivity of tumour cells to the BH3-mimetic inhibitor ABT-263, while overexpression of OTUD1 increases tumour cell tolerance of ABT-263. Furthermore, bioinformatics analysis data reveal that OTUD1 is a negative prognostic factor for liver cancer, ovarian cancer and specific subtypes of breast and cervical cancer. The deubiquitinating enzyme OTUD1 antagonizes BH3-mimetic inhibitor induced cell death through regulating the stability of the MCL1 protein. Thus, OTUD1 could be considered as a therapeutic target for curing these cancers.
